mouse pgc 1α Search Results


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  • 96
    Millipore mouse anti pgc 1α
    Hippocampal oxidative stress detected by Western blot and double-immunofluorescence staining in PV interneurons on day 1 post-surgery. (A) Representative Western blot images of PV, IL-1β, 4-HNE and <t>PGC-1α</t> in the hippocampus in the four groups; (B) Quantitative analysis. (C,D) Quantification of PV and 8-OH-dG fluorescence in areas CA1 and CA3. (E,F) Quantification of PV and 4-HNE fluorescence in areas CA1 and CA3. The data are presented as the mean ± S.E.M. (5 mice in each group in A,B , 8 mice in each group in C–F ). * p
    Mouse Anti Pgc 1α, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 114 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Proteintech mouse ppargc1a monoclonal
    SET8 interacts with <t>PGC1.</t> (a) Mass spectrometry was used to analyse protein bands in the purified SET8 complex. (b) Interaction between SET8 and PGC1 α in HCC cells was measured by immunoprecipitation. (c) Colocalization of SET8 and PGC1 α in HCC cells as detected by confocal microscopy.
    Mouse Ppargc1a Monoclonal, supplied by Proteintech, used in various techniques. Bioz Stars score: 95/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    The Jackson Laboratory control ln non target shrna eet agonist eet agonist plus ln pgc 1α shrna age matched c57bl 6j mice c57
    SET8 interacts with <t>PGC1.</t> (a) Mass spectrometry was used to analyse protein bands in the purified SET8 complex. (b) Interaction between SET8 and PGC1 α in HCC cells was measured by immunoprecipitation. (c) Colocalization of SET8 and PGC1 α in HCC cells as detected by confocal microscopy.
    Control Ln Non Target Shrna Eet Agonist Eet Agonist Plus Ln Pgc 1α Shrna Age Matched C57bl 6j Mice C57, supplied by The Jackson Laboratory, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/control ln non target shrna eet agonist eet agonist plus ln pgc 1α shrna age matched c57bl 6j mice c57/product/The Jackson Laboratory
    Average 92 stars, based on 6 article reviews
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    control ln non target shrna eet agonist eet agonist plus ln pgc 1α shrna age matched c57bl 6j mice c57 - by Bioz Stars, 2020-09
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    94
    Santa Cruz Biotechnology mouse anti pgc1α
    SET8 interacts with <t>PGC1.</t> (a) Mass spectrometry was used to analyse protein bands in the purified SET8 complex. (b) Interaction between SET8 and PGC1 α in HCC cells was measured by immunoprecipitation. (c) Colocalization of SET8 and PGC1 α in HCC cells as detected by confocal microscopy.
    Mouse Anti Pgc1α, