Structured Review

Millipore pgc 1α
Quercetin promoted translocation of <t>PGC‐1α</t> from cytoplasm to nucleus and enhanced PGC‐1α binding. ( A‐D ) The representative photomicrographs showing PGC‐1α immunohistochemistry of tissue from different group 24 hrs after TBI. ( E, H ) The nuclear PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( F, I ) The cytoplasmic protein PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( G, J ) The total protein PGC‐1α expression after melatonin treatment in mice with TBI, as measured by Western blot. Bars represent the mean ± S.E.M. * P
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Images

1) Product Images from "Neuroprotection by quercetin via mitochondrial function adaptation in traumatic brain injury: PGC‐1α pathway as a potential mechanism"

Article Title: Neuroprotection by quercetin via mitochondrial function adaptation in traumatic brain injury: PGC‐1α pathway as a potential mechanism

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.13313

Quercetin promoted translocation of PGC‐1α from cytoplasm to nucleus and enhanced PGC‐1α binding. ( A‐D ) The representative photomicrographs showing PGC‐1α immunohistochemistry of tissue from different group 24 hrs after TBI. ( E, H ) The nuclear PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( F, I ) The cytoplasmic protein PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( G, J ) The total protein PGC‐1α expression after melatonin treatment in mice with TBI, as measured by Western blot. Bars represent the mean ± S.E.M. * P
Figure Legend Snippet: Quercetin promoted translocation of PGC‐1α from cytoplasm to nucleus and enhanced PGC‐1α binding. ( A‐D ) The representative photomicrographs showing PGC‐1α immunohistochemistry of tissue from different group 24 hrs after TBI. ( E, H ) The nuclear PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( F, I ) The cytoplasmic protein PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( G, J ) The total protein PGC‐1α expression after melatonin treatment in mice with TBI, as measured by Western blot. Bars represent the mean ± S.E.M. * P

Techniques Used: Translocation Assay, Pyrolysis Gas Chromatography, Binding Assay, Immunohistochemistry, Expressing, Mouse Assay, Western Blot

2) Product Images from "PGC-1α and PGC-1β Increase Protein Synthesis via ERRα in C2C12 Myotubes"

Article Title: PGC-1α and PGC-1β Increase Protein Synthesis via ERRα in C2C12 Myotubes

Journal: Frontiers in Physiology

doi: 10.3389/fphys.2018.01336

Protein synthesis and myotube diameter in C2C12 myotubes infected with AdshERRα and PGC-1 adenoviruses. Myotubes were infected with either AdSUPER or AdshERRα for 24 h, followed by infection with GFP, PGC-1α, or PGC-1β for a further 48 h. (A) ERRα protein, normalized to GAPDH protein. n = 3–4 per group. (B) Protein synthesis, measured via [ 3 H]-tyrosine incorporation for 24 hours after infections. n = 6 per group, repeated in three experiments. (C) Average myotube diameter from 10 myotubes per visual field (10 visual fields for each group). (D) Representative images of GFP, PGC-1α, and PGC-1β infected myotubes, with AdSUPER or AdshERRα. ∗∗∗ P
Figure Legend Snippet: Protein synthesis and myotube diameter in C2C12 myotubes infected with AdshERRα and PGC-1 adenoviruses. Myotubes were infected with either AdSUPER or AdshERRα for 24 h, followed by infection with GFP, PGC-1α, or PGC-1β for a further 48 h. (A) ERRα protein, normalized to GAPDH protein. n = 3–4 per group. (B) Protein synthesis, measured via [ 3 H]-tyrosine incorporation for 24 hours after infections. n = 6 per group, repeated in three experiments. (C) Average myotube diameter from 10 myotubes per visual field (10 visual fields for each group). (D) Representative images of GFP, PGC-1α, and PGC-1β infected myotubes, with AdSUPER or AdshERRα. ∗∗∗ P

Techniques Used: Infection, Pyrolysis Gas Chromatography

mRNA expression of genes identified from the microarray based on their GO terms involved with protein synthesis, translation, and growth. Myotubes were infected with GFP, PGC-1α, or PGC-1β adenoviruses for 48 h, and samples were extracted after 72 h. mRNA of biasedly selected genes that were (A) upregulated and (B) downregulated in the microarray. mRNA expression of the genes selected unbiasedly from the microarray that were most significantly (C) upregulated and (D) downregulated. Values were normalized to 36B4 mRNA expression. n = 3, repeated in three experiments. ∗ P
Figure Legend Snippet: mRNA expression of genes identified from the microarray based on their GO terms involved with protein synthesis, translation, and growth. Myotubes were infected with GFP, PGC-1α, or PGC-1β adenoviruses for 48 h, and samples were extracted after 72 h. mRNA of biasedly selected genes that were (A) upregulated and (B) downregulated in the microarray. mRNA expression of the genes selected unbiasedly from the microarray that were most significantly (C) upregulated and (D) downregulated. Values were normalized to 36B4 mRNA expression. n = 3, repeated in three experiments. ∗ P

Techniques Used: Expressing, Microarray, Infection, Pyrolysis Gas Chromatography

Western blot analysis of Akt and p70S6k proteins in GFP, PGC-1α, and PGC-1β infected C2C12 myotubes. Myotubes were infected with GFP, PGC-1α, or PGC-1β adenoviruses for 48 h, and samples were extracted after 72 h. (A) Phospho-Akt (ser473), (B) total Akt protein, (C) phospho-p70S6k (thr389), and (D) total p70S6k protein expression. Samples were harvested after 72 h of infection. Bands were normalized to GAPDH protein. The same control images have been used for A , C , and B , D . n = 5 per group. ∗ P
Figure Legend Snippet: Western blot analysis of Akt and p70S6k proteins in GFP, PGC-1α, and PGC-1β infected C2C12 myotubes. Myotubes were infected with GFP, PGC-1α, or PGC-1β adenoviruses for 48 h, and samples were extracted after 72 h. (A) Phospho-Akt (ser473), (B) total Akt protein, (C) phospho-p70S6k (thr389), and (D) total p70S6k protein expression. Samples were harvested after 72 h of infection. Bands were normalized to GAPDH protein. The same control images have been used for A , C , and B , D . n = 5 per group. ∗ P

Techniques Used: Western Blot, Pyrolysis Gas Chromatography, Infection, Expressing

Western blot analysis of Akt and p70S6k proteins in C2C12 myotubes infected with AdshERRα and PGC-1 adenoviruses. Myotubes were infected with either AdSUPER or AdshERRα for 24 h, followed by infection with GFP, PGC-1α, or PGC-1β for a further 48 h. Samples were harvested after 96 h. (A) Phospho-Akt (ser473), (B) total Akt protein, (C) phospho-p70S6k (thr389), and (D) total p70S6k protein expression. Bands were normalized to GAPDH protein. The same control images have been used for A–C . n = 4 per group. ∗∗ P
Figure Legend Snippet: Western blot analysis of Akt and p70S6k proteins in C2C12 myotubes infected with AdshERRα and PGC-1 adenoviruses. Myotubes were infected with either AdSUPER or AdshERRα for 24 h, followed by infection with GFP, PGC-1α, or PGC-1β for a further 48 h. Samples were harvested after 96 h. (A) Phospho-Akt (ser473), (B) total Akt protein, (C) phospho-p70S6k (thr389), and (D) total p70S6k protein expression. Bands were normalized to GAPDH protein. The same control images have been used for A–C . n = 4 per group. ∗∗ P

Techniques Used: Western Blot, Infection, Pyrolysis Gas Chromatography, Expressing

Protein synthesis and myotube diameter in GFP, PGC-1α, and PGC-1β infected C2C12 myotubes. (A) PGC-1α and (B) PGC-1β protein 72 h after infection with GFP, PGC-1α, and PGC-1β adenoviruses. Bands were normalized to GAPDH protein; n = 4 per group. ∗∗∗ P
Figure Legend Snippet: Protein synthesis and myotube diameter in GFP, PGC-1α, and PGC-1β infected C2C12 myotubes. (A) PGC-1α and (B) PGC-1β protein 72 h after infection with GFP, PGC-1α, and PGC-1β adenoviruses. Bands were normalized to GAPDH protein; n = 4 per group. ∗∗∗ P

Techniques Used: Pyrolysis Gas Chromatography, Infection

Overview of the GSEA performed on genes commonly regulated by both PGC-1α and PGC-1β in C2C12 myotubes. Proportional representation of gene numbers significantly enriched in GO-related (A) biological processes, (B) cellular compartment, and (C) molecular functions with the number of genes indicated in brackets. The proportion of genes making up the specific sub-groups; CC GO term mitochondrial inner membrane, and MF GO terms translation elongation factor activity are also indicated.
Figure Legend Snippet: Overview of the GSEA performed on genes commonly regulated by both PGC-1α and PGC-1β in C2C12 myotubes. Proportional representation of gene numbers significantly enriched in GO-related (A) biological processes, (B) cellular compartment, and (C) molecular functions with the number of genes indicated in brackets. The proportion of genes making up the specific sub-groups; CC GO term mitochondrial inner membrane, and MF GO terms translation elongation factor activity are also indicated.

Techniques Used: Pyrolysis Gas Chromatography, Activity Assay

3) Product Images from "PGC-1? rescues Huntington's disease proteotoxicity by preventing oxidative stress and promoting TFEB function"

Article Title: PGC-1? rescues Huntington's disease proteotoxicity by preventing oxidative stress and promoting TFEB function

Journal: Science translational medicine

doi: 10.1126/scitranslmed.3003799

PGC-1α expression counters htt protein aggregate formation induced by oxidative stress
Figure Legend Snippet: PGC-1α expression counters htt protein aggregate formation induced by oxidative stress

Techniques Used: Pyrolysis Gas Chromatography, Expressing

PGC-1α promotes TFEB target gene induction and TFEB-mediated htt aggregate reduction
Figure Legend Snippet: PGC-1α promotes TFEB target gene induction and TFEB-mediated htt aggregate reduction

Techniques Used: Pyrolysis Gas Chromatography

PGC-1α expression prevents htt aggregate formation and rescues HD neurodegeneration
Figure Legend Snippet: PGC-1α expression prevents htt aggregate formation and rescues HD neurodegeneration

Techniques Used: Pyrolysis Gas Chromatography, Expressing

PGC-1α expression restores mitochondrial function in HD transgenic mice
Figure Legend Snippet: PGC-1α expression restores mitochondrial function in HD transgenic mice

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Transgenic Assay, Mouse Assay

PGC-1α expression protects against HD oxidative damage by inducing reactive oxygen species defense genes
Figure Legend Snippet: PGC-1α expression protects against HD oxidative damage by inducing reactive oxygen species defense genes

Techniques Used: Pyrolysis Gas Chromatography, Expressing

PolyQ-expanded htt interferes with PGC-1α transactivation of TFEB expression
Figure Legend Snippet: PolyQ-expanded htt interferes with PGC-1α transactivation of TFEB expression

Techniques Used: Pyrolysis Gas Chromatography, Expressing

PGC-1α expression rescues HD neurological phenotypes
Figure Legend Snippet: PGC-1α expression rescues HD neurological phenotypes

Techniques Used: Pyrolysis Gas Chromatography, Expressing

4) Product Images from "Accelerated recovery of renal mitochondrial and tubule homeostasis with SIRT1/PGC-1α activation following ischemia-reperfusion injury"

Article Title: Accelerated recovery of renal mitochondrial and tubule homeostasis with SIRT1/PGC-1α activation following ischemia-reperfusion injury

Journal: Toxicology and applied pharmacology

doi: 10.1016/j.taap.2013.09.026

SRT1720-induced deacetylation of PGC-1α after I/R
Figure Legend Snippet: SRT1720-induced deacetylation of PGC-1α after I/R

Techniques Used: Pyrolysis Gas Chromatography

5) Product Images from "PPAR-γ Coactivator-1α Regulates Progesterone Production in Ovarian Granulosa Cells with SF-1 and LRH-1"

Article Title: PPAR-γ Coactivator-1α Regulates Progesterone Production in Ovarian Granulosa Cells with SF-1 and LRH-1

Journal: Molecular Endocrinology

doi: 10.1210/me.2009-0352

A, PGC-1α was induced in UCB-MSCs. The mRNA levels of each gene in MSCs were analyzed by RT-PCR. B–E, The expression and localization of the NR5A protein family and PGC-1α in the murine ovary. B, The mRNA levels of each gene were analyzed by RT-PCR. Lanes O and L represent an ovary and a liver, respectively. C–E, Localization of NR5A and Pgc-1α proteins in the murine ovary. Positive staining for Pgc-1α (C) and Lrh-1 (D) in nuclei of granulosa cells, and Sf-1 (E) in nuclei of granulosa and theca/interstitial cells. Absence of any nuclear staining in a control section incubated with nonimmune IgG and counterstained with eosin (F).
Figure Legend Snippet: A, PGC-1α was induced in UCB-MSCs. The mRNA levels of each gene in MSCs were analyzed by RT-PCR. B–E, The expression and localization of the NR5A protein family and PGC-1α in the murine ovary. B, The mRNA levels of each gene were analyzed by RT-PCR. Lanes O and L represent an ovary and a liver, respectively. C–E, Localization of NR5A and Pgc-1α proteins in the murine ovary. Positive staining for Pgc-1α (C) and Lrh-1 (D) in nuclei of granulosa cells, and Sf-1 (E) in nuclei of granulosa and theca/interstitial cells. Absence of any nuclear staining in a control section incubated with nonimmune IgG and counterstained with eosin (F).

Techniques Used: Pyrolysis Gas Chromatography, Reverse Transcription Polymerase Chain Reaction, Expressing, Staining, Incubation

6) Product Images from "Fetal PGC-1? Overexpression Programs Adult Pancreatic ?-Cell Dysfunction"

Article Title: Fetal PGC-1? Overexpression Programs Adult Pancreatic ?-Cell Dysfunction

Journal: Diabetes

doi: 10.2337/db12-0314

PGC-1α overexpression during fetal life only is sufficient to impair β-cell function. A : β-Cell fraction was morphometrically measured on pancreatic sections from control (white bars) and Ins-PGC-1α (black bars) newborn mice. B : PGC-1α mRNA levels in pancreata of control (white bars) and Ins-PGC-1α (black bars) mice at postnatal day 1 (P1) and 21 (P21, left to right ) upon Dox treatment from birth. C : PGC-1α and β-cell genes mRNA levels in islets and β-cell mass of 4-month-old control (white bars) and Ins-PGC-1α (black bars) mice upon Dox treatment from birth. D : IpGTT performed on 4-month-old Ins-PGC-1α (black triangles) compared with control (white circles) mice under Dox treatment from birth. Inset shows the area under the curve for 0–120 min of plasma glucose of these mice. E : Serum insulin levels before and 15 min after intraperitoneal glucose injection in control (white bars) and Ins-PGC-1α (black bars) mice. F : β-Cell mass of control (white bars) and Ins-PGC-1α (black bars) mice. All values are means ± SD. * P
Figure Legend Snippet: PGC-1α overexpression during fetal life only is sufficient to impair β-cell function. A : β-Cell fraction was morphometrically measured on pancreatic sections from control (white bars) and Ins-PGC-1α (black bars) newborn mice. B : PGC-1α mRNA levels in pancreata of control (white bars) and Ins-PGC-1α (black bars) mice at postnatal day 1 (P1) and 21 (P21, left to right ) upon Dox treatment from birth. C : PGC-1α and β-cell genes mRNA levels in islets and β-cell mass of 4-month-old control (white bars) and Ins-PGC-1α (black bars) mice upon Dox treatment from birth. D : IpGTT performed on 4-month-old Ins-PGC-1α (black triangles) compared with control (white circles) mice under Dox treatment from birth. Inset shows the area under the curve for 0–120 min of plasma glucose of these mice. E : Serum insulin levels before and 15 min after intraperitoneal glucose injection in control (white bars) and Ins-PGC-1α (black bars) mice. F : β-Cell mass of control (white bars) and Ins-PGC-1α (black bars) mice. All values are means ± SD. * P

Techniques Used: Pyrolysis Gas Chromatography, Over Expression, Cell Function Assay, Mouse Assay, Injection

PGC-1α overexpression from adult age does not alter insulin secretion. A : PGC-1α expression in islets of 4-month-old control (white bars) and Ins-PGC-1α (black bars) mice after Dox treatment from conception. B : IpGTT performed on Ins-PGC-1α (black triangles) and control (white circles) mice. Inset shows the area under the curve for 0–120 min (AUC 0–120 min ) of plasma glucose of these mice. C : Serum insulin levels before and 15 min after intraperitoneal glucose in control (white bars) and Ins-PGC-1α (black bars) mice. D : PGC-1α expression in islets of control (white bars) and Ins-PGC-1α (black bars) mice 4 months after stopping Dox treatment. E and F : IpGTT and GSIS in Ins-PGC-1α (black triangles) and control (white circles) mice. Inset shows AUC 0–120 min of plasma glucose of these mice. G : Islet gene expression in islets of control (white bars) and Ins-PGC-1α (black bars) mice 4 months after stopping Dox treatment. All values are means ± SD. * P
Figure Legend Snippet: PGC-1α overexpression from adult age does not alter insulin secretion. A : PGC-1α expression in islets of 4-month-old control (white bars) and Ins-PGC-1α (black bars) mice after Dox treatment from conception. B : IpGTT performed on Ins-PGC-1α (black triangles) and control (white circles) mice. Inset shows the area under the curve for 0–120 min (AUC 0–120 min ) of plasma glucose of these mice. C : Serum insulin levels before and 15 min after intraperitoneal glucose in control (white bars) and Ins-PGC-1α (black bars) mice. D : PGC-1α expression in islets of control (white bars) and Ins-PGC-1α (black bars) mice 4 months after stopping Dox treatment. E and F : IpGTT and GSIS in Ins-PGC-1α (black triangles) and control (white circles) mice. Inset shows AUC 0–120 min of plasma glucose of these mice. G : Islet gene expression in islets of control (white bars) and Ins-PGC-1α (black bars) mice 4 months after stopping Dox treatment. All values are means ± SD. * P

Techniques Used: Pyrolysis Gas Chromatography, Over Expression, Expressing, Mouse Assay

PGC-1α inhibits Pdx1 expression through interaction with the GR. A : Gene expression in Min6 cells infected with adenoviruses expressing only the green fluorescent protein (GFP, white bars) or expressing PGC-1α and GFP (black bars). Gene expression was measured in Min6 cells by real-time PCR 24 h after infection and normalized to Min6 cells infected with adenovirus expressing GFP. B : Pdx1 expression in isolated islets from control mice (GR lox/lox ) and mice lacking the GR in mature β-cells (GR RipCre ) were infected with adenoviruses expressing GFP (white bars) or PGC-1α and GFP (black bars). C : ChIP of areas I, II, and III of the Pdx1 promoter with an anti-GR or an anti–PGC-1α antibody. Agarose gels showing (from left to right): molecular weight markers, positive control, input (DNA without IP), IP with anti-GR antibody, IP with anti–PGC-1α antibody, and IP with anti-IgG. Right panel shows sequential IP with first anti-GR antibody, then with anti-PGC-1α or anti-GR antibody. Lines 1 , 2 , and 3 show typical results obtained with primers located in area III, II, and I, respectively. Results are means ± SD on n = 4 independent experiments. * P
Figure Legend Snippet: PGC-1α inhibits Pdx1 expression through interaction with the GR. A : Gene expression in Min6 cells infected with adenoviruses expressing only the green fluorescent protein (GFP, white bars) or expressing PGC-1α and GFP (black bars). Gene expression was measured in Min6 cells by real-time PCR 24 h after infection and normalized to Min6 cells infected with adenovirus expressing GFP. B : Pdx1 expression in isolated islets from control mice (GR lox/lox ) and mice lacking the GR in mature β-cells (GR RipCre ) were infected with adenoviruses expressing GFP (white bars) or PGC-1α and GFP (black bars). C : ChIP of areas I, II, and III of the Pdx1 promoter with an anti-GR or an anti–PGC-1α antibody. Agarose gels showing (from left to right): molecular weight markers, positive control, input (DNA without IP), IP with anti-GR antibody, IP with anti–PGC-1α antibody, and IP with anti-IgG. Right panel shows sequential IP with first anti-GR antibody, then with anti-PGC-1α or anti-GR antibody. Lines 1 , 2 , and 3 show typical results obtained with primers located in area III, II, and I, respectively. Results are means ± SD on n = 4 independent experiments. * P

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Infection, Real-time Polymerase Chain Reaction, Isolation, Mouse Assay, Chromatin Immunoprecipitation, Molecular Weight, Positive Control

GCs stimulate PGC-1α and inhibit Pdx1 in β-cells. A : PGC-1α expression in fetal pancreata at 18.5 days of pregnancy (E18.5) in control (C, white bars) or GCs overexposure conditions induced by maternal under nutrition (UN, black bars), in mouse islets, Min6 cells, and fetal rat islets cultured in control conditions (C, white bars) or treated with Dex (black bars) for 24 h. B : PGC-1α protein levels in mouse islets cultured in control conditions (C, white bar) or treated with Dex (black bar). C : Gene expression in Min6 cells cultured in control (white bars) or Dex-treated (black bars) conditions for 24 h. Time course effect of Dex on PGC-1α ( D ) and Pdx1 ( E ) expression measured after 1, 3, 6, and 16 h in control (white bars) or Dex-treated (black bars) Min6 cells. Results are expressed as means ± SD for n = 4 independent experiments. * P
Figure Legend Snippet: GCs stimulate PGC-1α and inhibit Pdx1 in β-cells. A : PGC-1α expression in fetal pancreata at 18.5 days of pregnancy (E18.5) in control (C, white bars) or GCs overexposure conditions induced by maternal under nutrition (UN, black bars), in mouse islets, Min6 cells, and fetal rat islets cultured in control conditions (C, white bars) or treated with Dex (black bars) for 24 h. B : PGC-1α protein levels in mouse islets cultured in control conditions (C, white bar) or treated with Dex (black bar). C : Gene expression in Min6 cells cultured in control (white bars) or Dex-treated (black bars) conditions for 24 h. Time course effect of Dex on PGC-1α ( D ) and Pdx1 ( E ) expression measured after 1, 3, 6, and 16 h in control (white bars) or Dex-treated (black bars) Min6 cells. Results are expressed as means ± SD for n = 4 independent experiments. * P

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Cell Culture

PGC-1α overexpression in β-cells impairs glucose tolerance. PGC-1α mRNA ( A ) and protein levels ( B ) in islets from control mice (white bars) and Ins-PGC-1α mice (black bars). C : The ipGTT of Ins-PGC-1α (black triangles) is compared with control mice (white circles). The inset shows the area under the curve from 0 to 120 min of plasma glucose of these mice. D : Serum insulin levels before and 15 min after glucose injection in control (white bars) and Ins-PGC-1α (black bars) mice. E : Insulin tolerance test was performed in Ins-PGC-1α (black triangles) and control (white circles) mice. All values are means ± SD. * P
Figure Legend Snippet: PGC-1α overexpression in β-cells impairs glucose tolerance. PGC-1α mRNA ( A ) and protein levels ( B ) in islets from control mice (white bars) and Ins-PGC-1α mice (black bars). C : The ipGTT of Ins-PGC-1α (black triangles) is compared with control mice (white circles). The inset shows the area under the curve from 0 to 120 min of plasma glucose of these mice. D : Serum insulin levels before and 15 min after glucose injection in control (white bars) and Ins-PGC-1α (black bars) mice. E : Insulin tolerance test was performed in Ins-PGC-1α (black triangles) and control (white circles) mice. All values are means ± SD. * P

Techniques Used: Pyrolysis Gas Chromatography, Over Expression, Mouse Assay, Injection

Impaired β-cell gene expression and mass in Ins-PGC-1α mice. A : Gene expression in islets from control (white bars) and Ins-PGC-1α (black bars) mice. Morphometric analysis of control (white bars) and Ins-PGC-1α (black bars) mice: β-cell fraction ( B ), absolute β-cell mass ( C ), and β-cell mass relative to body weight ( D ). E : Pancreatic insulin content from Ins-PGC-1α vs. control mice. Number of islets per cm 2 ( F ) and mean islet size in Ins-PGC-1α and control mice ( G ). H : Individual β-cell size was morphometrically quantified in control (white bars) and Ins-PGC-1α (black bars) mice and illustrated by immunofluorescent staining for E-cadherin. Scale bar is 50 µm for upper panels and 25 µm for lower panels. Results are expressed as means ± SD. * P
Figure Legend Snippet: Impaired β-cell gene expression and mass in Ins-PGC-1α mice. A : Gene expression in islets from control (white bars) and Ins-PGC-1α (black bars) mice. Morphometric analysis of control (white bars) and Ins-PGC-1α (black bars) mice: β-cell fraction ( B ), absolute β-cell mass ( C ), and β-cell mass relative to body weight ( D ). E : Pancreatic insulin content from Ins-PGC-1α vs. control mice. Number of islets per cm 2 ( F ) and mean islet size in Ins-PGC-1α and control mice ( G ). H : Individual β-cell size was morphometrically quantified in control (white bars) and Ins-PGC-1α (black bars) mice and illustrated by immunofluorescent staining for E-cadherin. Scale bar is 50 µm for upper panels and 25 µm for lower panels. Results are expressed as means ± SD. * P

Techniques Used: Expressing, Pyrolysis Gas Chromatography, Mouse Assay, Staining

7) Product Images from "Peroxisome proliferator‐activated receptor‐γ coactivator 1 α1 induces a cardiac excitation–contraction coupling phenotype without metabolic remodelling"

Article Title: Peroxisome proliferator‐activated receptor‐γ coactivator 1 α1 induces a cardiac excitation–contraction coupling phenotype without metabolic remodelling

Journal: The Journal of Physiology

doi: 10.1113/JP272847

Acute PGC‐1α1 expression and dose dependence in cardiomyocytes A , representative immunoblot of protein (top panel) and bar graph of mRNA expression (lower panel) in neonatal cardiomyocytes after PGC‐1α1 overexpression by adenoviral transduction with multiplicity of infection (MOI) 1–30 ( n ≥ 8). B–D , acute PGC‐1α1 mRNA expression in neonatal cardiomyocytes by adenoviral transduction with multiplicity of infection (MOI) 1–10. B , correlation and slope between PGC‐1α expression levels and gene expression of indicated genes. Statistically significant correlation at over 33%. C , scatter plot of selected target genes with correlation ( r ) more than 70% with each square representing an individual sample ( n = 36). D , scatter plot showing the response of selected target gene expression to PGC‐1α levels with each dot representing the average from a group of samples ( n ≥ 8). mRNA expression levels were normalized to B2M and presented here as fold changes relative to expression level in Ad‐CMV transduced cells (= 1, dotted line in C ). 1/2 max (red), a half‐maximal response. mRNA data were obtained from qRT‐PCR analyses. * P
Figure Legend Snippet: Acute PGC‐1α1 expression and dose dependence in cardiomyocytes A , representative immunoblot of protein (top panel) and bar graph of mRNA expression (lower panel) in neonatal cardiomyocytes after PGC‐1α1 overexpression by adenoviral transduction with multiplicity of infection (MOI) 1–30 ( n ≥ 8). B–D , acute PGC‐1α1 mRNA expression in neonatal cardiomyocytes by adenoviral transduction with multiplicity of infection (MOI) 1–10. B , correlation and slope between PGC‐1α expression levels and gene expression of indicated genes. Statistically significant correlation at over 33%. C , scatter plot of selected target genes with correlation ( r ) more than 70% with each square representing an individual sample ( n = 36). D , scatter plot showing the response of selected target gene expression to PGC‐1α levels with each dot representing the average from a group of samples ( n ≥ 8). mRNA expression levels were normalized to B2M and presented here as fold changes relative to expression level in Ad‐CMV transduced cells (= 1, dotted line in C ). 1/2 max (red), a half‐maximal response. mRNA data were obtained from qRT‐PCR analyses. * P

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Over Expression, Transduction, Infection, Quantitative RT-PCR

8) Product Images from "Repeated transient mRNA bursts precede increases in transcriptional and mitochondrial proteins during training in human skeletal muscle"

Article Title: Repeated transient mRNA bursts precede increases in transcriptional and mitochondrial proteins during training in human skeletal muscle

Journal: The Journal of Physiology

doi: 10.1113/jphysiol.2010.199448

Representative figure demonstrating temporal responses and relationship of PGC-1α mRNA, PGC-1α protein and CS maximal activity throughout 2 weeks of high-intensity interval training
Figure Legend Snippet: Representative figure demonstrating temporal responses and relationship of PGC-1α mRNA, PGC-1α protein and CS maximal activity throughout 2 weeks of high-intensity interval training

Techniques Used: Pyrolysis Gas Chromatography, Activity Assay

Skeletal muscle PGC-1α and PGC-1β mRNA ( A and B ) and protein content ( C and D ) throughout 2 weeks of high-intensity interval training
Figure Legend Snippet: Skeletal muscle PGC-1α and PGC-1β mRNA ( A and B ) and protein content ( C and D ) throughout 2 weeks of high-intensity interval training

Techniques Used: Pyrolysis Gas Chromatography

9) Product Images from "Enhanced longevity and metabolism by brown adipose tissue with disruption of the regulator of G protein signaling 14, et al. Enhanced longevity and metabolism by brown adipose tissue with disruption of the regulator of G protein signaling 14"

Article Title: Enhanced longevity and metabolism by brown adipose tissue with disruption of the regulator of G protein signaling 14, et al. Enhanced longevity and metabolism by brown adipose tissue with disruption of the regulator of G protein signaling 14

Journal: Aging Cell

doi: 10.1111/acel.12751

BAT mediates energy metabolism. (a) Oxidative phosphorylation (OXPHOS) capacity was increased in BAT from RGS14 KO vs. BAT from WT as reflected by increased CIL: Complex I leak respiration; CIP: OXPHOS capacity of Complex I; CI CIIP: OXPHOS capacity of Complex I II; and CIP: OXPHOS capacity of Complex II. (b) PGC‐1α, a key regulator of mitochondrial biogenesis, was increased at the protein level in the BAT of the RGS14 KO mice ( n = 3/group). (c) SIRT3 protein levels were increased in BAT of RGS14 KO mice ( n = 3/group). (d) Increased mitochondrial DNA/nuclear DNA ratio was found in BAT of RGS14 KO ( n = 5/group). The data comparing BAT transplants and recipients are shown and demonstrate that WT BAT recipients gained the protective features of RGS14 KO and RGS14 KO lost these protective features (e–g). (e) Oxygen consumption was increased in BAT recipients compared to BAT donors ( n = 4/group). (f) Thermogenic protection was lost in BAT donors and gained in BAT recipients ( n = 10/group). (g) The area above the curve was significantly greater in BAT recipients than in BAT donors. Results are expressed as mean ± SEM . Statistical significance was determined by the use of a Student's t test. * p
Figure Legend Snippet: BAT mediates energy metabolism. (a) Oxidative phosphorylation (OXPHOS) capacity was increased in BAT from RGS14 KO vs. BAT from WT as reflected by increased CIL: Complex I leak respiration; CIP: OXPHOS capacity of Complex I; CI CIIP: OXPHOS capacity of Complex I II; and CIP: OXPHOS capacity of Complex II. (b) PGC‐1α, a key regulator of mitochondrial biogenesis, was increased at the protein level in the BAT of the RGS14 KO mice ( n = 3/group). (c) SIRT3 protein levels were increased in BAT of RGS14 KO mice ( n = 3/group). (d) Increased mitochondrial DNA/nuclear DNA ratio was found in BAT of RGS14 KO ( n = 5/group). The data comparing BAT transplants and recipients are shown and demonstrate that WT BAT recipients gained the protective features of RGS14 KO and RGS14 KO lost these protective features (e–g). (e) Oxygen consumption was increased in BAT recipients compared to BAT donors ( n = 4/group). (f) Thermogenic protection was lost in BAT donors and gained in BAT recipients ( n = 10/group). (g) The area above the curve was significantly greater in BAT recipients than in BAT donors. Results are expressed as mean ± SEM . Statistical significance was determined by the use of a Student's t test. * p

Techniques Used: Pyrolysis Gas Chromatography, Mouse Assay

Increased NAD + /NADH ratio in RGS14 KO in skeletal muscle. (a) Both the absolute level of NAD + and NAD + /NADH ratio were elevated in the RGS14 KO mice ( n = 4/group). (b) CD38, a mechanism for changes in NAD + , was reduced in RGS14 KO skeletal muscle, further confirmed in the increased NAD + level ( n = 6–7/group). (c) Increase in mitochondrial DNA content in skeletal muscle was measured by mitochondrial DNA/nuclear DNA ratio ( n = 5/group). (d) Complex I activity in skeletal muscle was significantly increased in RGS14 KO animals ( n = 7/group). (e) PGC‐1α, a key regulator of mitochondrial biogenesis, was increased at the protein level in the BAT of the RGS14 KO mice ( n = 3/group). Results are expressed as mean ± SEM . Statistical significance was determined by Student's t test * p
Figure Legend Snippet: Increased NAD + /NADH ratio in RGS14 KO in skeletal muscle. (a) Both the absolute level of NAD + and NAD + /NADH ratio were elevated in the RGS14 KO mice ( n = 4/group). (b) CD38, a mechanism for changes in NAD + , was reduced in RGS14 KO skeletal muscle, further confirmed in the increased NAD + level ( n = 6–7/group). (c) Increase in mitochondrial DNA content in skeletal muscle was measured by mitochondrial DNA/nuclear DNA ratio ( n = 5/group). (d) Complex I activity in skeletal muscle was significantly increased in RGS14 KO animals ( n = 7/group). (e) PGC‐1α, a key regulator of mitochondrial biogenesis, was increased at the protein level in the BAT of the RGS14 KO mice ( n = 3/group). Results are expressed as mean ± SEM . Statistical significance was determined by Student's t test * p

Techniques Used: Mouse Assay, Activity Assay, Pyrolysis Gas Chromatography

10) Product Images from "Cell Density and Joint microRNA-133a and microRNA-696 Inhibition Enhance Differentiation and Contractile Function of Engineered Human Skeletal Muscle Tissues"

Article Title: Cell Density and Joint microRNA-133a and microRNA-696 Inhibition Enhance Differentiation and Contractile Function of Engineered Human Skeletal Muscle Tissues

Journal: Tissue Engineering. Part A

doi: 10.1089/ten.tea.2015.0359

PGC-1α (A) , HIF-2α (B) , and COXII (C) mRNA expression of 3D-engineered human skeletal muscle myobundles 2 weeks after addition of DM. Expression was normalized to GAPDH and reference total mouse embryo RNA. Myobundles prepared from HSkM
Figure Legend Snippet: PGC-1α (A) , HIF-2α (B) , and COXII (C) mRNA expression of 3D-engineered human skeletal muscle myobundles 2 weeks after addition of DM. Expression was normalized to GAPDH and reference total mouse embryo RNA. Myobundles prepared from HSkM

Techniques Used: Pyrolysis Gas Chromatography, Expressing

11) Product Images from "Dysregulation of Mitochondrial Quality Control Processes Contribute to Sarcopenia in a Mouse Model of Premature Aging"

Article Title: Dysregulation of Mitochondrial Quality Control Processes Contribute to Sarcopenia in a Mouse Model of Premature Aging

Journal: PLoS ONE

doi: 10.1371/journal.pone.0069327

PolG mice display higher levels of mitochondrial regulatory proteins and transcription factors. AMPKα activation ( A ), PGC-1α ( B ), NRF-1 ( C ), and Tfam ( D ) were determined by Western Blotting in muscle from young (3–6 mo) and older (8–15 mo) WT and PolG animals. AMPKα activation is determined by phosphorylated AMPKα over total AMPKα. Representative blots are shown above with a graphical summary of the data below (n = 7–13). Significance was set at P
Figure Legend Snippet: PolG mice display higher levels of mitochondrial regulatory proteins and transcription factors. AMPKα activation ( A ), PGC-1α ( B ), NRF-1 ( C ), and Tfam ( D ) were determined by Western Blotting in muscle from young (3–6 mo) and older (8–15 mo) WT and PolG animals. AMPKα activation is determined by phosphorylated AMPKα over total AMPKα. Representative blots are shown above with a graphical summary of the data below (n = 7–13). Significance was set at P

Techniques Used: Mouse Assay, Activation Assay, Pyrolysis Gas Chromatography, Western Blot

12) Product Images from "Voluntary Running Aids to Maintain High Body Temperature in Rats Bred for High Aerobic Capacity"

Article Title: Voluntary Running Aids to Maintain High Body Temperature in Rats Bred for High Aerobic Capacity

Journal: Frontiers in Physiology

doi: 10.3389/fphys.2016.00311

Western blot analyses from gastrocnemius muscle . HCRs had higher UCP2, PGC-1α, cyt c, and OXPHOS protein levels (line effect p
Figure Legend Snippet: Western blot analyses from gastrocnemius muscle . HCRs had higher UCP2, PGC-1α, cyt c, and OXPHOS protein levels (line effect p

Techniques Used: Western Blot, Pyrolysis Gas Chromatography

13) Product Images from "Maternal Obesity during Gestation Impairs Fatty Acid Oxidation and Mitochondrial SIRT3 Expression in Rat Offspring at Weaning"

Article Title: Maternal Obesity during Gestation Impairs Fatty Acid Oxidation and Mitochondrial SIRT3 Expression in Rat Offspring at Weaning

Journal: PLoS ONE

doi: 10.1371/journal.pone.0024068

Fasting-induced changes in SIRT3 and PGC-1α mRNA and protein expression of lean and obese dam offspring. ( A ) SIRT3 mRNA expression, ( B ) SIRT3 mitochondrial protein content, and ( C ) PGC-1α mRNA expression in liver from fed and fasted offspring of lean and obese dams at PND 21 (N = 8–15 per group). Representative blot is also shown in FIG 5B for SIRT3 protein content (N = 4 per group). Values are expressed as means±SE, different letter superscripts indicate statistical significance (p
Figure Legend Snippet: Fasting-induced changes in SIRT3 and PGC-1α mRNA and protein expression of lean and obese dam offspring. ( A ) SIRT3 mRNA expression, ( B ) SIRT3 mitochondrial protein content, and ( C ) PGC-1α mRNA expression in liver from fed and fasted offspring of lean and obese dams at PND 21 (N = 8–15 per group). Representative blot is also shown in FIG 5B for SIRT3 protein content (N = 4 per group). Values are expressed as means±SE, different letter superscripts indicate statistical significance (p

Techniques Used: Pyrolysis Gas Chromatography, Expressing

14) Product Images from "Sex differences in mitochondrial respiratory function in human skeletal muscle"

Article Title: Sex differences in mitochondrial respiratory function in human skeletal muscle

Journal: American Journal of Physiology - Regulatory, Integrative and Comparative Physiology

doi: 10.1152/ajpregu.00025.2018

Maximal mitochondrial respiration and markers of mitochondrial content. Rates of oxygen consumption (JO 2 ; A ) in permeabilized muscle fibers were determined in men and women with the sequential addition of pyruvate+malate (PM, Complex I), ADP (PMD), glutamate (PMDG, maximal Complex I), and succinate (PMDGS, Complex I+II). Respiratory control ratio (RCR) is complex I respiration in the presence and absence of ADP. B : Western blots were used to estimate the abundance of mitochondrial proteins, as well as proteins involved in regulating mitochondrial biogenesis. GCN5, histone acetyltransferase-5; PDHE1α, pyruvate-dehydrogenase-subunit E1α; PDK4, pyruvate dehydrogenase kinase-4; PGC-1α, peroxisome proliferator-activated receptor γ-coactivator 1-α; PGC-1β, peroxisome proliferator-activated receptor-γ coactivator 1-β; SIRT1, sirtuin-1. C denotes the complex of various subunits of the electron transport chain (CI, CII, CIII, and CV). *Significant difference between men and women ( P
Figure Legend Snippet: Maximal mitochondrial respiration and markers of mitochondrial content. Rates of oxygen consumption (JO 2 ; A ) in permeabilized muscle fibers were determined in men and women with the sequential addition of pyruvate+malate (PM, Complex I), ADP (PMD), glutamate (PMDG, maximal Complex I), and succinate (PMDGS, Complex I+II). Respiratory control ratio (RCR) is complex I respiration in the presence and absence of ADP. B : Western blots were used to estimate the abundance of mitochondrial proteins, as well as proteins involved in regulating mitochondrial biogenesis. GCN5, histone acetyltransferase-5; PDHE1α, pyruvate-dehydrogenase-subunit E1α; PDK4, pyruvate dehydrogenase kinase-4; PGC-1α, peroxisome proliferator-activated receptor γ-coactivator 1-α; PGC-1β, peroxisome proliferator-activated receptor-γ coactivator 1-β; SIRT1, sirtuin-1. C denotes the complex of various subunits of the electron transport chain (CI, CII, CIII, and CV). *Significant difference between men and women ( P

Techniques Used: Western Blot, Pyrolysis Gas Chromatography

15) Product Images from "Supplementation with ?-Lipoic Acid, CoQ10, and Vitamin E Augments Running Performance and Mitochondrial Function in Female Mice"

Article Title: Supplementation with ?-Lipoic Acid, CoQ10, and Vitamin E Augments Running Performance and Mitochondrial Function in Female Mice

Journal: PLoS ONE

doi: 10.1371/journal.pone.0060722

Expression of mitochondrial proteins and PGC-1α. Expression of mitochondrial proteins and PGC-1α were determined using Western blotting on protein homogenates prepared from tibialis anterior muscle tissue (n = 4–6 mice/gender/group). Data are means ± SEM and representative bands from each gender and group are shown. φ indicates main effect of training, p≤0.05, and post-hoc testing was used to compare antioxidant- and placebo-supplemented groups, * indicates p≤0.05.
Figure Legend Snippet: Expression of mitochondrial proteins and PGC-1α. Expression of mitochondrial proteins and PGC-1α were determined using Western blotting on protein homogenates prepared from tibialis anterior muscle tissue (n = 4–6 mice/gender/group). Data are means ± SEM and representative bands from each gender and group are shown. φ indicates main effect of training, p≤0.05, and post-hoc testing was used to compare antioxidant- and placebo-supplemented groups, * indicates p≤0.05.

Techniques Used: Expressing, Pyrolysis Gas Chromatography, Western Blot, Mouse Assay

16) Product Images from "Selenium preserves mitochondrial function, stimulates mitochondrial biogenesis, and reduces infarct volume after focal cerebral ischemia"

Article Title: Selenium preserves mitochondrial function, stimulates mitochondrial biogenesis, and reduces infarct volume after focal cerebral ischemia

Journal: BMC Neuroscience

doi: 10.1186/1471-2202-13-79

Selenium pretreatment increases protein levels of mitochondrial biogenesis markers, PGC-1α and NRF1. Representative Western blot and analysis of PGC-1α and NRF1 in control, 5- and 24 h of recirculation in saline and selenium pretreated groups (n = 4 each group). The results were normalized as relative % of control set at 100%. Data represents mean ± SD. *p
Figure Legend Snippet: Selenium pretreatment increases protein levels of mitochondrial biogenesis markers, PGC-1α and NRF1. Representative Western blot and analysis of PGC-1α and NRF1 in control, 5- and 24 h of recirculation in saline and selenium pretreated groups (n = 4 each group). The results were normalized as relative % of control set at 100%. Data represents mean ± SD. *p

Techniques Used: Pyrolysis Gas Chromatography, Western Blot

17) Product Images from "A dual agonist of farnesoid X receptor (FXR) and the G protein–coupled receptor TGR5, INT-767, reverses age-related kidney disease in mice"

Article Title: A dual agonist of farnesoid X receptor (FXR) and the G protein–coupled receptor TGR5, INT-767, reverses age-related kidney disease in mice

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.C117.794982

INT-767 treatment increases mitochondrial biogenesis and function. A , INT-767 increases the mitochondrial to nuclear DNA ratio and mRNA level of NRF1 in aging kidneys. B , INT-767 treatment increases the activated AMPK level and prevents the age-related decreases in SIRT1 mRNA and nuclear hormone receptor ERR-α mRNA. C , INT-767 prevents the age-related decrease in PGC-1α mRNA and protein; mitochondrial SIRT3 mRNA and protein; and its target, MCAD protein. D , INT-767 reverses the age-related increase in the acetylated form of mitochondrial isocitrate dehydrogenase as shown in the Western blot. 2-month INT-767 treatment also reverses the decreased mitochondrial complex I and complex IV activity in aged kidneys. Error bars represent S.D. n = 6 mice. *, p
Figure Legend Snippet: INT-767 treatment increases mitochondrial biogenesis and function. A , INT-767 increases the mitochondrial to nuclear DNA ratio and mRNA level of NRF1 in aging kidneys. B , INT-767 treatment increases the activated AMPK level and prevents the age-related decreases in SIRT1 mRNA and nuclear hormone receptor ERR-α mRNA. C , INT-767 prevents the age-related decrease in PGC-1α mRNA and protein; mitochondrial SIRT3 mRNA and protein; and its target, MCAD protein. D , INT-767 reverses the age-related increase in the acetylated form of mitochondrial isocitrate dehydrogenase as shown in the Western blot. 2-month INT-767 treatment also reverses the decreased mitochondrial complex I and complex IV activity in aged kidneys. Error bars represent S.D. n = 6 mice. *, p

Techniques Used: Pyrolysis Gas Chromatography, Western Blot, Activity Assay, Mouse Assay

18) Product Images from "A metabolic switch toward lipid use in glycolytic muscle is an early pathologic event in a mouse model of amyotrophic lateral sclerosis"

Article Title: A metabolic switch toward lipid use in glycolytic muscle is an early pathologic event in a mouse model of amyotrophic lateral sclerosis

Journal: EMBO Molecular Medicine

doi: 10.15252/emmm.201404433

DCA treatment had beneficial effects on metabolism and mitochondrial function of SOD1 G86R mice A–I Relative mRNA levels of (A) Pdk4 , (B) Pparβ/δ , (C) Foxo1 , (D) Pfk1 , (E) Acsf2, (F) citrate synthase , (G) PGC-1α , (H) Mfn2, and (I) Gpx1 were evaluated by qPCR in tibialis anterior of control (CT) or DCA-treated (DCA) WT and SOD1 G86R mice. Graphs represent mean fold change ± SEM from CT WT group. P -values versus WT: Pdk4 *** P = 0.002 and ## P = 0.0039, Pparβ/δ # P = 0.0178, Foxo1 ** P = 0.0033 and ## P = 0.0038, Pfk1 *** P = 0.0002 and ## P = 0.0080, Acsf2 * P = 0.0437, citrate synthase ### P = 0.0004, Pgc-1α ** P = 0.0084 and ### P = 0.0009, Mfn2 * P = 0.0272, $ P = 0.0145 and ### P = 0.0002 and Gpx1 *** P
Figure Legend Snippet: DCA treatment had beneficial effects on metabolism and mitochondrial function of SOD1 G86R mice A–I Relative mRNA levels of (A) Pdk4 , (B) Pparβ/δ , (C) Foxo1 , (D) Pfk1 , (E) Acsf2, (F) citrate synthase , (G) PGC-1α , (H) Mfn2, and (I) Gpx1 were evaluated by qPCR in tibialis anterior of control (CT) or DCA-treated (DCA) WT and SOD1 G86R mice. Graphs represent mean fold change ± SEM from CT WT group. P -values versus WT: Pdk4 *** P = 0.002 and ## P = 0.0039, Pparβ/δ # P = 0.0178, Foxo1 ** P = 0.0033 and ## P = 0.0038, Pfk1 *** P = 0.0002 and ## P = 0.0080, Acsf2 * P = 0.0437, citrate synthase ### P = 0.0004, Pgc-1α ** P = 0.0084 and ### P = 0.0009, Mfn2 * P = 0.0272, $ P = 0.0145 and ### P = 0.0002 and Gpx1 *** P

Techniques Used: Mouse Assay, Pyrolysis Gas Chromatography, Real-time Polymerase Chain Reaction

Transcription factors, PGC-1α, and citrate synthase are differentially regulated in SOD1 G86R mice A–D Relative mRNA levels of (A) Pparß/δ , (B) Foxo1 , (C) citrate synthase , and (D) Pgc-1α were evaluated by qPCR at the indicated ages in tibialis anterior of WT and SOD1 G86R mice. Graphs represent mean fold change ± SEM from age-matched WT. P -values versus WT: Pparβ/δ ** P = 0.0016 at 65 days; Foxo1 *** P = 0.0001 at 105 days, citrate synthase *** P
Figure Legend Snippet: Transcription factors, PGC-1α, and citrate synthase are differentially regulated in SOD1 G86R mice A–D Relative mRNA levels of (A) Pparß/δ , (B) Foxo1 , (C) citrate synthase , and (D) Pgc-1α were evaluated by qPCR at the indicated ages in tibialis anterior of WT and SOD1 G86R mice. Graphs represent mean fold change ± SEM from age-matched WT. P -values versus WT: Pparβ/δ ** P = 0.0016 at 65 days; Foxo1 *** P = 0.0001 at 105 days, citrate synthase *** P

Techniques Used: Pyrolysis Gas Chromatography, Mouse Assay, Real-time Polymerase Chain Reaction

19) Product Images from "Impaired Mitochondrial Biogenesis Contributes to Mitochondrial Dysfunction in Alzheimer's Disease"

Article Title: Impaired Mitochondrial Biogenesis Contributes to Mitochondrial Dysfunction in Alzheimer's Disease

Journal: Journal of Neurochemistry

doi: 10.1111/j.1471-4159.2011.07581.x

Transfection with miR RNAi of PGC-1α exacerbated the impaired mitochondrial biogenesis in APPswe cells. A) Representative immunoblotting and quantification analysis showed that the expression of PGC-1α significantly reduced after transient
Figure Legend Snippet: Transfection with miR RNAi of PGC-1α exacerbated the impaired mitochondrial biogenesis in APPswe cells. A) Representative immunoblotting and quantification analysis showed that the expression of PGC-1α significantly reduced after transient

Techniques Used: Transfection, Pyrolysis Gas Chromatography, Expressing

Downregulation of PGC-1α led to reduced mitochondrial biogenesis proteins and mitochondrial content in M17 cells. A) Representative immunoblot results of PGC-1α expression in PGC-1α Knockdown mixed clone (KDm), single clone4 (KD4)
Figure Legend Snippet: Downregulation of PGC-1α led to reduced mitochondrial biogenesis proteins and mitochondrial content in M17 cells. A) Representative immunoblot results of PGC-1α expression in PGC-1α Knockdown mixed clone (KDm), single clone4 (KD4)

Techniques Used: Pyrolysis Gas Chromatography, Expressing

The expression of human APP swedish mutation caused reduced expression of mitochondrial biogenesis proteins and reduced mitochondrial content. A) Immunoblot and quantification analysis revealed that the nuclear levels of PGC-1α were significantly
Figure Legend Snippet: The expression of human APP swedish mutation caused reduced expression of mitochondrial biogenesis proteins and reduced mitochondrial content. A) Immunoblot and quantification analysis revealed that the nuclear levels of PGC-1α were significantly

Techniques Used: Expressing, Mutagenesis, Pyrolysis Gas Chromatography

Overexpression of PGC-1α could rescue the impaired mitochondrial biogenesis signal in APPswe cells. A) Representative immunoblot and quantification analysis showed that the expression of PGC-1α increased significantly after transient transfection
Figure Legend Snippet: Overexpression of PGC-1α could rescue the impaired mitochondrial biogenesis signal in APPswe cells. A) Representative immunoblot and quantification analysis showed that the expression of PGC-1α increased significantly after transient transfection

Techniques Used: Over Expression, Pyrolysis Gas Chromatography, Expressing, Transfection

PKA/CREB pathway played a critical role in the reduced expression of PGC-1α in APPswe cells. A) Immunoblotting and quantification analysis revealed that the level of p-CREB was significantly reduced in APPswe cells ( Δ p
Figure Legend Snippet: PKA/CREB pathway played a critical role in the reduced expression of PGC-1α in APPswe cells. A) Immunoblotting and quantification analysis revealed that the level of p-CREB was significantly reduced in APPswe cells ( Δ p

Techniques Used: Expressing, Pyrolysis Gas Chromatography

Mitochondrial biogenesis proteins were reduced in AD hippocampus. A) Immunoblot and quantification analysis revealed that total protein levels of PGC-1α were significantly reduced in AD hippocampus (n=8) compared to controls (n=7) (*p
Figure Legend Snippet: Mitochondrial biogenesis proteins were reduced in AD hippocampus. A) Immunoblot and quantification analysis revealed that total protein levels of PGC-1α were significantly reduced in AD hippocampus (n=8) compared to controls (n=7) (*p

Techniques Used: Pyrolysis Gas Chromatography

20) Product Images from "Combination of exercise training and erythropoietin prevents cancer-induced muscle alterations"

Article Title: Combination of exercise training and erythropoietin prevents cancer-induced muscle alterations

Journal: Oncotarget

doi:

Exercise training and EPO regulate bioenergetics-related gene and protein expression in LLC-bearing mice A. Protein expression analysis of PGC-1α, LC3B (either in native or lipidated form, -I and -II, respectively) and Bnip3 corrected for tubulin abundance in gastrocnemius (GSN) muscle of control (C) and LLC-bearing mice (LLC). LLC groups were subdivided in sedentary, EPO-treated (EPO), exercised (EX), and exercised EPO-treated (EX EPO). Data (mean±SD) expressed as % of controls. B. Gene expression analysis of EPOR, myoglobin (MB), Atrogin-1, PGC-1alpha, PGC-1beta, NRF1, Nix, Bnip3, DRP-1 and Fis-1 in the tibialis anterior muscle. Specific mRNA abundance was corrected for the mean of TBP (TATA box-binding protein) and β-actin levels on individual samples. Data (mean±SE) are compared by 2-way ANOVA. Significance of the differences: * p
Figure Legend Snippet: Exercise training and EPO regulate bioenergetics-related gene and protein expression in LLC-bearing mice A. Protein expression analysis of PGC-1α, LC3B (either in native or lipidated form, -I and -II, respectively) and Bnip3 corrected for tubulin abundance in gastrocnemius (GSN) muscle of control (C) and LLC-bearing mice (LLC). LLC groups were subdivided in sedentary, EPO-treated (EPO), exercised (EX), and exercised EPO-treated (EX EPO). Data (mean±SD) expressed as % of controls. B. Gene expression analysis of EPOR, myoglobin (MB), Atrogin-1, PGC-1alpha, PGC-1beta, NRF1, Nix, Bnip3, DRP-1 and Fis-1 in the tibialis anterior muscle. Specific mRNA abundance was corrected for the mean of TBP (TATA box-binding protein) and β-actin levels on individual samples. Data (mean±SE) are compared by 2-way ANOVA. Significance of the differences: * p

Techniques Used: Expressing, Mouse Assay, Pyrolysis Gas Chromatography, Binding Assay

Proposed mechanism of action of exercise, EPO and PGC-1α in counteracting tumor-induced muscle alterations See text for further details.
Figure Legend Snippet: Proposed mechanism of action of exercise, EPO and PGC-1α in counteracting tumor-induced muscle alterations See text for further details.

Techniques Used: Pyrolysis Gas Chromatography

Exercise training and EPO counteract oxidative fiber atrophy and glycolytic shift stimulating PGC-1α expression A. SDH (succinate dehydrogenase) staining in cross sections of tibialis muscle from control (C), C26-bearing (C26) and C26 exercised EPO-treated (EX EPO) mice (2 weeks of exercise). The two micrographs for each group represent two regions with distinct frequency of oxidative (Ox) and glycolytic (Glyc) fibers. B. Morphometric analysis of myofiber CSA (cross-sectional area) performed on SDH stained sections. Data (mean±SD) are expressed as percentages of controls. C. Quantification of fiber type frequency in the tibialis muscle. Data (mean±SD) are expressed as relative percentages. D. PGC-1α nuclear protein expression in the tibialis muscles. Densitometric quantifications were normalized according to GAPDH levels. Data (mean±SD) are expressed as percentages of controls. Significance of the differences: * p
Figure Legend Snippet: Exercise training and EPO counteract oxidative fiber atrophy and glycolytic shift stimulating PGC-1α expression A. SDH (succinate dehydrogenase) staining in cross sections of tibialis muscle from control (C), C26-bearing (C26) and C26 exercised EPO-treated (EX EPO) mice (2 weeks of exercise). The two micrographs for each group represent two regions with distinct frequency of oxidative (Ox) and glycolytic (Glyc) fibers. B. Morphometric analysis of myofiber CSA (cross-sectional area) performed on SDH stained sections. Data (mean±SD) are expressed as percentages of controls. C. Quantification of fiber type frequency in the tibialis muscle. Data (mean±SD) are expressed as relative percentages. D. PGC-1α nuclear protein expression in the tibialis muscles. Densitometric quantifications were normalized according to GAPDH levels. Data (mean±SD) are expressed as percentages of controls. Significance of the differences: * p

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Staining, Mouse Assay

PGC-1α overexpression prevents cachexia in LLC-bearing mice Gastrocnemius (GSN), tibialis (TIB) and heart weight A. and tibialis fiber CSA B. in female control WT (C WT), PGC (C PGC) and LLC-bearing mice WT (LLC WT) and PGC (LLC PGC). Data (mean±SD) are expressed as percentages of C WT. C. Gene expression analysis of Atrogin-1 and MuRF1 transcripts. Specific mRNA abundance was corrected for the mean of TBP (TATA box-binding protein) and β-actin levels on individual samples. Data (means ± SE) are compared by 2-way ANOVA. Significance of the differences: * p
Figure Legend Snippet: PGC-1α overexpression prevents cachexia in LLC-bearing mice Gastrocnemius (GSN), tibialis (TIB) and heart weight A. and tibialis fiber CSA B. in female control WT (C WT), PGC (C PGC) and LLC-bearing mice WT (LLC WT) and PGC (LLC PGC). Data (mean±SD) are expressed as percentages of C WT. C. Gene expression analysis of Atrogin-1 and MuRF1 transcripts. Specific mRNA abundance was corrected for the mean of TBP (TATA box-binding protein) and β-actin levels on individual samples. Data (means ± SE) are compared by 2-way ANOVA. Significance of the differences: * p

Techniques Used: Pyrolysis Gas Chromatography, Over Expression, Mouse Assay, Expressing, Binding Assay

21) Product Images from "Sirtuin 3, a New Target of PGC-1?, Plays an Important Role in the Suppression of ROS and Mitochondrial Biogenesis"

Article Title: Sirtuin 3, a New Target of PGC-1?, Plays an Important Role in the Suppression of ROS and Mitochondrial Biogenesis

Journal: PLoS ONE

doi: 10.1371/journal.pone.0011707

SIRT3 mediates the PGC-1α induction of mitochondrial-related genes in C 2 C 12 skeletal muscle cells. A , Knockdown of mSIRT3 protein level with shRNA in C 2 C 12 myotubes. C 2 C 12 cells were induced to differentiate into myotubes and infected with adenovirus expressing either control shRNA (siControl) or SIRT3 shRNA (siSIRT3). Cells were harvested 48 h after infection, and protein was extracted for western blotting with the indicated antibodies. B , mSirt3 mRNA level was reduced by shRNA against mSirt3 in C 2 C 12 myotubes. C 2 C 12 myoblasts were induced into myotubes and infected with the indicated adenovirus expressing siSIRT3 or siControl, in the presence of Ad-GFP or Ad-PGC-1α and/or Ad-ERRα. Total RNA was extracted 48 h after infection, and Sirt3 mRNA level was determined by qPCR, normalized to β-actin, and expressed relative to control cells infected with Ad-GFP. C , Knockdown of SIRT3 decreases the PGC-1α induction of mitochondrial-related gene expression. C 2 C 12 cells were treated as described in Panel B. The mRNA levels of SOD2, GPx1, ATP5c and Cyt c were measured by qPCR. D , C 2 C 12 cells were treated as described in Panel B. The protein levels of SOD2 were determined by western blotting. E , Overexpression of SIRT3 increased the mRNA levels of GPx1 and ATP5c. C 2 C 12 myotubes were infected with adenoviruses expressing GFP or long-form mSIRT3. Cells were harvested and total RNA was extracted 48 h after infection. The mRNA levels of GPx1 and ATP5c were measured by qPCR, normalized to β-actin, and expressed relative to control cells infected with Ad-GFP. Values represent the mean of three independent experiments performed in triplicate. *, P
Figure Legend Snippet: SIRT3 mediates the PGC-1α induction of mitochondrial-related genes in C 2 C 12 skeletal muscle cells. A , Knockdown of mSIRT3 protein level with shRNA in C 2 C 12 myotubes. C 2 C 12 cells were induced to differentiate into myotubes and infected with adenovirus expressing either control shRNA (siControl) or SIRT3 shRNA (siSIRT3). Cells were harvested 48 h after infection, and protein was extracted for western blotting with the indicated antibodies. B , mSirt3 mRNA level was reduced by shRNA against mSirt3 in C 2 C 12 myotubes. C 2 C 12 myoblasts were induced into myotubes and infected with the indicated adenovirus expressing siSIRT3 or siControl, in the presence of Ad-GFP or Ad-PGC-1α and/or Ad-ERRα. Total RNA was extracted 48 h after infection, and Sirt3 mRNA level was determined by qPCR, normalized to β-actin, and expressed relative to control cells infected with Ad-GFP. C , Knockdown of SIRT3 decreases the PGC-1α induction of mitochondrial-related gene expression. C 2 C 12 cells were treated as described in Panel B. The mRNA levels of SOD2, GPx1, ATP5c and Cyt c were measured by qPCR. D , C 2 C 12 cells were treated as described in Panel B. The protein levels of SOD2 were determined by western blotting. E , Overexpression of SIRT3 increased the mRNA levels of GPx1 and ATP5c. C 2 C 12 myotubes were infected with adenoviruses expressing GFP or long-form mSIRT3. Cells were harvested and total RNA was extracted 48 h after infection. The mRNA levels of GPx1 and ATP5c were measured by qPCR, normalized to β-actin, and expressed relative to control cells infected with Ad-GFP. Values represent the mean of three independent experiments performed in triplicate. *, P

Techniques Used: Pyrolysis Gas Chromatography, shRNA, Infection, Expressing, Western Blot, Real-time Polymerase Chain Reaction, Over Expression

Scheme illustrating a regulatory pathway including PGC-1α and SIRT3 governing ROS level and mitochondrial biogenesis. PGC-1α coactivates ERRα to stimulate the expression of mSIRT3, which, in turn, increases the expression of the ROS-detoxifying enzymes GPx1 and SOD2 to suppress the ROS levels. Meanwhile, ectopic expression of SIRT3 leads to an increase of CREB phosphorylation, which subsequently stimulates the expression of PGC-1α and its target gene UCP1, finally decreasing intracellular ROS level. SIRT3 is also involved in mitochondrial biogenesis.
Figure Legend Snippet: Scheme illustrating a regulatory pathway including PGC-1α and SIRT3 governing ROS level and mitochondrial biogenesis. PGC-1α coactivates ERRα to stimulate the expression of mSIRT3, which, in turn, increases the expression of the ROS-detoxifying enzymes GPx1 and SOD2 to suppress the ROS levels. Meanwhile, ectopic expression of SIRT3 leads to an increase of CREB phosphorylation, which subsequently stimulates the expression of PGC-1α and its target gene UCP1, finally decreasing intracellular ROS level. SIRT3 is also involved in mitochondrial biogenesis.

Techniques Used: Pyrolysis Gas Chromatography, Expressing

ERRα is required for the PGC-1α induction of Sirt3 expression. A , The full-length wild-type Sirt3 promoter fused to luciferase reporter gene (Luc-2036) was cotransfected into HepG2 cells with pcDNA3.1 (control) or PGC-1α in the presence of shRNA against ERRα or luciferase (control). Two days later, cells were harvested and RLA analyzed. B , Knockdown of ERRα reduced the induction of Sirt3 mRNA level by PGC-1α. C 2 C 12 myotubes were infected with adenoviruses expressing GFP or PGC-1α in the presence of Ad-siControl or Ad-siERRα. Total RNA was isolated 48 h later. Sirt3 mRNA level was determined by qPCR, normalized to β-actin, and expressed relative to control cells infected with Ad-GFP and Ad-siControl. All values represent at least three independent transfections, each conducted in triplicate. *, P
Figure Legend Snippet: ERRα is required for the PGC-1α induction of Sirt3 expression. A , The full-length wild-type Sirt3 promoter fused to luciferase reporter gene (Luc-2036) was cotransfected into HepG2 cells with pcDNA3.1 (control) or PGC-1α in the presence of shRNA against ERRα or luciferase (control). Two days later, cells were harvested and RLA analyzed. B , Knockdown of ERRα reduced the induction of Sirt3 mRNA level by PGC-1α. C 2 C 12 myotubes were infected with adenoviruses expressing GFP or PGC-1α in the presence of Ad-siControl or Ad-siERRα. Total RNA was isolated 48 h later. Sirt3 mRNA level was determined by qPCR, normalized to β-actin, and expressed relative to control cells infected with Ad-GFP and Ad-siControl. All values represent at least three independent transfections, each conducted in triplicate. *, P

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Luciferase, shRNA, Infection, Isolation, Real-time Polymerase Chain Reaction, Transfection

PGC-1α regulates the expression of SIRT3. A , Differentiated C 2 C 12 cells (left panel), primary hepatocytes isolated from mouse liver (middle panel) and HepG2 cells (right panel) were infected with adenoviruses expressing GFP (control) or PGC-1α. Cells were harvested 48 h after infection, and total RNA was extracted. The mRNA levels of Sirt3 were quantified by qPCR, normalized to β-actin, and expressed relative to the GFP-expressing control cells. B , C 2 C 12 myotubes and primary hepatocytes were treated as described in Panel A, and SIRT3 protein level was determined by western blotting. Two specific bands of SIRT3 in C 2 C 12 (left panel) and primary hepatocytes (right panel) were detected. L, long form of mSIRT3 (approximately 37 kDa). S, short form of mSIRT3 (approximately 28 kDa). C, left panel , C 2 C 12 myoblasts were induced to differentiate into myotubes. Cells were harvested on day 0 (before differentiation) and day 5 (after differentiation), and total RNA was isolated. C, right panel , Total RNA was extracted from normal or fasted mouse livers. The mRNA levels of PGC-1α and Sirt3 were quantified by qPCR, normalized to β-actin and expressed relative to levels in the control. D , Differentiated C 2 C 12 (left panel) and primary hepatocytes (right panel) were infected with adenovirus expressing luciferase shRNA (siControl) or PGC-1α shRNA (siPGC-1α). Cells were harvested 48 hours after infection, and total RNA was extracted. The mRNA levels of Sirt3 and PGC-1α were quantified by qPCR, normalized to β-actin, and expressed relative to the control cells. *, P
Figure Legend Snippet: PGC-1α regulates the expression of SIRT3. A , Differentiated C 2 C 12 cells (left panel), primary hepatocytes isolated from mouse liver (middle panel) and HepG2 cells (right panel) were infected with adenoviruses expressing GFP (control) or PGC-1α. Cells were harvested 48 h after infection, and total RNA was extracted. The mRNA levels of Sirt3 were quantified by qPCR, normalized to β-actin, and expressed relative to the GFP-expressing control cells. B , C 2 C 12 myotubes and primary hepatocytes were treated as described in Panel A, and SIRT3 protein level was determined by western blotting. Two specific bands of SIRT3 in C 2 C 12 (left panel) and primary hepatocytes (right panel) were detected. L, long form of mSIRT3 (approximately 37 kDa). S, short form of mSIRT3 (approximately 28 kDa). C, left panel , C 2 C 12 myoblasts were induced to differentiate into myotubes. Cells were harvested on day 0 (before differentiation) and day 5 (after differentiation), and total RNA was isolated. C, right panel , Total RNA was extracted from normal or fasted mouse livers. The mRNA levels of PGC-1α and Sirt3 were quantified by qPCR, normalized to β-actin and expressed relative to levels in the control. D , Differentiated C 2 C 12 (left panel) and primary hepatocytes (right panel) were infected with adenovirus expressing luciferase shRNA (siControl) or PGC-1α shRNA (siPGC-1α). Cells were harvested 48 hours after infection, and total RNA was extracted. The mRNA levels of Sirt3 and PGC-1α were quantified by qPCR, normalized to β-actin, and expressed relative to the control cells. *, P

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Isolation, Infection, Real-time Polymerase Chain Reaction, Western Blot, Luciferase, shRNA

SIRT3 controls intracellular ROS levels. A , C 2 C 12 myotubes were infected with adenovirus expressing GFP or SIRT3. DHE (5 µM) was added to media 30 min before collecting cells. The cells were harvested and immediately analyzed with a flow cytometry, and data were processed with Expo 32ADC software. The histogram overlays showed overexpression of mSIRT3 reduced the cellular ROS level. B , Knockdown of PGC-1α or SIRT3 increased cellular ROS level. C 2 C 12 myotubes were treated with the indicated adenovirus (Ad-siControl, Ad-siPGC-1α or Ad-siSIRT3), treated with DHE, and analyzed with a flow cytometry as described in panel A. C , Overexpression of PGC-1α decreased cellular ROS level, and knockdown of SIRT3 blocked the inhibitory effect of PGC-1α on ROS production. C 2 C 12 myotubes were treated with the indicated adenovirus (Ad-GFP, Ad-PGC-1α, Ad-siControl, or/and Ad-siSIRT3), treated with DHE, and analyzed with a flow cytometer as described in panel A. x -Axis, fluorescence intensity showing the extent of DHE oxidation; y -axis, cell number. The image is representative of three experiments. Right panels , Flow cytometry analysis of myotube cells. Values represent the mean of four independent experiments performed in duplicate. MFI, mean fluorescent intensity. *, P
Figure Legend Snippet: SIRT3 controls intracellular ROS levels. A , C 2 C 12 myotubes were infected with adenovirus expressing GFP or SIRT3. DHE (5 µM) was added to media 30 min before collecting cells. The cells were harvested and immediately analyzed with a flow cytometry, and data were processed with Expo 32ADC software. The histogram overlays showed overexpression of mSIRT3 reduced the cellular ROS level. B , Knockdown of PGC-1α or SIRT3 increased cellular ROS level. C 2 C 12 myotubes were treated with the indicated adenovirus (Ad-siControl, Ad-siPGC-1α or Ad-siSIRT3), treated with DHE, and analyzed with a flow cytometry as described in panel A. C , Overexpression of PGC-1α decreased cellular ROS level, and knockdown of SIRT3 blocked the inhibitory effect of PGC-1α on ROS production. C 2 C 12 myotubes were treated with the indicated adenovirus (Ad-GFP, Ad-PGC-1α, Ad-siControl, or/and Ad-siSIRT3), treated with DHE, and analyzed with a flow cytometer as described in panel A. x -Axis, fluorescence intensity showing the extent of DHE oxidation; y -axis, cell number. The image is representative of three experiments. Right panels , Flow cytometry analysis of myotube cells. Values represent the mean of four independent experiments performed in duplicate. MFI, mean fluorescent intensity. *, P

Techniques Used: Infection, Expressing, Flow Cytometry, Cytometry, Software, Over Expression, Pyrolysis Gas Chromatography, Fluorescence

SIRT3 mediates the PGC-1α induction of mitochondrial biogenesis in C 2 C 12 myotubes. A , SIRT3 overexpression stimulated mitochondrial biogenesis. C 2 C 12 myotubes were infected with Ad-GFP or Ad-SIRT3. Cells were harvested 48 h after infection, and the DNA level of the mitochondrial-encoded COX II gene was measured by qPCR, normalized to DNA levels of the nuclear-encoded gene cyclophilin A, and expressed relative to levels in control cells expressing GFP, which were set to 1. B , Knockdown of SIRT3 inhibited the induction of mitochondrial biogenesis by PGC-1α. C 2 C 12 myotubes were infected with the indicated adenovirus (Ad-GFP, Ad-PGC-1α, Ad-siControl, or/and Ad-siSIRT3). Mitochondrial DNA copy number was measured as described in panel A. C , Knockdown of SIRT3 inhibited the induction of mRNA level of COX I, COX II and COX VIIa by PGC-1α. C 2 C 12 myotubes were infected with the indicated adenovirus (Ad-GFP, Ad-PGC-1α, Ad-siControl, and/or Ad-siSIRT3). Cells were harvested and total RNA was extracted 48 h after infection. The mRNA levels of mitochondrial-encoded (COX I and COX II) and nuclear-encoded (COX VIIa) subunits of COX were measured by qPCR, normalized to β-actin, and expressed relative to control cells infected with Ad-GFP and Ad-siControl. Values represent the mean of three independent experiments performed in duplicate. *, P
Figure Legend Snippet: SIRT3 mediates the PGC-1α induction of mitochondrial biogenesis in C 2 C 12 myotubes. A , SIRT3 overexpression stimulated mitochondrial biogenesis. C 2 C 12 myotubes were infected with Ad-GFP or Ad-SIRT3. Cells were harvested 48 h after infection, and the DNA level of the mitochondrial-encoded COX II gene was measured by qPCR, normalized to DNA levels of the nuclear-encoded gene cyclophilin A, and expressed relative to levels in control cells expressing GFP, which were set to 1. B , Knockdown of SIRT3 inhibited the induction of mitochondrial biogenesis by PGC-1α. C 2 C 12 myotubes were infected with the indicated adenovirus (Ad-GFP, Ad-PGC-1α, Ad-siControl, or/and Ad-siSIRT3). Mitochondrial DNA copy number was measured as described in panel A. C , Knockdown of SIRT3 inhibited the induction of mRNA level of COX I, COX II and COX VIIa by PGC-1α. C 2 C 12 myotubes were infected with the indicated adenovirus (Ad-GFP, Ad-PGC-1α, Ad-siControl, and/or Ad-siSIRT3). Cells were harvested and total RNA was extracted 48 h after infection. The mRNA levels of mitochondrial-encoded (COX I and COX II) and nuclear-encoded (COX VIIa) subunits of COX were measured by qPCR, normalized to β-actin, and expressed relative to control cells infected with Ad-GFP and Ad-siControl. Values represent the mean of three independent experiments performed in duplicate. *, P

Techniques Used: Pyrolysis Gas Chromatography, Over Expression, Infection, Real-time Polymerase Chain Reaction, Expressing

ERRα interacts with the mouse Sirt3 promoter in vitro and in vivo . A , Electrophoretic mobility shift assay was executed using a biotin probe. Biotin-labeled double-stranded oligonucleotides were incubated with or without nuclear extract containing ERRα protein. Approximately 200-fold excess wild-type and ERRE-mutated unlabeled double-stranded oligonucleotides were used for competitive inhibition. B , Primary hepatocytes were isolated, cultured in 100 mm dishes, and infected with adenoviruses expressing ERRα-FLAG and/or PGC-1α, or GFP as a control. For ChIP, protein-DNA complexes were immunoprecipitated with anti-FLAG or control IgG antibody. The mSirt3 promoter region harboring the ERRE site was amplified by PCR. C , Primary hepatocytes were isolated from mouse liver, and chromatin was immunoprecipitated with anti-PGC-1α antibody. Normal IgG was used as control. The mSirt3 promoter region harboring the ERRE (proximal region) could be amplified by PCR. However, the distal region of the mSirt3 promoter, having no ERRE and used as a negative control, could not be amplified.
Figure Legend Snippet: ERRα interacts with the mouse Sirt3 promoter in vitro and in vivo . A , Electrophoretic mobility shift assay was executed using a biotin probe. Biotin-labeled double-stranded oligonucleotides were incubated with or without nuclear extract containing ERRα protein. Approximately 200-fold excess wild-type and ERRE-mutated unlabeled double-stranded oligonucleotides were used for competitive inhibition. B , Primary hepatocytes were isolated, cultured in 100 mm dishes, and infected with adenoviruses expressing ERRα-FLAG and/or PGC-1α, or GFP as a control. For ChIP, protein-DNA complexes were immunoprecipitated with anti-FLAG or control IgG antibody. The mSirt3 promoter region harboring the ERRE site was amplified by PCR. C , Primary hepatocytes were isolated from mouse liver, and chromatin was immunoprecipitated with anti-PGC-1α antibody. Normal IgG was used as control. The mSirt3 promoter region harboring the ERRE (proximal region) could be amplified by PCR. However, the distal region of the mSirt3 promoter, having no ERRE and used as a negative control, could not be amplified.

Techniques Used: In Vitro, In Vivo, Electrophoretic Mobility Shift Assay, Labeling, Incubation, Inhibition, Isolation, Cell Culture, Infection, Expressing, Pyrolysis Gas Chromatography, Chromatin Immunoprecipitation, Immunoprecipitation, Amplification, Polymerase Chain Reaction, Negative Control

ERRα mediates the PGC-1α activation of the Sirt3 gene promoter in HepG2 cells. A , Schematic representation of the promoter sequence of mSirt3 (Luc-2036). Exon 1A (E1A) and exon 1B (E1B) of mSirt3 are alternatively spliced according to previous report [34] . Thus, mSirt3 has two different transcriptional start sites. However, E1A does not encode amino acids. B , 5′-Deletion series of the mSirt3 promoter fused to luciferase reporter gene were cotransfected into HepG2 cells together with pcDNA3.1 (control) or PGC-1α in the presence or absence of ERRα expression plasmids. Two days later, cells were harvested and the relative luciferase activity (RLA) was corrected for Renilla luciferase activity and normalized to the control activity. C , The nucleotide sequence from −424 to −366 of the mouse (Mou) Sirt3 gene promoter was aligned with corresponding sequences from different species, including rat, humans (Hum), and chimpanzee (Chp). Evolutionarily conserved elements are indicated in large, bold, italic type. D, left panel , Wild-type putative ERRα binding element and its mutant sequence; right panel , Reporter gene plasmid containing 2.2 kb of the wild-type (WT) Sirt3 promoter (Luc-2036) or ERRE mutant (mut Luc-2036) were transfected into HepG2 cells together with PGC-1α in the presence or absence of ERRα expression plasmids or empty plasmid (pcDNA3.1). The graph depicts RLA corrected for Renilla luciferase activity and normalized to the control activity of mSirt3. All values represent at least three independent transfections, each conducted in triplicate. *, P
Figure Legend Snippet: ERRα mediates the PGC-1α activation of the Sirt3 gene promoter in HepG2 cells. A , Schematic representation of the promoter sequence of mSirt3 (Luc-2036). Exon 1A (E1A) and exon 1B (E1B) of mSirt3 are alternatively spliced according to previous report [34] . Thus, mSirt3 has two different transcriptional start sites. However, E1A does not encode amino acids. B , 5′-Deletion series of the mSirt3 promoter fused to luciferase reporter gene were cotransfected into HepG2 cells together with pcDNA3.1 (control) or PGC-1α in the presence or absence of ERRα expression plasmids. Two days later, cells were harvested and the relative luciferase activity (RLA) was corrected for Renilla luciferase activity and normalized to the control activity. C , The nucleotide sequence from −424 to −366 of the mouse (Mou) Sirt3 gene promoter was aligned with corresponding sequences from different species, including rat, humans (Hum), and chimpanzee (Chp). Evolutionarily conserved elements are indicated in large, bold, italic type. D, left panel , Wild-type putative ERRα binding element and its mutant sequence; right panel , Reporter gene plasmid containing 2.2 kb of the wild-type (WT) Sirt3 promoter (Luc-2036) or ERRE mutant (mut Luc-2036) were transfected into HepG2 cells together with PGC-1α in the presence or absence of ERRα expression plasmids or empty plasmid (pcDNA3.1). The graph depicts RLA corrected for Renilla luciferase activity and normalized to the control activity of mSirt3. All values represent at least three independent transfections, each conducted in triplicate. *, P

Techniques Used: Pyrolysis Gas Chromatography, Activation Assay, Sequencing, Luciferase, Expressing, Activity Assay, Binding Assay, Mutagenesis, Plasmid Preparation, Transfection

22) Product Images from "Methylene blue alleviates nuclear and mitochondrial abnormalities in progeria"

Article Title: Methylene blue alleviates nuclear and mitochondrial abnormalities in progeria

Journal: Aging Cell

doi: 10.1111/acel.12434

Reduced PGC ‐1α expression in HGPS cells. (A) Quantitative RT – PCR analysis of PGC ‐1α expression in two normal and two HGPS fibroblast cell lines (** P
Figure Legend Snippet: Reduced PGC ‐1α expression in HGPS cells. (A) Quantitative RT – PCR analysis of PGC ‐1α expression in two normal and two HGPS fibroblast cell lines (** P

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Quantitative RT-PCR

23) Product Images from "Black Tea High-Molecular-Weight Polyphenol Stimulates Exercise Training-Induced Improvement of Endurance Capacity in Mouse via the Link between AMPK and GLUT4"

Article Title: Black Tea High-Molecular-Weight Polyphenol Stimulates Exercise Training-Induced Improvement of Endurance Capacity in Mouse via the Link between AMPK and GLUT4

Journal: PLoS ONE

doi: 10.1371/journal.pone.0069480

MAF intake increases exercise training-induced factors involved in fast-to-slow transition. AMPKα phosphorylation and expression levels of PGC-1α, PPARδ, cytochrome c, and myoglobin in each group were measured by Western blotting. Representative blots ( A ) and quantification ( B ) are shown for each protein. p-AMPK was determined as p-AMPKα/total AMPKα ratio. Other proteins are normalized to β-actin. *, and §, statistically significant difference between the C and T M groups. #, statistically significant difference between the T and TM groups (* and #: p
Figure Legend Snippet: MAF intake increases exercise training-induced factors involved in fast-to-slow transition. AMPKα phosphorylation and expression levels of PGC-1α, PPARδ, cytochrome c, and myoglobin in each group were measured by Western blotting. Representative blots ( A ) and quantification ( B ) are shown for each protein. p-AMPK was determined as p-AMPKα/total AMPKα ratio. Other proteins are normalized to β-actin. *, and §, statistically significant difference between the C and T M groups. #, statistically significant difference between the T and TM groups (* and #: p

Techniques Used: Expressing, Pyrolysis Gas Chromatography, Western Blot

24) Product Images from "Impaired Muscle AMPK Activation in the Metabolic Syndrome May Attenuate Improved Insulin Action after Exercise Training"

Article Title: Impaired Muscle AMPK Activation in the Metabolic Syndrome May Attenuate Improved Insulin Action after Exercise Training

Journal: The Journal of Clinical Endocrinology and Metabolism

doi: 10.1210/jc.2010-2532

Training-related changes in GLUT4, GLUT5, AMPK, phospho-AMPK, PGC-1α, ATP synthase, total mTOR, and phospho-mTOR. Muscle glucose transporter expression was increased after resistance training. Panels A and B, Examples of typical immunoblots for
Figure Legend Snippet: Training-related changes in GLUT4, GLUT5, AMPK, phospho-AMPK, PGC-1α, ATP synthase, total mTOR, and phospho-mTOR. Muscle glucose transporter expression was increased after resistance training. Panels A and B, Examples of typical immunoblots for

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Western Blot

25) Product Images from "Neuroprotection by quercetin via mitochondrial function adaptation in traumatic brain injury: PGC‐1α pathway as a potential mechanism"

Article Title: Neuroprotection by quercetin via mitochondrial function adaptation in traumatic brain injury: PGC‐1α pathway as a potential mechanism

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.13313

Quercetin promoted translocation of PGC‐1α from cytoplasm to nucleus and enhanced PGC‐1α binding. ( A‐D ) The representative photomicrographs showing PGC‐1α immunohistochemistry of tissue from different group 24 hrs after TBI. ( E, H ) The nuclear PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( F, I ) The cytoplasmic protein PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( G, J ) The total protein PGC‐1α expression after melatonin treatment in mice with TBI, as measured by Western blot. Bars represent the mean ± S.E.M. * P
Figure Legend Snippet: Quercetin promoted translocation of PGC‐1α from cytoplasm to nucleus and enhanced PGC‐1α binding. ( A‐D ) The representative photomicrographs showing PGC‐1α immunohistochemistry of tissue from different group 24 hrs after TBI. ( E, H ) The nuclear PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( F, I ) The cytoplasmic protein PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( G, J ) The total protein PGC‐1α expression after melatonin treatment in mice with TBI, as measured by Western blot. Bars represent the mean ± S.E.M. * P

Techniques Used: Translocation Assay, Pyrolysis Gas Chromatography, Binding Assay, Immunohistochemistry, Expressing, Mouse Assay, Western Blot

26) Product Images from "Sirtuin 1 (SIRT1) Deacetylase Activity Is Not Required for Mitochondrial Biogenesis or Peroxisome Proliferator-activated Receptor-? Coactivator-1? (PGC-1?) Deacetylation following Endurance Exercise *"

Article Title: Sirtuin 1 (SIRT1) Deacetylase Activity Is Not Required for Mitochondrial Biogenesis or Peroxisome Proliferator-activated Receptor-? Coactivator-1? (PGC-1?) Deacetylation following Endurance Exercise *

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M111.261685

mKO mice display normal activation of PGC-1α and exercise-responsive genes following AEX. A , PGC-1 α and, B, mitofusin-2 , cytochrome c , and pyruvate dehydrogenase kinase 4 ( PDK4 ) skeletal muscle gene expression on sedentary ( SED ) or 3 h
Figure Legend Snippet: mKO mice display normal activation of PGC-1α and exercise-responsive genes following AEX. A , PGC-1 α and, B, mitofusin-2 , cytochrome c , and pyruvate dehydrogenase kinase 4 ( PDK4 ) skeletal muscle gene expression on sedentary ( SED ) or 3 h

Techniques Used: Mouse Assay, Activation Assay, Pyrolysis Gas Chromatography, Expressing

PGC-1α nuclear translocation and deacetylation following AEX are unaffected by loss of SIRT1 activity. A and B , integrity of nuclear and cytosolic fractions was determined via immunoblotting for lactate dehydrogenase ( LDH ) (cytosolic; Cyto ) and
Figure Legend Snippet: PGC-1α nuclear translocation and deacetylation following AEX are unaffected by loss of SIRT1 activity. A and B , integrity of nuclear and cytosolic fractions was determined via immunoblotting for lactate dehydrogenase ( LDH ) (cytosolic; Cyto ) and

Techniques Used: Pyrolysis Gas Chromatography, Translocation Assay, Activity Assay

Loss of SIRT1 activity does not impair mitochondrial biogenesis following 20-days of voluntary wheel running ( VWR ). A , average running time per day during 20 days of VWR in mKO and WT mice. B , immunoblotting and quantification of PGC-1α and electron
Figure Legend Snippet: Loss of SIRT1 activity does not impair mitochondrial biogenesis following 20-days of voluntary wheel running ( VWR ). A , average running time per day during 20 days of VWR in mKO and WT mice. B , immunoblotting and quantification of PGC-1α and electron

Techniques Used: Activity Assay, Mouse Assay, Pyrolysis Gas Chromatography

Nuclear abundance of GCN5 and the association of GCN5 with PGC-1α are decreased after AEX. A , immunoblotting ( IB ) of GCN5 and H2B in nuclear fractions of sedentary ( SED ) and 3 h after AEX ( 3h Post ) skeletal muscle of WT and mKO mice. 3 h after
Figure Legend Snippet: Nuclear abundance of GCN5 and the association of GCN5 with PGC-1α are decreased after AEX. A , immunoblotting ( IB ) of GCN5 and H2B in nuclear fractions of sedentary ( SED ) and 3 h after AEX ( 3h Post ) skeletal muscle of WT and mKO mice. 3 h after

Techniques Used: Pyrolysis Gas Chromatography, Mouse Assay

27) Product Images from "Peroxisome Proliferator-activated Receptor ? Co-activator 1? (PGC-1?) and Sirtuin 1 (SIRT1) Reside in Mitochondria"

Article Title: Peroxisome Proliferator-activated Receptor ? Co-activator 1? (PGC-1?) and Sirtuin 1 (SIRT1) Reside in Mitochondria

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M109.070169

Detection of mitochondrial SIRT1 and PGC-1α by immunofluorescence microscopy in SH-SY5Y cells. A , mitochondrial network and nuclei were evidenced by incubation with mouse anti-cytochrome c and Hoechst 33342, respectively. PGC-1α or SIRT1 was stained by using rabbit antibodies (Santa Cruz Biotechnology). B , PGC-1α and SIRT1 were stained by using goat anti-PGC-1α (Santa Cruz Biotechnology) and rabbit anti-SIRT1. Cells were analyzed by an Olympus Delta vision deconvolution fluorescent microscope. The yellow-orange color obtained by image merge indicates the regions where the green and red signals superimpose. White arrows indicate some regions of co-localization signals. Scale bar, 10 μm.
Figure Legend Snippet: Detection of mitochondrial SIRT1 and PGC-1α by immunofluorescence microscopy in SH-SY5Y cells. A , mitochondrial network and nuclei were evidenced by incubation with mouse anti-cytochrome c and Hoechst 33342, respectively. PGC-1α or SIRT1 was stained by using rabbit antibodies (Santa Cruz Biotechnology). B , PGC-1α and SIRT1 were stained by using goat anti-PGC-1α (Santa Cruz Biotechnology) and rabbit anti-SIRT1. Cells were analyzed by an Olympus Delta vision deconvolution fluorescent microscope. The yellow-orange color obtained by image merge indicates the regions where the green and red signals superimpose. White arrows indicate some regions of co-localization signals. Scale bar, 10 μm.

Techniques Used: Pyrolysis Gas Chromatography, Immunofluorescence, Microscopy, Incubation, Staining

Assay of the presence of SIRT1 and PGC-1α in cross-linked mitochondrial nucleoids. A , scheme for purification of nucleoids ( N ) from mouse liver mitochondria. Fractions ( 1–14 ) were finally collected by pricking the bottom of the tube. B , presence of mtDNA in the collected fractions was assayed performing PCR analysis of D-loop region. The presence of genomic DNA was excluded by performing PCR analysis of actin gene. After cross-linking reversion, fractions were subjected to SDS-PAGE. Western blot analysis with mouse anti-cytochrome c oxidase subunit IV ( COX IV ) and mouse anti-cytochrome c ( Cyt c ) was carried out to determine the possible presence of protein contaminants. SIRT1, HSP60, TFAM, and SOD2 were detected by using specific rabbit antibodies. PGC-1α was detected by using both the Santa Cruz Biotechnology and the Calbiochem antibodies. C , cross-linked mitochondria from mouse liver were sonicated and immunoprecipitated with goat anti-TFAM or goat anti-PGC-1α antibody (Santa Cruz Biotechnology). DNA was extracted, and PCR analysis of the region +15,600/+15,868 of mtDNA was successively carried out. Input and immunoprecipitation with a control IgG were used as positive and negative controls. D , mitochondrial protein extracts from HEK293 cells were analyzed by oligonucleotide pulldown assay using TFAM biotinylated consensus oligonucleotide and Western blot analysis using Santa Cruz Biotechnology anti-TFAM, anti-SIRT1, and anti-PGC-1α antibody. Mito , total mitochondrial lysates; lanes 1 and 2 , two independent oligonucleotide pulldown experiments. Immunoblots reported are from one experiment representative of at least three that gave similar results.
Figure Legend Snippet: Assay of the presence of SIRT1 and PGC-1α in cross-linked mitochondrial nucleoids. A , scheme for purification of nucleoids ( N ) from mouse liver mitochondria. Fractions ( 1–14 ) were finally collected by pricking the bottom of the tube. B , presence of mtDNA in the collected fractions was assayed performing PCR analysis of D-loop region. The presence of genomic DNA was excluded by performing PCR analysis of actin gene. After cross-linking reversion, fractions were subjected to SDS-PAGE. Western blot analysis with mouse anti-cytochrome c oxidase subunit IV ( COX IV ) and mouse anti-cytochrome c ( Cyt c ) was carried out to determine the possible presence of protein contaminants. SIRT1, HSP60, TFAM, and SOD2 were detected by using specific rabbit antibodies. PGC-1α was detected by using both the Santa Cruz Biotechnology and the Calbiochem antibodies. C , cross-linked mitochondria from mouse liver were sonicated and immunoprecipitated with goat anti-TFAM or goat anti-PGC-1α antibody (Santa Cruz Biotechnology). DNA was extracted, and PCR analysis of the region +15,600/+15,868 of mtDNA was successively carried out. Input and immunoprecipitation with a control IgG were used as positive and negative controls. D , mitochondrial protein extracts from HEK293 cells were analyzed by oligonucleotide pulldown assay using TFAM biotinylated consensus oligonucleotide and Western blot analysis using Santa Cruz Biotechnology anti-TFAM, anti-SIRT1, and anti-PGC-1α antibody. Mito , total mitochondrial lysates; lanes 1 and 2 , two independent oligonucleotide pulldown experiments. Immunoblots reported are from one experiment representative of at least three that gave similar results.

Techniques Used: Pyrolysis Gas Chromatography, Purification, Polymerase Chain Reaction, SDS Page, Western Blot, Sonication, Immunoprecipitation

Determination of the association of SIRT1 and PGC-1α with mtDNA and TFAM by confocal microscopy in HeLa cells. A , mtDNA was labeled by BrdUrd incorporation followed by methanol-acetone fixing and immunostaining with mouse anti-BrdUrd. SIRT1 or PGC-1α was also immunostained using Santa Cruz Biotechnology antibodies. Cells were then visualized by confocal microscopy, and the level of superimposition of SIRT1 or PGC-1α-derived signals with that of BrdUrd was evaluated by calculation of the Pearson's correlation coefficient ( R ( r )). Values > 0.50 were considered to be significant. B , HeLa cells were fixed with paraformaldehyde and immunostained with goat anti-TFAM and rabbit Santa Cruz Biotechnology anti-PGC-1α or SIRT1. Cells were then visualized by confocal microscopy, and the level of superimposition of SIRT1 or PGC-1α-derived signals with that of TFAM was evaluated by calculation of the Pearson's correlation coefficient ( R ( r )). Values > 0.50 were considered to be significant. Scale bar, 10 μm.
Figure Legend Snippet: Determination of the association of SIRT1 and PGC-1α with mtDNA and TFAM by confocal microscopy in HeLa cells. A , mtDNA was labeled by BrdUrd incorporation followed by methanol-acetone fixing and immunostaining with mouse anti-BrdUrd. SIRT1 or PGC-1α was also immunostained using Santa Cruz Biotechnology antibodies. Cells were then visualized by confocal microscopy, and the level of superimposition of SIRT1 or PGC-1α-derived signals with that of BrdUrd was evaluated by calculation of the Pearson's correlation coefficient ( R ( r )). Values > 0.50 were considered to be significant. B , HeLa cells were fixed with paraformaldehyde and immunostained with goat anti-TFAM and rabbit Santa Cruz Biotechnology anti-PGC-1α or SIRT1. Cells were then visualized by confocal microscopy, and the level of superimposition of SIRT1 or PGC-1α-derived signals with that of TFAM was evaluated by calculation of the Pearson's correlation coefficient ( R ( r )). Values > 0.50 were considered to be significant. Scale bar, 10 μm.

Techniques Used: Pyrolysis Gas Chromatography, Confocal Microscopy, Labeling, Immunostaining, Derivative Assay

Detection of mitochondrial SIRT1 and PGC-1α in mitochondria purified from HeLa cells and mouse organs and in human platelets. A , scheme for purification of mitochondria from HeLa and mouse organs. B , 10 μg of proteins obtained from HeLa purified mitochondria ( Mito ) and nuclei-enriched pellets ( P1 ) were subjected to SDS-PAGE followed by Western blot analysis. The possible presence of nuclear protein contaminants was measured by incubating nitrocellulose membrane with rabbit anti-H2B. The effective mitochondria isolation was assessed by staining with rabbit anti-TFAM and mouse anti-cytochrome c oxidase sub IV ( COX IV ). PGC-1α and SIRT1 were detected by using rabbit Santa Cruz Biotechnology antibodies. C , 10 μg of proteins obtained from nuclei-enriched pellets ( P1 ) and mitochondria ( Mito ) isolated from mice brain ( B ), skeletal muscle ( M ), and liver ( L ) were subjected to SDS-PAGE followed by Western blot analysis. The possible presence of nuclear protein contaminants was measured by incubating nitrocellulose membrane with rabbit anti-lamin B. The effective mitochondrial isolation was assessed by staining with rabbit anti-SOD2. PGC-1α and SIRT1 were detected by using Santa Cruz Biotechnology antibodies. D , human platelets were purified from peripheral blood, and 20 μg of protein extracts were subjected to SDS-PAGE followed by Western blot analysis. The possible presence of nuclear proteins was measured by incubating the nitrocellulose membrane with rabbit anti-H2B. PGC-1α and SIRT1 were detected by using Santa Cruz Biotechnology antibodies. Immunoblots reported are from one experiment representative of at least three that gave similar results.
Figure Legend Snippet: Detection of mitochondrial SIRT1 and PGC-1α in mitochondria purified from HeLa cells and mouse organs and in human platelets. A , scheme for purification of mitochondria from HeLa and mouse organs. B , 10 μg of proteins obtained from HeLa purified mitochondria ( Mito ) and nuclei-enriched pellets ( P1 ) were subjected to SDS-PAGE followed by Western blot analysis. The possible presence of nuclear protein contaminants was measured by incubating nitrocellulose membrane with rabbit anti-H2B. The effective mitochondria isolation was assessed by staining with rabbit anti-TFAM and mouse anti-cytochrome c oxidase sub IV ( COX IV ). PGC-1α and SIRT1 were detected by using rabbit Santa Cruz Biotechnology antibodies. C , 10 μg of proteins obtained from nuclei-enriched pellets ( P1 ) and mitochondria ( Mito ) isolated from mice brain ( B ), skeletal muscle ( M ), and liver ( L ) were subjected to SDS-PAGE followed by Western blot analysis. The possible presence of nuclear protein contaminants was measured by incubating nitrocellulose membrane with rabbit anti-lamin B. The effective mitochondrial isolation was assessed by staining with rabbit anti-SOD2. PGC-1α and SIRT1 were detected by using Santa Cruz Biotechnology antibodies. D , human platelets were purified from peripheral blood, and 20 μg of protein extracts were subjected to SDS-PAGE followed by Western blot analysis. The possible presence of nuclear proteins was measured by incubating the nitrocellulose membrane with rabbit anti-H2B. PGC-1α and SIRT1 were detected by using Santa Cruz Biotechnology antibodies. Immunoblots reported are from one experiment representative of at least three that gave similar results.

Techniques Used: Pyrolysis Gas Chromatography, Purification, SDS Page, Western Blot, Isolation, Staining, Mouse Assay

Identification of mitochondrial multiprotein complexes by BN-PAGE in liver purified mitochondria. A , mitochondrial proteins were extracted from liver purified mitochondria ( mito ) using a lysis buffer maintaining native interaction in multiprotein complexes. Ten μg of proteins were loaded on blue native gel. The same samples were boiled in the presence of SDS and loaded in parallel with the respective native sample. Western blot ( WB ) analysis using rabbit Santa Cruz Biotechnology anti-SIRT1 or anti-PGC-1α was then performed. B , after BN-PAGE, a second SDS-PAGE dimension was carried out followed by Western blot analysis using rabbit Santa Cruz Biotechnology anti-PGC-1α or anti-SIRT1. MPC , multiprotein complexes. C , 10 μg of proteins were loaded on blue native gel, and Western blot using a rabbit anti-TFAM was carried out. 1 , multiprotein complex containing TFAM, PGC-1α, and SIRT1; 2 and 3, multiprotein complexes containing PGC-1α and SIRT1; 4 , multiprotein complex containing TFAM, and SIRT1; 5 multiprotein complex containing TFAM and PGC-1α; 6 , multiprotein complex containing TFAM-PGC-1α and TFAM-SIRT1; a–c , other TFAM multiprotein complexes. To visualize free TFAM protein, a major exposure was mandatory due to the lower cross-reactivity of TFAM antibody against native TFAM with respect to TFAM engaged in multiprotein complexes (see inset in TFAM immunoblot). Immunoblots reported are from one experiment representative of four that gave similar results.
Figure Legend Snippet: Identification of mitochondrial multiprotein complexes by BN-PAGE in liver purified mitochondria. A , mitochondrial proteins were extracted from liver purified mitochondria ( mito ) using a lysis buffer maintaining native interaction in multiprotein complexes. Ten μg of proteins were loaded on blue native gel. The same samples were boiled in the presence of SDS and loaded in parallel with the respective native sample. Western blot ( WB ) analysis using rabbit Santa Cruz Biotechnology anti-SIRT1 or anti-PGC-1α was then performed. B , after BN-PAGE, a second SDS-PAGE dimension was carried out followed by Western blot analysis using rabbit Santa Cruz Biotechnology anti-PGC-1α or anti-SIRT1. MPC , multiprotein complexes. C , 10 μg of proteins were loaded on blue native gel, and Western blot using a rabbit anti-TFAM was carried out. 1 , multiprotein complex containing TFAM, PGC-1α, and SIRT1; 2 and 3, multiprotein complexes containing PGC-1α and SIRT1; 4 , multiprotein complex containing TFAM, and SIRT1; 5 multiprotein complex containing TFAM and PGC-1α; 6 , multiprotein complex containing TFAM-PGC-1α and TFAM-SIRT1; a–c , other TFAM multiprotein complexes. To visualize free TFAM protein, a major exposure was mandatory due to the lower cross-reactivity of TFAM antibody against native TFAM with respect to TFAM engaged in multiprotein complexes (see inset in TFAM immunoblot). Immunoblots reported are from one experiment representative of four that gave similar results.

Techniques Used: Polyacrylamide Gel Electrophoresis, Purification, Lysis, Western Blot, Pyrolysis Gas Chromatography, SDS Page

Assay of the presence of SIRT1 and PGC-1α in mitochondrial native nucleoids. Native nucleoids were obtained from isolated liver mitochondria as described under “Experimental Procedures.” After sucrose gradient, nucleoid-containing fractions were identified by detecting the presence of TFAM by dot blot (using goat anti-TFAM) and mtDNA by PCR analysis of the D-loop region. Western blot analyses with mouse anti-cytochrome c oxidase subunit IV ( COX IV ), mouse anti-cytochrome c ( Cyt c ), rabbit anti-SOD2, and rabbit anti-HSP60 were carried out to determine the possible presence of protein contaminants. Fractions 6–9 were considered to contain native nucleoids due to the absence of protein contaminants and to the presence of TFAM and mtDNA. PGC-1α and SIRT1 were detected by using Santa Cruz Biotechnology antibodies. Immunoblots reported are from one experiment representative of at least three that gave similar results.
Figure Legend Snippet: Assay of the presence of SIRT1 and PGC-1α in mitochondrial native nucleoids. Native nucleoids were obtained from isolated liver mitochondria as described under “Experimental Procedures.” After sucrose gradient, nucleoid-containing fractions were identified by detecting the presence of TFAM by dot blot (using goat anti-TFAM) and mtDNA by PCR analysis of the D-loop region. Western blot analyses with mouse anti-cytochrome c oxidase subunit IV ( COX IV ), mouse anti-cytochrome c ( Cyt c ), rabbit anti-SOD2, and rabbit anti-HSP60 were carried out to determine the possible presence of protein contaminants. Fractions 6–9 were considered to contain native nucleoids due to the absence of protein contaminants and to the presence of TFAM and mtDNA. PGC-1α and SIRT1 were detected by using Santa Cruz Biotechnology antibodies. Immunoblots reported are from one experiment representative of at least three that gave similar results.

Techniques Used: Pyrolysis Gas Chromatography, Isolation, Dot Blot, Polymerase Chain Reaction, Western Blot

28) Product Images from "Multiple Binding Modes between HNF4? and the LXXLL Motifs of PGC-1? Lead to Full Activation *"

Article Title: Multiple Binding Modes between HNF4? and the LXXLL Motifs of PGC-1? Lead to Full Activation *

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M109.052506

Biochemical and Biological Evidence of Multiple Binding Modes between HNF4α and the LXXLL Motifs of PGC-1α
Figure Legend Snippet: Biochemical and Biological Evidence of Multiple Binding Modes between HNF4α and the LXXLL Motifs of PGC-1α

Techniques Used: Binding Assay, Pyrolysis Gas Chromatography

Schematic drawings and sequence alignments of the HNF4α and PGC-1α functional regions. A, functional domain structure of HNF4α and the sequence alignment of the LBD of NRs whose crystal structures in complex with the PGC-1α
Figure Legend Snippet: Schematic drawings and sequence alignments of the HNF4α and PGC-1α functional regions. A, functional domain structure of HNF4α and the sequence alignment of the LBD of NRs whose crystal structures in complex with the PGC-1α

Techniques Used: Sequencing, Pyrolysis Gas Chromatography, Functional Assay

Measurement of transactivation potential exerted by the PGC-1α mutants compared with the wild-type. The 1st 2 lanes refer to empty vectors ( 1st lane ) or transfected with the HNF4α-expressing vector only ( 2nd lane ). w/o , without; w/ , with;
Figure Legend Snippet: Measurement of transactivation potential exerted by the PGC-1α mutants compared with the wild-type. The 1st 2 lanes refer to empty vectors ( 1st lane ) or transfected with the HNF4α-expressing vector only ( 2nd lane ). w/o , without; w/ , with;

Techniques Used: Pyrolysis Gas Chromatography, Transfection, Expressing, Plasmid Preparation

Set of in vitro binding studies of HNF4α/PGC-1α wild type or mutants. A, GST pulldown with the recombinant proteins of GST-HNF4α-LBD (residues 120–368 containing the hinge region) and the in vitro translated and 35 S-labeled
Figure Legend Snippet: Set of in vitro binding studies of HNF4α/PGC-1α wild type or mutants. A, GST pulldown with the recombinant proteins of GST-HNF4α-LBD (residues 120–368 containing the hinge region) and the in vitro translated and 35 S-labeled

Techniques Used: In Vitro, Binding Assay, Pyrolysis Gas Chromatography, Recombinant, Labeling

Structural evidence of multiple binding modes by PGC-1α toward HNF4α. A, stereo view of 2 F o − F c ( blue mesh ) and F o − F c difference maps ( red mesh ) calculated with the initial model containing a polyalanine model of the
Figure Legend Snippet: Structural evidence of multiple binding modes by PGC-1α toward HNF4α. A, stereo view of 2 F o − F c ( blue mesh ) and F o − F c difference maps ( red mesh ) calculated with the initial model containing a polyalanine model of the

Techniques Used: Binding Assay, Pyrolysis Gas Chromatography

Crystals and the overall structure of HNF4α-PGC-1α complex. A, typical crystals of the complex grown after optimization; B, silver staining of dissolved crystals on SDS-PAGE, which clearly shows the presence of both intact proteins within
Figure Legend Snippet: Crystals and the overall structure of HNF4α-PGC-1α complex. A, typical crystals of the complex grown after optimization; B, silver staining of dissolved crystals on SDS-PAGE, which clearly shows the presence of both intact proteins within

Techniques Used: Pyrolysis Gas Chromatography, Silver Staining, SDS Page

29) Product Images from "Forty high-intensity interval training sessions blunt exercise-induced changes in the nuclear protein content of PGC-1α and p53 in human skeletal muscle"

Article Title: Forty high-intensity interval training sessions blunt exercise-induced changes in the nuclear protein content of PGC-1α and p53 in human skeletal muscle

Journal: bioRxiv

doi: 10.1101/580373

Peroxisome proliferator-activated receptor γ coactivator-1α (PGC-1α) protein. Protein content of PGC-1α in nuclear (a), and cytosolic (b) sub fractions before (Rest), immediately post (+0 h), and 3 h (+3 h) after a single session of high-intensity interval exercise (HIIE) performed at the same absolute intensity before (Pre-HVT) and (Post-HVT) 40 sessions of twice-daily high-volume high-intensity interval training (HVT), in the vastus lateralis muscle of young healthy men (n = 9). Open circles (Pre-HVT) and open diamonds (Post-HVT) represent individual values; white (Pre-HVT) and grey (Post-HVT) bars represent mean values. * P
Figure Legend Snippet: Peroxisome proliferator-activated receptor γ coactivator-1α (PGC-1α) protein. Protein content of PGC-1α in nuclear (a), and cytosolic (b) sub fractions before (Rest), immediately post (+0 h), and 3 h (+3 h) after a single session of high-intensity interval exercise (HIIE) performed at the same absolute intensity before (Pre-HVT) and (Post-HVT) 40 sessions of twice-daily high-volume high-intensity interval training (HVT), in the vastus lateralis muscle of young healthy men (n = 9). Open circles (Pre-HVT) and open diamonds (Post-HVT) represent individual values; white (Pre-HVT) and grey (Post-HVT) bars represent mean values. * P

Techniques Used: Pyrolysis Gas Chromatography

30) Product Images from "Regulation of PGC-1α mediated by acetylation and phosphorylation in MPP+ induced cell model of Parkinson’s disease"

Article Title: Regulation of PGC-1α mediated by acetylation and phosphorylation in MPP+ induced cell model of Parkinson’s disease

Journal: Aging (Albany NY)

doi: 10.18632/aging.103219

The cytosolic rather than the nuclear distribution of PGC-1α regulated by GCN5 in an MPP + -treated cell model. ( A ) The protein levels of GCN5 and PGC-1α; ( B , C ) The cytosolic levels of PGC-1α ( B ) and the nuclear levels of PGC-1α ( C ); ( D ) The relative transcriptional levels of GCN5 and PGC-1α normalized to GAPDH; ( E ) Semi-quantification of total GCN5 and PGC-1α proteins relative to β-actin; ( F , H ) Semi-quantification of the cytosolic ( F ) and the nuclear ( H ) PGC-1α proteins relative to β-actin; ( G , I ) The normalized cytosolic ( G ) and nuclear ( I ) proteins relative to the total protein; n=6, per group. * P
Figure Legend Snippet: The cytosolic rather than the nuclear distribution of PGC-1α regulated by GCN5 in an MPP + -treated cell model. ( A ) The protein levels of GCN5 and PGC-1α; ( B , C ) The cytosolic levels of PGC-1α ( B ) and the nuclear levels of PGC-1α ( C ); ( D ) The relative transcriptional levels of GCN5 and PGC-1α normalized to GAPDH; ( E ) Semi-quantification of total GCN5 and PGC-1α proteins relative to β-actin; ( F , H ) Semi-quantification of the cytosolic ( F ) and the nuclear ( H ) PGC-1α proteins relative to β-actin; ( G , I ) The normalized cytosolic ( G ) and nuclear ( I ) proteins relative to the total protein; n=6, per group. * P

Techniques Used: Pyrolysis Gas Chromatography

31) Product Images from "Mutant p53 controls tumor metabolism and metastasis by regulating PGC-1α"

Article Title: Mutant p53 controls tumor metabolism and metastasis by regulating PGC-1α

Journal: Genes & Development

doi: 10.1101/gad.309062.117

Mutant p53 binds PGC-1α. R72-mut-p53 shows decreased binding compared with P72-mut-p53. ( A ) Pathway analysis of RNA-seq data performed in H1299 cells containing R72-mut-p53 compared with P72-mut-p53 (R175H and R273H). The top-scoring pathways and their P -values are shown. ( B ) Immunoprecipitation-Western blot analysis of mutant p53 with PGC-1α. Input is shown at the left and the amount of mutant p53 immunoprecipitating with PGC-1α is shown at the right for the R175H and R273H mutants. (V) Vector control. The data shown are representative of three independent experiments performed in two independent clones for each mutant for each genotype. ( C ) Immunoprecipitation-Western blot analysis of mutant p53 with PGC-1α in HT-29 (P72-R273H) and SW-620 (R72-R273H). The data depicted are representative of two independent experiments. ( D ) Proximity ligation assay (PLA) in H1299 cells for PGC-1α and mutant p53. (Panels i , ii ) The left panels show PLA signals for PGC-1α mutant p53 interaction in cells containing the R175H and R273H mutants, respectively, and the middle panels show cells with the PLA signals for PGC-1α mutant p53 interaction counterstained with DAPI to detect nuclei. Boxed insets in the middle panels are magnified to show representative results from a single cell. Bar, 20 um. (Panel iii ) Negative control for PLA in H1299 cells expressing the vector. The data shown are representative of three independent experiments performed in two independent clones for each mutant for each genotype. ( E ) Quantification of the average number of PLA signals in H1299 cells expressing the vector control or either P72-mut-p53 or R72-mut-p53. Error bars represent SEM. n = 10 cells per group, counted from two independent experiments.
Figure Legend Snippet: Mutant p53 binds PGC-1α. R72-mut-p53 shows decreased binding compared with P72-mut-p53. ( A ) Pathway analysis of RNA-seq data performed in H1299 cells containing R72-mut-p53 compared with P72-mut-p53 (R175H and R273H). The top-scoring pathways and their P -values are shown. ( B ) Immunoprecipitation-Western blot analysis of mutant p53 with PGC-1α. Input is shown at the left and the amount of mutant p53 immunoprecipitating with PGC-1α is shown at the right for the R175H and R273H mutants. (V) Vector control. The data shown are representative of three independent experiments performed in two independent clones for each mutant for each genotype. ( C ) Immunoprecipitation-Western blot analysis of mutant p53 with PGC-1α in HT-29 (P72-R273H) and SW-620 (R72-R273H). The data depicted are representative of two independent experiments. ( D ) Proximity ligation assay (PLA) in H1299 cells for PGC-1α and mutant p53. (Panels i , ii ) The left panels show PLA signals for PGC-1α mutant p53 interaction in cells containing the R175H and R273H mutants, respectively, and the middle panels show cells with the PLA signals for PGC-1α mutant p53 interaction counterstained with DAPI to detect nuclei. Boxed insets in the middle panels are magnified to show representative results from a single cell. Bar, 20 um. (Panel iii ) Negative control for PLA in H1299 cells expressing the vector. The data shown are representative of three independent experiments performed in two independent clones for each mutant for each genotype. ( E ) Quantification of the average number of PLA signals in H1299 cells expressing the vector control or either P72-mut-p53 or R72-mut-p53. Error bars represent SEM. n = 10 cells per group, counted from two independent experiments.

Techniques Used: Mutagenesis, Pyrolysis Gas Chromatography, Binding Assay, RNA Sequencing Assay, Immunoprecipitation, Western Blot, Plasmid Preparation, Clone Assay, Proximity Ligation Assay, Negative Control, Expressing

Increased PGC-1α target genes in tumors cells with R72-mut-p53; silencing PGC-1α eliminates the invasiveness differences between P72-mut-p53 and R72-mut-p53. ( A ) qRT–PCR analysis of mRNA levels of PGC-1α downstream target genes associated with anti-oxidant function ( CATALASE , GPX4 , and SOD2 ), transcription ( ERR α), and the mitochondria electron transport chain ( ATP5g1 and NDUFS3) in H1299 cells containing vector or mutant p53 in cis with P72 or R72. Studies in two replicates were performed in quadruplicate. Error bars mark SD. (*) P
Figure Legend Snippet: Increased PGC-1α target genes in tumors cells with R72-mut-p53; silencing PGC-1α eliminates the invasiveness differences between P72-mut-p53 and R72-mut-p53. ( A ) qRT–PCR analysis of mRNA levels of PGC-1α downstream target genes associated with anti-oxidant function ( CATALASE , GPX4 , and SOD2 ), transcription ( ERR α), and the mitochondria electron transport chain ( ATP5g1 and NDUFS3) in H1299 cells containing vector or mutant p53 in cis with P72 or R72. Studies in two replicates were performed in quadruplicate. Error bars mark SD. (*) P

Techniques Used: Pyrolysis Gas Chromatography, Quantitative RT-PCR, Plasmid Preparation, Mutagenesis

Poorer survival in breast cancer patients with R72-mut-p53. ( A ) Kaplan-Meier survival curves depicting survival data in patients with breast cancer in the presence of both copies of arginine (R72/R72) at codon 72 of mutant p53 (pink line) compared with patients who possess at least one copy of P72 (orange line). Patients with wild-type p53 and one copy of P72 are denoted by the blue line, and patients with wild-type p53 and both copies of R72 are denoted by the green line. ( B ) Proposed model of how mutant p53 modulates PGC-1α function to drive cancer cell migration and invasion. P72-mut-p53 is associated with suppressed PGC-1α activity and reduced oxidative phosphorylation (OXPHOS). Cells containing R72-mut-p53 show increased complex formation of transcription factors (TF) such as HNF4α and PGC-1α and increased mitochondrial function along with increased invasion and metastasis.
Figure Legend Snippet: Poorer survival in breast cancer patients with R72-mut-p53. ( A ) Kaplan-Meier survival curves depicting survival data in patients with breast cancer in the presence of both copies of arginine (R72/R72) at codon 72 of mutant p53 (pink line) compared with patients who possess at least one copy of P72 (orange line). Patients with wild-type p53 and one copy of P72 are denoted by the blue line, and patients with wild-type p53 and both copies of R72 are denoted by the green line. ( B ) Proposed model of how mutant p53 modulates PGC-1α function to drive cancer cell migration and invasion. P72-mut-p53 is associated with suppressed PGC-1α activity and reduced oxidative phosphorylation (OXPHOS). Cells containing R72-mut-p53 show increased complex formation of transcription factors (TF) such as HNF4α and PGC-1α and increased mitochondrial function along with increased invasion and metastasis.

Techniques Used: Mutagenesis, Pyrolysis Gas Chromatography, Migration, Activity Assay

HNF4α signature is enhanced in cells with R72-mut-p53. ( A ) Expression heat map for genes significantly correlated with the percentage of R72 (as per RNA-seq reads) in patients with p53 missense mutations. n = 161. Analysis of upstream regulators revealed HNF4α as a top hit with the highest significant number of known targets (131) in the list. P = 0.0008. ( B ) PLA in colon cancer cells for PGC-1α and HNF4α. The top and bottom panels show PLA signals for PGC-1α and HNF4α interaction in HT-29 cells and SW-620 cells containing the R273H mutation in p53, respectively. ( C ) Quantification of the number of PLA signals in HT-29 and SW-620 cells. Error bars show SEM. (**) P
Figure Legend Snippet: HNF4α signature is enhanced in cells with R72-mut-p53. ( A ) Expression heat map for genes significantly correlated with the percentage of R72 (as per RNA-seq reads) in patients with p53 missense mutations. n = 161. Analysis of upstream regulators revealed HNF4α as a top hit with the highest significant number of known targets (131) in the list. P = 0.0008. ( B ) PLA in colon cancer cells for PGC-1α and HNF4α. The top and bottom panels show PLA signals for PGC-1α and HNF4α interaction in HT-29 cells and SW-620 cells containing the R273H mutation in p53, respectively. ( C ) Quantification of the number of PLA signals in HT-29 and SW-620 cells. Error bars show SEM. (**) P

Techniques Used: Expressing, RNA Sequencing Assay, Proximity Ligation Assay, Pyrolysis Gas Chromatography, Mutagenesis

32) Product Images from "Bitter melon extract attenuating hepatic steatosis may be mediated by FGF21 and AMPK/Sirt1 signaling in mice"

Article Title: Bitter melon extract attenuating hepatic steatosis may be mediated by FGF21 and AMPK/Sirt1 signaling in mice

Journal: Scientific Reports

doi: 10.1038/srep03142

The effects of BM extracts on fasting plasma and liver FGF21 levels as well as FGF21 signaling in mice. FGF21 was measured using a mouse FGF21 ELISA kit from R D Systems Inc (Minneapolis, MN). (A) Fasting plasma FGF21 concentrations. (B) Liver FGF21 content. Mean ± SEM (n = 10/group). (C) FGF21 signaling proteins were measured by Western blotting assay. Results were normalized by β-actin content. BM-V significantly increased FGFR1, FGFR3, FGFR4 and PGC-1α, slightly reduced PPARα, but did not affect b-Klotho protein abundance in comparison with HFD animals. Mean ± SEM (n = 10/group). * P
Figure Legend Snippet: The effects of BM extracts on fasting plasma and liver FGF21 levels as well as FGF21 signaling in mice. FGF21 was measured using a mouse FGF21 ELISA kit from R D Systems Inc (Minneapolis, MN). (A) Fasting plasma FGF21 concentrations. (B) Liver FGF21 content. Mean ± SEM (n = 10/group). (C) FGF21 signaling proteins were measured by Western blotting assay. Results were normalized by β-actin content. BM-V significantly increased FGFR1, FGFR3, FGFR4 and PGC-1α, slightly reduced PPARα, but did not affect b-Klotho protein abundance in comparison with HFD animals. Mean ± SEM (n = 10/group). * P

Techniques Used: Mouse Assay, Enzyme-linked Immunosorbent Assay, Western Blot, Pyrolysis Gas Chromatography

33) Product Images from "Enhanced longevity and metabolism by brown adipose tissue with disruption of the regulator of G protein signaling 14, et al. Enhanced longevity and metabolism by brown adipose tissue with disruption of the regulator of G protein signaling 14"

Article Title: Enhanced longevity and metabolism by brown adipose tissue with disruption of the regulator of G protein signaling 14, et al. Enhanced longevity and metabolism by brown adipose tissue with disruption of the regulator of G protein signaling 14

Journal: Aging Cell

doi: 10.1111/acel.12751

BAT mediates energy metabolism. (a) Oxidative phosphorylation (OXPHOS) capacity was increased in BAT from RGS14 KO vs. BAT from WT as reflected by increased CIL: Complex I leak respiration; CIP: OXPHOS capacity of Complex I; CI CIIP: OXPHOS capacity of Complex I II; and CIP: OXPHOS capacity of Complex II. (b) PGC‐1α, a key regulator of mitochondrial biogenesis, was increased at the protein level in the BAT of the RGS14 KO mice ( n = 3/group). (c) SIRT3 protein levels were increased in BAT of RGS14 KO mice ( n = 3/group). (d) Increased mitochondrial DNA/nuclear DNA ratio was found in BAT of RGS14 KO ( n = 5/group). The data comparing BAT transplants and recipients are shown and demonstrate that WT BAT recipients gained the protective features of RGS14 KO and RGS14 KO lost these protective features (e–g). (e) Oxygen consumption was increased in BAT recipients compared to BAT donors ( n = 4/group). (f) Thermogenic protection was lost in BAT donors and gained in BAT recipients ( n = 10/group). (g) The area above the curve was significantly greater in BAT recipients than in BAT donors. Results are expressed as mean ± SEM . Statistical significance was determined by the use of a Student's t test. * p
Figure Legend Snippet: BAT mediates energy metabolism. (a) Oxidative phosphorylation (OXPHOS) capacity was increased in BAT from RGS14 KO vs. BAT from WT as reflected by increased CIL: Complex I leak respiration; CIP: OXPHOS capacity of Complex I; CI CIIP: OXPHOS capacity of Complex I II; and CIP: OXPHOS capacity of Complex II. (b) PGC‐1α, a key regulator of mitochondrial biogenesis, was increased at the protein level in the BAT of the RGS14 KO mice ( n = 3/group). (c) SIRT3 protein levels were increased in BAT of RGS14 KO mice ( n = 3/group). (d) Increased mitochondrial DNA/nuclear DNA ratio was found in BAT of RGS14 KO ( n = 5/group). The data comparing BAT transplants and recipients are shown and demonstrate that WT BAT recipients gained the protective features of RGS14 KO and RGS14 KO lost these protective features (e–g). (e) Oxygen consumption was increased in BAT recipients compared to BAT donors ( n = 4/group). (f) Thermogenic protection was lost in BAT donors and gained in BAT recipients ( n = 10/group). (g) The area above the curve was significantly greater in BAT recipients than in BAT donors. Results are expressed as mean ± SEM . Statistical significance was determined by the use of a Student's t test. * p

Techniques Used: Pyrolysis Gas Chromatography, Mouse Assay

Increased NAD + /NADH ratio in RGS14 KO in skeletal muscle. (a) Both the absolute level of NAD + and NAD + /NADH ratio were elevated in the RGS14 KO mice ( n = 4/group). (b) CD38, a mechanism for changes in NAD + , was reduced in RGS14 KO skeletal muscle, further confirmed in the increased NAD + level ( n = 6–7/group). (c) Increase in mitochondrial DNA content in skeletal muscle was measured by mitochondrial DNA/nuclear DNA ratio ( n = 5/group). (d) Complex I activity in skeletal muscle was significantly increased in RGS14 KO animals ( n = 7/group). (e) PGC‐1α, a key regulator of mitochondrial biogenesis, was increased at the protein level in the BAT of the RGS14 KO mice ( n = 3/group). Results are expressed as mean ± SEM . Statistical significance was determined by Student's t test * p
Figure Legend Snippet: Increased NAD + /NADH ratio in RGS14 KO in skeletal muscle. (a) Both the absolute level of NAD + and NAD + /NADH ratio were elevated in the RGS14 KO mice ( n = 4/group). (b) CD38, a mechanism for changes in NAD + , was reduced in RGS14 KO skeletal muscle, further confirmed in the increased NAD + level ( n = 6–7/group). (c) Increase in mitochondrial DNA content in skeletal muscle was measured by mitochondrial DNA/nuclear DNA ratio ( n = 5/group). (d) Complex I activity in skeletal muscle was significantly increased in RGS14 KO animals ( n = 7/group). (e) PGC‐1α, a key regulator of mitochondrial biogenesis, was increased at the protein level in the BAT of the RGS14 KO mice ( n = 3/group). Results are expressed as mean ± SEM . Statistical significance was determined by Student's t test * p

Techniques Used: Mouse Assay, Activity Assay, Pyrolysis Gas Chromatography

34) Product Images from "Cardiac lipin 1 expression is regulated by the peroxisome proliferator activated receptor ? coactivator 1?/estrogen related receptor axis"

Article Title: Cardiac lipin 1 expression is regulated by the peroxisome proliferator activated receptor ? coactivator 1?/estrogen related receptor axis

Journal: Journal of molecular and cellular cardiology

doi: 10.1016/j.yjmcc.2011.04.009

PGC-1α induces Lpin1 gene expression in NRVMs through an intronic promoter element. A. RT-PCR analyses to quantify lipin 1 in mRNA isolated from NRVM infected with Ad-GFP and Ad-PGC-1α (n=6). Values are normalized (=1.0) to Ad-GFP. B.
Figure Legend Snippet: PGC-1α induces Lpin1 gene expression in NRVMs through an intronic promoter element. A. RT-PCR analyses to quantify lipin 1 in mRNA isolated from NRVM infected with Ad-GFP and Ad-PGC-1α (n=6). Values are normalized (=1.0) to Ad-GFP. B.

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Reverse Transcription Polymerase Chain Reaction, Isolation, Infection

ERRs regulate lipin 1 expression and are required for the induction in lipin 1 expression after PGC-1α overexpression. A. RT-PCR analyses to quantify lipin 1 in mRNA isolated from NRVM infected with Ad-GFP, Ad-ERRα, or Ad-ERRγ
Figure Legend Snippet: ERRs regulate lipin 1 expression and are required for the induction in lipin 1 expression after PGC-1α overexpression. A. RT-PCR analyses to quantify lipin 1 in mRNA isolated from NRVM infected with Ad-GFP, Ad-ERRα, or Ad-ERRγ

Techniques Used: Expressing, Pyrolysis Gas Chromatography, Over Expression, Reverse Transcription Polymerase Chain Reaction, Isolation, Infection

Cardiac lipin 1 is a PGC-1α target gene in the intact mouse heart. A. Results of RT-PCR and Western blot analyses to quantify PGC-1α, ERRα, ERRγ, and lipin 1 mRNA and protein in cardiac tissue from control NTG and Tet-ON
Figure Legend Snippet: Cardiac lipin 1 is a PGC-1α target gene in the intact mouse heart. A. Results of RT-PCR and Western blot analyses to quantify PGC-1α, ERRα, ERRγ, and lipin 1 mRNA and protein in cardiac tissue from control NTG and Tet-ON

Techniques Used: Pyrolysis Gas Chromatography, Reverse Transcription Polymerase Chain Reaction, Western Blot

Cardiac lipin 1 expression is induced by β2-adrenergic agonism in a PGC-1α dependent manner. A. Results of RT-PCR analyses for PGC-1α and lipin 1 in mRNA isolated from cardiac tissues harvested from mice treated with PBS, dobutamine,
Figure Legend Snippet: Cardiac lipin 1 expression is induced by β2-adrenergic agonism in a PGC-1α dependent manner. A. Results of RT-PCR analyses for PGC-1α and lipin 1 in mRNA isolated from cardiac tissues harvested from mice treated with PBS, dobutamine,

Techniques Used: Expressing, Pyrolysis Gas Chromatography, Reverse Transcription Polymerase Chain Reaction, Isolation, Mouse Assay

Schematic representation of cardiac Lpin1 transcriptional regulation by PGC-1α, ERRα, and ERRγ by pathologic cardiac hypertrophy and β-adrenergic agonism.
Figure Legend Snippet: Schematic representation of cardiac Lpin1 transcriptional regulation by PGC-1α, ERRα, and ERRγ by pathologic cardiac hypertrophy and β-adrenergic agonism.

Techniques Used: Pyrolysis Gas Chromatography

35) Product Images from "Chronic AMPK activation via loss of FLCN induces functional beige adipose tissue through PGC-1α/ERRα"

Article Title: Chronic AMPK activation via loss of FLCN induces functional beige adipose tissue through PGC-1α/ERRα

Journal: Genes & Development

doi: 10.1101/gad.281410.116

FLCN repression up-regulates an AMPK/PGC-1α/ERRα molecular axis, promoting metabolic reprogramming and WAT browning. ( A , B ) Western blot analysis performed with the indicated antibodies on iWAT ( A ) and BAT ( B ) of 4-mo-old mice fed either chow or a HFD. Relative expression of mRNA transcripts encoding PGC-1α ( Ppargc1a ) and ERRα ( Esrra ) ( C ) as well as mRNA levels of mitochondrial associated genes ( D ) in iWAT and BAT of wild-type and Adipoq-FLCN knockout mice are shown. ( E ) Adipose tissue mitochondrial content was determined by the ratio of mtDNA:nDNA. Quantitative RT–PCR (qRT–PCR) analysis of genes related to lipid metabolism ( F ) and thermogenesis ( G ) in iWAT and BAT of wild-type and Adipoq-FLCN knockout mice. ( H ) UCP1 protein levels in BAT of wild-type and Adipoq-FLCN-null mice fed chow or a HFD. Tubulin levels are shown as a loading control. Data in C–G are presented as mean ± SEM. n = 8–10 mice per group. (*) P
Figure Legend Snippet: FLCN repression up-regulates an AMPK/PGC-1α/ERRα molecular axis, promoting metabolic reprogramming and WAT browning. ( A , B ) Western blot analysis performed with the indicated antibodies on iWAT ( A ) and BAT ( B ) of 4-mo-old mice fed either chow or a HFD. Relative expression of mRNA transcripts encoding PGC-1α ( Ppargc1a ) and ERRα ( Esrra ) ( C ) as well as mRNA levels of mitochondrial associated genes ( D ) in iWAT and BAT of wild-type and Adipoq-FLCN knockout mice are shown. ( E ) Adipose tissue mitochondrial content was determined by the ratio of mtDNA:nDNA. Quantitative RT–PCR (qRT–PCR) analysis of genes related to lipid metabolism ( F ) and thermogenesis ( G ) in iWAT and BAT of wild-type and Adipoq-FLCN knockout mice. ( H ) UCP1 protein levels in BAT of wild-type and Adipoq-FLCN-null mice fed chow or a HFD. Tubulin levels are shown as a loading control. Data in C–G are presented as mean ± SEM. n = 8–10 mice per group. (*) P

Techniques Used: Pyrolysis Gas Chromatography, Western Blot, Mouse Assay, Expressing, Knock-Out, Quantitative RT-PCR

PGC-1α/ERRα expression/activity and mitochondrial respiration are induced upon loss of FLCN in an AMPK-dependent manner. ( A ) Western blot analysis of the indicated proteins is shown in wild-type and FLCN-null MEFs. ( B ) Transcript levels of Ppargc1a , Esrra , and genes related to mitochondrial activity in FLCN wild-type or knockout MEFs are shown. ( C ) PGC-1/ERR activity assessed using an ERRE luciferase reporter assay in MEFs expressing FLCN or not. ( D ) Relative fold enrichments of ERRα binding to metabolic target genes by ChIP-qPCR in wild-type or FLCN knockout MEFs. n = 3. ( E ) Extracellular OCR profiles following addition of the indicated mitochondrial perturbing drugs in FLCN wild-type or knockout MEFs. (Oligo) Oligomycin. ( F , left ) Etomoxir, an inhibitor of FAO, abolished the induced OCR levels in FLCN-null MEFs. ( Right ) Western blot analysis of FLCN protein levels in wild-type and FLCN knockout MEFs. β-Actin levels are shown as a loading control. ( G ) Extracellular OCR profiles following addition of the indicated mitochondrial perturbing drugs in FLCN wild-type or knockout MEFs treated with siRNAs against ERRα (siERRα) or control (siC). (Oligo) Oligomycin. ( H , left ) The increased OCR in FLCN knockout MEFs was lost when ERRα expression was inhibited. ( Right ) Western blot analysis of FLCN and ERRα protein levels in the wild-type or FLCN MEFs treated with or without siERRα or siC. β-Actin levels are shown as a loading control. ( I ) Western blot analysis of the indicated proteins are shown in wild-type and AMPKα-null MEFs treated with shRNAs against FLCN (shFlcn) or control (shEV). ( J ) Transcript levels of Ppargc1a , Esrra , and genes related to FAO and thermogenesis in AMPKα wild-type and knockout MEFs treated with or without shFlcn. ( K ) Loss of AMPKα in MEFs abolished the increased recruitment of ERRα to metabolic target genes following FLCN repression as determined by ChIP-qPCR analyses. n = 3. Data in B , C , E – H , and J are presented as mean ± SEM taken from at least three independent experiments. (*) P
Figure Legend Snippet: PGC-1α/ERRα expression/activity and mitochondrial respiration are induced upon loss of FLCN in an AMPK-dependent manner. ( A ) Western blot analysis of the indicated proteins is shown in wild-type and FLCN-null MEFs. ( B ) Transcript levels of Ppargc1a , Esrra , and genes related to mitochondrial activity in FLCN wild-type or knockout MEFs are shown. ( C ) PGC-1/ERR activity assessed using an ERRE luciferase reporter assay in MEFs expressing FLCN or not. ( D ) Relative fold enrichments of ERRα binding to metabolic target genes by ChIP-qPCR in wild-type or FLCN knockout MEFs. n = 3. ( E ) Extracellular OCR profiles following addition of the indicated mitochondrial perturbing drugs in FLCN wild-type or knockout MEFs. (Oligo) Oligomycin. ( F , left ) Etomoxir, an inhibitor of FAO, abolished the induced OCR levels in FLCN-null MEFs. ( Right ) Western blot analysis of FLCN protein levels in wild-type and FLCN knockout MEFs. β-Actin levels are shown as a loading control. ( G ) Extracellular OCR profiles following addition of the indicated mitochondrial perturbing drugs in FLCN wild-type or knockout MEFs treated with siRNAs against ERRα (siERRα) or control (siC). (Oligo) Oligomycin. ( H , left ) The increased OCR in FLCN knockout MEFs was lost when ERRα expression was inhibited. ( Right ) Western blot analysis of FLCN and ERRα protein levels in the wild-type or FLCN MEFs treated with or without siERRα or siC. β-Actin levels are shown as a loading control. ( I ) Western blot analysis of the indicated proteins are shown in wild-type and AMPKα-null MEFs treated with shRNAs against FLCN (shFlcn) or control (shEV). ( J ) Transcript levels of Ppargc1a , Esrra , and genes related to FAO and thermogenesis in AMPKα wild-type and knockout MEFs treated with or without shFlcn. ( K ) Loss of AMPKα in MEFs abolished the increased recruitment of ERRα to metabolic target genes following FLCN repression as determined by ChIP-qPCR analyses. n = 3. Data in B , C , E – H , and J are presented as mean ± SEM taken from at least three independent experiments. (*) P

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Activity Assay, Western Blot, Knock-Out, Luciferase, Reporter Assay, Binding Assay, Chromatin Immunoprecipitation, Real-time Polymerase Chain Reaction

36) Product Images from "Sustained kidney biochemical derangement in treated experimental diabetes: a clue to metabolic memory"

Article Title: Sustained kidney biochemical derangement in treated experimental diabetes: a clue to metabolic memory

Journal: Scientific Reports

doi: 10.1038/srep40544

Levels of PGC-1α, fumarate, and mitochondrial DNA methylation and hydroxymethylation are changed during 12 weeks of diabetes and are not normalized after late glycemic control. ( a , b and c ) Kidney PGC-1α expression after eight, 12, and 24 weeks and representative immunoblots. ( d , e and f ) Fumarate levels in kidney tissue after eight, 12, and 24 weeks. ( g , h and i ) Percentage of 5-methylcytosine (5-mC) and ( j , k and l ) percentage of 5-hydroxymethylcytosine (5-hmC) in mitochondrial DNA after eight, 12, and 24 weeks. The data are expressed as the means ± SEM. *p
Figure Legend Snippet: Levels of PGC-1α, fumarate, and mitochondrial DNA methylation and hydroxymethylation are changed during 12 weeks of diabetes and are not normalized after late glycemic control. ( a , b and c ) Kidney PGC-1α expression after eight, 12, and 24 weeks and representative immunoblots. ( d , e and f ) Fumarate levels in kidney tissue after eight, 12, and 24 weeks. ( g , h and i ) Percentage of 5-methylcytosine (5-mC) and ( j , k and l ) percentage of 5-hydroxymethylcytosine (5-hmC) in mitochondrial DNA after eight, 12, and 24 weeks. The data are expressed as the means ± SEM. *p

Techniques Used: Pyrolysis Gas Chromatography, DNA Methylation Assay, Expressing, Western Blot

37) Product Images from "Changes in skeletal muscle mitochondria in response to the development of type 2 diabetes or prevention by daily wheel running in hyperphagic OLETF rats"

Article Title: Changes in skeletal muscle mitochondria in response to the development of type 2 diabetes or prevention by daily wheel running in hyperphagic OLETF rats

Journal: American Journal of Physiology - Endocrinology and Metabolism

doi: 10.1152/ajpendo.00703.2009

Changes in silent SIRT1 ( A ), PGC-1α ( B ), cytochrome c ( C ), and cytochrome c oxidase IV (COX-IV)-subunit I protein content ( D ) in the RG muscle. Values are means ± SE ( n = 5–8). #Significant difference between 20- and 40-wk values
Figure Legend Snippet: Changes in silent SIRT1 ( A ), PGC-1α ( B ), cytochrome c ( C ), and cytochrome c oxidase IV (COX-IV)-subunit I protein content ( D ) in the RG muscle. Values are means ± SE ( n = 5–8). #Significant difference between 20- and 40-wk values

Techniques Used: Pyrolysis Gas Chromatography

38) Product Images from "Metformin induces PGC-1α expression and selectively affects hepatic PGC-1α functions"

Article Title: Metformin induces PGC-1α expression and selectively affects hepatic PGC-1α functions

Journal: British Journal of Pharmacology

doi: 10.1111/bph.12585

A proposed model for the effect of metformin on hepatic PGC-1α regulation and function. We propose that metformin activates PGC-1α gene transcription through AMPK and SIRT1. However, metformin represses the increase in PGC-1α induced
Figure Legend Snippet: A proposed model for the effect of metformin on hepatic PGC-1α regulation and function. We propose that metformin activates PGC-1α gene transcription through AMPK and SIRT1. However, metformin represses the increase in PGC-1α induced

Techniques Used: Pyrolysis Gas Chromatography

Effect of metformin on acetylation of PGC-1α and genes regulating PEPCK and G6Pase. (A) HepG2 cells were transfected with PGC-1α-FLAG plasmid and 24 h post transfection treated with 2 mM metformin for 72 h after
Figure Legend Snippet: Effect of metformin on acetylation of PGC-1α and genes regulating PEPCK and G6Pase. (A) HepG2 cells were transfected with PGC-1α-FLAG plasmid and 24 h post transfection treated with 2 mM metformin for 72 h after

Techniques Used: Pyrolysis Gas Chromatography, Transfection, Plasmid Preparation

Effect of metformin treatment on PGC-1α and gluconeogenic gene expression. (A) Mouse primary hepatocytes were treated with metformin for 48 h after which mRNAs were measured by RT-qPCR ( n = 3). (B) Mouse primary hepatocytes were treated
Figure Legend Snippet: Effect of metformin treatment on PGC-1α and gluconeogenic gene expression. (A) Mouse primary hepatocytes were treated with metformin for 48 h after which mRNAs were measured by RT-qPCR ( n = 3). (B) Mouse primary hepatocytes were treated

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Quantitative RT-PCR

The functional effect of metformin on gluconeogenesis and selected mitochondrial-acting genes. Mouse primary hepatocytes were infected with PGC-1α-Ad at MOI 1 for 24 h after which 1 mM metformin was added. After 48 h cells
Figure Legend Snippet: The functional effect of metformin on gluconeogenesis and selected mitochondrial-acting genes. Mouse primary hepatocytes were infected with PGC-1α-Ad at MOI 1 for 24 h after which 1 mM metformin was added. After 48 h cells

Techniques Used: Functional Assay, Infection, Pyrolysis Gas Chromatography

Effect of metformin and cAMP on PGC-1α mRNA expression and promoter activity. (A) Mouse primary hepatocytes were treated with 1 mM metformin or 25 μM db-cAMP alone or combined for 2 and 24 h after which mRNA expressions
Figure Legend Snippet: Effect of metformin and cAMP on PGC-1α mRNA expression and promoter activity. (A) Mouse primary hepatocytes were treated with 1 mM metformin or 25 μM db-cAMP alone or combined for 2 and 24 h after which mRNA expressions

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Activity Assay

AMPK modulators and AMPK overexpression affect mouse PGC-1α expression level. (A) Mouse primary hepatocytes were treated with 1 mM metformin or 1 mM AICAR for 12, 24, 48 and 72 h after which mRNAs were analysed by RT-qPCR
Figure Legend Snippet: AMPK modulators and AMPK overexpression affect mouse PGC-1α expression level. (A) Mouse primary hepatocytes were treated with 1 mM metformin or 1 mM AICAR for 12, 24, 48 and 72 h after which mRNAs were analysed by RT-qPCR

Techniques Used: Over Expression, Pyrolysis Gas Chromatography, Expressing, Quantitative RT-PCR

39) Product Images from "PGC-1? rescues Huntington's disease proteotoxicity by preventing oxidative stress and promoting TFEB function"

Article Title: PGC-1? rescues Huntington's disease proteotoxicity by preventing oxidative stress and promoting TFEB function

Journal: Science translational medicine

doi: 10.1126/scitranslmed.3003799

PGC-1α expression counters htt protein aggregate formation induced by oxidative stress
Figure Legend Snippet: PGC-1α expression counters htt protein aggregate formation induced by oxidative stress

Techniques Used: Pyrolysis Gas Chromatography, Expressing

PGC-1α promotes TFEB target gene induction and TFEB-mediated htt aggregate reduction
Figure Legend Snippet: PGC-1α promotes TFEB target gene induction and TFEB-mediated htt aggregate reduction

Techniques Used: Pyrolysis Gas Chromatography

PGC-1α expression prevents htt aggregate formation and rescues HD neurodegeneration
Figure Legend Snippet: PGC-1α expression prevents htt aggregate formation and rescues HD neurodegeneration

Techniques Used: Pyrolysis Gas Chromatography, Expressing

PGC-1α expression restores mitochondrial function in HD transgenic mice
Figure Legend Snippet: PGC-1α expression restores mitochondrial function in HD transgenic mice

Techniques Used: Pyrolysis Gas Chromatography, Expressing, Transgenic Assay, Mouse Assay

PGC-1α expression protects against HD oxidative damage by inducing reactive oxygen species defense genes
Figure Legend Snippet: PGC-1α expression protects against HD oxidative damage by inducing reactive oxygen species defense genes

Techniques Used: Pyrolysis Gas Chromatography, Expressing

PolyQ-expanded htt interferes with PGC-1α transactivation of TFEB expression
Figure Legend Snippet: PolyQ-expanded htt interferes with PGC-1α transactivation of TFEB expression

Techniques Used: Pyrolysis Gas Chromatography, Expressing

PGC-1α expression rescues HD neurological phenotypes
Figure Legend Snippet: PGC-1α expression rescues HD neurological phenotypes

Techniques Used: Pyrolysis Gas Chromatography, Expressing

40) Product Images from "Effects of Nitric Oxide Synthase Inhibition on Fiber-Type Composition, Mitochondrial Biogenesis, and SIRT1 Expression in Rat Skeletal Muscle"

Article Title: Effects of Nitric Oxide Synthase Inhibition on Fiber-Type Composition, Mitochondrial Biogenesis, and SIRT1 Expression in Rat Skeletal Muscle

Journal: Journal of Sports Science & Medicine

doi:

Expression levels of SIRT1 (a) and PGC-1α (b) proteins in the soleus and plantaris muscles in the control (open columns) and L-NAME-treated (filled columns) groups. Values represent means ± SE; n = 10 muscles per group. * P
Figure Legend Snippet: Expression levels of SIRT1 (a) and PGC-1α (b) proteins in the soleus and plantaris muscles in the control (open columns) and L-NAME-treated (filled columns) groups. Values represent means ± SE; n = 10 muscles per group. * P

Techniques Used: Expressing, Pyrolysis Gas Chromatography

Related Articles

Chromatin Immunoprecipitation:

Article Title: Ribosomal transcription is regulated by PGC-1alpha and disturbed in Huntington’s disease
Article Snippet: .. Antibodies PGC1a mouse monoclonal (4C1.3), Calbiochem/ST1202, raised against aa 1–120 of mPGC-1α (ChIP); PGC-1α rabbit polyclonal, Millipore/AB3242 raised against aa777–797 of mPGC-1α (IF); Nucleolin C23 (F-18) goat polyclonal, Santa Cruz/sc9893; Immunoglobulin G, mouse Santa Cruz/sc-3877; RNA-Polymerase I, Lebedev et al . .. 2008; Anti-FLAG M2, Sigma A2220 (IP); Acetyl-lysine mouse monoclonal, Acris/AM33097PU-S.

Pyrolysis Gas Chromatography:

Article Title: The effect of acute and chronic sprint‐interval training on LRP130, SIRT3, and PGC‐1α expression in human skeletal muscle. The effect of acute and chronic sprint‐interval training on LRP130, SIRT3, and PGC‐1α expression in human skeletal muscle
Article Snippet: .. Commercially available antibodies were used to detect SIRT3 (Cell Signaling, Danvers, MA; #4590, lot# 2), LRP130 (Abcam, Cambridge, UK; ab97505, lot# GR40843‐18), and PGC‐1α (EMD Millipore, Darmstadt, Germany; AB3242, lot# J0510). .. All primary antibodies were used at a concentration of 1:1000 and diluted in 5% BSA with TBS‐T.

Article Title: Ribosomal transcription is regulated by PGC-1alpha and disturbed in Huntington’s disease
Article Snippet: .. Antibodies PGC1a mouse monoclonal (4C1.3), Calbiochem/ST1202, raised against aa 1–120 of mPGC-1α (ChIP); PGC-1α rabbit polyclonal, Millipore/AB3242 raised against aa777–797 of mPGC-1α (IF); Nucleolin C23 (F-18) goat polyclonal, Santa Cruz/sc9893; Immunoglobulin G, mouse Santa Cruz/sc-3877; RNA-Polymerase I, Lebedev et al . .. 2008; Anti-FLAG M2, Sigma A2220 (IP); Acetyl-lysine mouse monoclonal, Acris/AM33097PU-S.

Article Title: Potential roles of PINK1 for increased PGC-1α-mediated mitochondrial fatty acid oxidation and their associations with Alzheimer disease and diabetes
Article Snippet: .. Primary antibodies used included rabbit PGC-1α (1:5000) , anti-actin (1:2000; MAB1501R; Millipore, Billerica, MA, U.S.A.), anti-HSP 60 (1:1000, Cell Signaling, 4870), and anti-PINK1 (1:1000; LS-B3384; LSBio, Seattle, WA, U.S.A.). .. Horseradish peroxidase-conjugated secondary antibodies were purchased from Pierce Biotechnology.

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  • 95
    Millipore pgc 1α
    Quercetin promoted translocation of <t>PGC‐1α</t> from cytoplasm to nucleus and enhanced PGC‐1α binding. ( A‐D ) The representative photomicrographs showing PGC‐1α immunohistochemistry of tissue from different group 24 hrs after TBI. ( E, H ) The nuclear PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( F, I ) The cytoplasmic protein PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( G, J ) The total protein PGC‐1α expression after melatonin treatment in mice with TBI, as measured by Western blot. Bars represent the mean ± S.E.M. * P
    Pgc 1α, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 177 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore pgc 1α protein
    Skeletal muscle glycogen content and blood lactate concentration before and after exercise. <t>PGC-1α-b</t> transgenic mice and wild-type littermates (Wt) (each 8 weeks old) were exercised by forced running on a treadmill at 10 m/min. The speed increased 2 m/min every 3 min up to 30 m/min. Mice ran for 30 min. Skeletal muscle (gastrocnemius) glycogen content was measured before (Sed) and after 30 min of exercise (n = 3–5). Values are means ± SE. ** P
    Pgc 1α Protein, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgc 1α protein/product/Millipore
    Average 85 stars, based on 3 article reviews
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    Quercetin promoted translocation of PGC‐1α from cytoplasm to nucleus and enhanced PGC‐1α binding. ( A‐D ) The representative photomicrographs showing PGC‐1α immunohistochemistry of tissue from different group 24 hrs after TBI. ( E, H ) The nuclear PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( F, I ) The cytoplasmic protein PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( G, J ) The total protein PGC‐1α expression after melatonin treatment in mice with TBI, as measured by Western blot. Bars represent the mean ± S.E.M. * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Neuroprotection by quercetin via mitochondrial function adaptation in traumatic brain injury: PGC‐1α pathway as a potential mechanism

    doi: 10.1111/jcmm.13313

    Figure Lengend Snippet: Quercetin promoted translocation of PGC‐1α from cytoplasm to nucleus and enhanced PGC‐1α binding. ( A‐D ) The representative photomicrographs showing PGC‐1α immunohistochemistry of tissue from different group 24 hrs after TBI. ( E, H ) The nuclear PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( F, I ) The cytoplasmic protein PGC‐1α expression after quercetin treatment in mice with TBI, as measured by Western blot. ( G, J ) The total protein PGC‐1α expression after melatonin treatment in mice with TBI, as measured by Western blot. Bars represent the mean ± S.E.M. * P

    Article Snippet: The nuclear protein was incubated overnight at 4°C with PGC‐1α (1:1000 diluted, rabbit; Millipore, Billerica, MA, USA) and histone H3 (1:1000 diluted, rabbit; Cell Signaling Technology, Beverly, MA, USA) in blocking buffer.

    Techniques: Translocation Assay, Pyrolysis Gas Chromatography, Binding Assay, Immunohistochemistry, Expressing, Mouse Assay, Western Blot

    SRT1720-induced deacetylation of PGC-1α after I/R

    Journal: Toxicology and applied pharmacology

    Article Title: Accelerated recovery of renal mitochondrial and tubule homeostasis with SIRT1/PGC-1α activation following ischemia-reperfusion injury

    doi: 10.1016/j.taap.2013.09.026

    Figure Lengend Snippet: SRT1720-induced deacetylation of PGC-1α after I/R

    Article Snippet: Antibodies used include phosphorylated AMPK, AMPK, acetylated-lysine, and histone H3 (Cell Signaling Technologies, Danvers, MA), SIRT1, PGC-1α, and Na+ ,K+ -ATPase α1 subunit (EMD Millipore, Billerica, MA), GAPDH (Fitzgerald Antibodies, Acton, MA), ATP synthase β and VDAC (Abcam, Cambridge, MA), cytochrome c oxidase subunit I and NDUFB8 (Invitrogen, Grand Island, NY), Mfn2 and vimentin (Sigma-Aldrich, St. Louis, MO), Drp1 (Santa Cruz Biotechnology, Dallas, TX), and KIM-1 (R & D Systems, Minneapolis, MN).

    Techniques: Pyrolysis Gas Chromatography

    Acute PGC‐1α1 expression and dose dependence in cardiomyocytes A , representative immunoblot of protein (top panel) and bar graph of mRNA expression (lower panel) in neonatal cardiomyocytes after PGC‐1α1 overexpression by adenoviral transduction with multiplicity of infection (MOI) 1–30 ( n ≥ 8). B–D , acute PGC‐1α1 mRNA expression in neonatal cardiomyocytes by adenoviral transduction with multiplicity of infection (MOI) 1–10. B , correlation and slope between PGC‐1α expression levels and gene expression of indicated genes. Statistically significant correlation at over 33%. C , scatter plot of selected target genes with correlation ( r ) more than 70% with each square representing an individual sample ( n = 36). D , scatter plot showing the response of selected target gene expression to PGC‐1α levels with each dot representing the average from a group of samples ( n ≥ 8). mRNA expression levels were normalized to B2M and presented here as fold changes relative to expression level in Ad‐CMV transduced cells (= 1, dotted line in C ). 1/2 max (red), a half‐maximal response. mRNA data were obtained from qRT‐PCR analyses. * P

    Journal: The Journal of Physiology

    Article Title: Peroxisome proliferator‐activated receptor‐γ coactivator 1 α1 induces a cardiac excitation–contraction coupling phenotype without metabolic remodelling

    doi: 10.1113/JP272847

    Figure Lengend Snippet: Acute PGC‐1α1 expression and dose dependence in cardiomyocytes A , representative immunoblot of protein (top panel) and bar graph of mRNA expression (lower panel) in neonatal cardiomyocytes after PGC‐1α1 overexpression by adenoviral transduction with multiplicity of infection (MOI) 1–30 ( n ≥ 8). B–D , acute PGC‐1α1 mRNA expression in neonatal cardiomyocytes by adenoviral transduction with multiplicity of infection (MOI) 1–10. B , correlation and slope between PGC‐1α expression levels and gene expression of indicated genes. Statistically significant correlation at over 33%. C , scatter plot of selected target genes with correlation ( r ) more than 70% with each square representing an individual sample ( n = 36). D , scatter plot showing the response of selected target gene expression to PGC‐1α levels with each dot representing the average from a group of samples ( n ≥ 8). mRNA expression levels were normalized to B2M and presented here as fold changes relative to expression level in Ad‐CMV transduced cells (= 1, dotted line in C ). 1/2 max (red), a half‐maximal response. mRNA data were obtained from qRT‐PCR analyses. * P

    Article Snippet: Primary antibodies used were as follows: anti‐AMP‐activated protein kinase α (AMPKα) (Sigma‐Aldrich), phospho‐protein kinase B (Akt1/PKBα) (Ser473) and phosphatidylinositol 3 (PI3) kinase p85 (Millipore, Temecula, CA, USA), GAPDH (14C10, Cell Signaling Technology, Danvers, MA, USA), anti‐Lamin B1 antibody (Abcam, Cambridge, UK), p‐AMPKα1/2 (Thr172), PI3 kinase p110α (H‐201), PI3 kinase p110β (S‐19) (Santa Cruz Biotechnology Inc., Dallas, TX, USA) and PGC‐1α (4C1.3, Calbiochem, Darmstadt, Germany).

    Techniques: Pyrolysis Gas Chromatography, Expressing, Over Expression, Transduction, Infection, Quantitative RT-PCR

    Skeletal muscle glycogen content and blood lactate concentration before and after exercise. PGC-1α-b transgenic mice and wild-type littermates (Wt) (each 8 weeks old) were exercised by forced running on a treadmill at 10 m/min. The speed increased 2 m/min every 3 min up to 30 m/min. Mice ran for 30 min. Skeletal muscle (gastrocnemius) glycogen content was measured before (Sed) and after 30 min of exercise (n = 3–5). Values are means ± SE. ** P

    Journal: PLoS ONE

    Article Title: Skeletal Muscle-Specific Expression of PGC-1?-b, an Exercise-Responsive Isoform, Increases Exercise Capacity and Peak Oxygen Uptake

    doi: 10.1371/journal.pone.0028290

    Figure Lengend Snippet: Skeletal muscle glycogen content and blood lactate concentration before and after exercise. PGC-1α-b transgenic mice and wild-type littermates (Wt) (each 8 weeks old) were exercised by forced running on a treadmill at 10 m/min. The speed increased 2 m/min every 3 min up to 30 m/min. Mice ran for 30 min. Skeletal muscle (gastrocnemius) glycogen content was measured before (Sed) and after 30 min of exercise (n = 3–5). Values are means ± SE. ** P

    Article Snippet: PGC-1α protein was identified by Western blotting with anti-PGC-1α (Rabbit polyclonal IgG) against the carboxyl terminus, 777–797 (Calbiochem, San Diego, CA).

    Techniques: Concentration Assay, Pyrolysis Gas Chromatography, Transgenic Assay, Mouse Assay

    Skeletal muscle-specific expression of PGC-1α-b induced angiogenesis in skeletal muscle. (A) Transverse frozen sections of TA from wild-type (Wt) and PGC-1α-b transgenic mice at 10–11 weeks of age were immunostained for CD31 (endothelial-specific PECAM). Representative immunostains in the superficial region is shown. (B) Quantification of CD31-positive capillaries/mm 2 and capillaries per individual myofiber in superficial and deep regions (n = 3 per group). Data are presented as mean ± SE. *, P

    Journal: PLoS ONE

    Article Title: Skeletal Muscle-Specific Expression of PGC-1?-b, an Exercise-Responsive Isoform, Increases Exercise Capacity and Peak Oxygen Uptake

    doi: 10.1371/journal.pone.0028290

    Figure Lengend Snippet: Skeletal muscle-specific expression of PGC-1α-b induced angiogenesis in skeletal muscle. (A) Transverse frozen sections of TA from wild-type (Wt) and PGC-1α-b transgenic mice at 10–11 weeks of age were immunostained for CD31 (endothelial-specific PECAM). Representative immunostains in the superficial region is shown. (B) Quantification of CD31-positive capillaries/mm 2 and capillaries per individual myofiber in superficial and deep regions (n = 3 per group). Data are presented as mean ± SE. *, P

    Article Snippet: PGC-1α protein was identified by Western blotting with anti-PGC-1α (Rabbit polyclonal IgG) against the carboxyl terminus, 777–797 (Calbiochem, San Diego, CA).

    Techniques: Expressing, Pyrolysis Gas Chromatography, Transgenic Assay, Mouse Assay

    Mitochondrial volume and its function in skeletal muscles overexpressing PGC-1α-b. (A) For estimation of mitochondrial DNA copy number in skeletal muscle (tibialis anterior (TA), extensor digitorum longus (EDL), and soleus (Sol)), the relative mitochondrial DNA copy number from individual mice in each group was calculated as the ratio of COX2 (mitochondrial) to COX4 (nuclear) genes as determined by real-time PCR. The relative mitochondrial DNA copy number was expressed as the percentage of the ratio in wild-type (Wt). CS activity (gastrocnemius (Gas), EDL, and Sol) was normalized to tissue weight. Values are means ± SE of Wt and PGC-1α-b transgenic mice (A-line and B-line) at 10 weeks of age (n = 3–4). * P

    Journal: PLoS ONE

    Article Title: Skeletal Muscle-Specific Expression of PGC-1?-b, an Exercise-Responsive Isoform, Increases Exercise Capacity and Peak Oxygen Uptake

    doi: 10.1371/journal.pone.0028290

    Figure Lengend Snippet: Mitochondrial volume and its function in skeletal muscles overexpressing PGC-1α-b. (A) For estimation of mitochondrial DNA copy number in skeletal muscle (tibialis anterior (TA), extensor digitorum longus (EDL), and soleus (Sol)), the relative mitochondrial DNA copy number from individual mice in each group was calculated as the ratio of COX2 (mitochondrial) to COX4 (nuclear) genes as determined by real-time PCR. The relative mitochondrial DNA copy number was expressed as the percentage of the ratio in wild-type (Wt). CS activity (gastrocnemius (Gas), EDL, and Sol) was normalized to tissue weight. Values are means ± SE of Wt and PGC-1α-b transgenic mice (A-line and B-line) at 10 weeks of age (n = 3–4). * P

    Article Snippet: PGC-1α protein was identified by Western blotting with anti-PGC-1α (Rabbit polyclonal IgG) against the carboxyl terminus, 777–797 (Calbiochem, San Diego, CA).

    Techniques: Pyrolysis Gas Chromatography, Mouse Assay, Real-time Polymerase Chain Reaction, Activity Assay, Transgenic Assay

    PGC-1α-b-mediated increase in fatty acid utilization in skeletal muscle improves maximal oxygen uptake and exercise capacity.

    Journal: PLoS ONE

    Article Title: Skeletal Muscle-Specific Expression of PGC-1?-b, an Exercise-Responsive Isoform, Increases Exercise Capacity and Peak Oxygen Uptake

    doi: 10.1371/journal.pone.0028290

    Figure Lengend Snippet: PGC-1α-b-mediated increase in fatty acid utilization in skeletal muscle improves maximal oxygen uptake and exercise capacity.

    Article Snippet: PGC-1α protein was identified by Western blotting with anti-PGC-1α (Rabbit polyclonal IgG) against the carboxyl terminus, 777–797 (Calbiochem, San Diego, CA).

    Techniques: Pyrolysis Gas Chromatography

    Skeletal muscle-specific expression of PGC-1α-b. (A) Total expression of PGC-1α and its target genes, COX2 and COX4, in wild-type (Wt) and PGC-1α-b mice (A line and B line) at 25 weeks of age (n = 3) was measured by quantitative real-time RT-PCR in skeletal muscle (gastrocnemius, Gas) and heart. Values are means ± SE. *** P

    Journal: PLoS ONE

    Article Title: Skeletal Muscle-Specific Expression of PGC-1?-b, an Exercise-Responsive Isoform, Increases Exercise Capacity and Peak Oxygen Uptake

    doi: 10.1371/journal.pone.0028290

    Figure Lengend Snippet: Skeletal muscle-specific expression of PGC-1α-b. (A) Total expression of PGC-1α and its target genes, COX2 and COX4, in wild-type (Wt) and PGC-1α-b mice (A line and B line) at 25 weeks of age (n = 3) was measured by quantitative real-time RT-PCR in skeletal muscle (gastrocnemius, Gas) and heart. Values are means ± SE. *** P

    Article Snippet: PGC-1α protein was identified by Western blotting with anti-PGC-1α (Rabbit polyclonal IgG) against the carboxyl terminus, 777–797 (Calbiochem, San Diego, CA).

    Techniques: Expressing, Pyrolysis Gas Chromatography, Mouse Assay, Quantitative RT-PCR

    PGC-1α-b induced changes in gene expression in skeletal muscle. Results of quantitative RT-PCR analysis of transcripts encoding proteins involved in fiber type, glucose metabolism, lipid metabolism, and others in quadriceps from wild-type (Wt) and PGC-1α-b mice (A line and B line) at 8 weeks of age. Values are means ± SE (n = 6–9). * P

    Journal: PLoS ONE

    Article Title: Skeletal Muscle-Specific Expression of PGC-1?-b, an Exercise-Responsive Isoform, Increases Exercise Capacity and Peak Oxygen Uptake

    doi: 10.1371/journal.pone.0028290

    Figure Lengend Snippet: PGC-1α-b induced changes in gene expression in skeletal muscle. Results of quantitative RT-PCR analysis of transcripts encoding proteins involved in fiber type, glucose metabolism, lipid metabolism, and others in quadriceps from wild-type (Wt) and PGC-1α-b mice (A line and B line) at 8 weeks of age. Values are means ± SE (n = 6–9). * P

    Article Snippet: PGC-1α protein was identified by Western blotting with anti-PGC-1α (Rabbit polyclonal IgG) against the carboxyl terminus, 777–797 (Calbiochem, San Diego, CA).

    Techniques: Pyrolysis Gas Chromatography, Expressing, Quantitative RT-PCR, Mouse Assay

    Exercise tolerance, RQ ratio, and calculated glucose and lipid oxidation rate, during exercise. (A) PGC-1α-b transgenic mice (A-line and B-line, n = 3 and 4) and wild-type littermates (Wt, n = 7) (each 8 weeks old) were exercised by forced running on a treadmill at 10 m/min. The speed increased by 2 m/min every 3 min until exhaustion. Mice ran until exhaustion (exercise tolerance test). Exercise tolerance is shown as a Kaplan-Meier survival curve. A significant difference ( P

    Journal: PLoS ONE

    Article Title: Skeletal Muscle-Specific Expression of PGC-1?-b, an Exercise-Responsive Isoform, Increases Exercise Capacity and Peak Oxygen Uptake

    doi: 10.1371/journal.pone.0028290

    Figure Lengend Snippet: Exercise tolerance, RQ ratio, and calculated glucose and lipid oxidation rate, during exercise. (A) PGC-1α-b transgenic mice (A-line and B-line, n = 3 and 4) and wild-type littermates (Wt, n = 7) (each 8 weeks old) were exercised by forced running on a treadmill at 10 m/min. The speed increased by 2 m/min every 3 min until exhaustion. Mice ran until exhaustion (exercise tolerance test). Exercise tolerance is shown as a Kaplan-Meier survival curve. A significant difference ( P

    Article Snippet: PGC-1α protein was identified by Western blotting with anti-PGC-1α (Rabbit polyclonal IgG) against the carboxyl terminus, 777–797 (Calbiochem, San Diego, CA).

    Techniques: Pyrolysis Gas Chromatography, Transgenic Assay, Mouse Assay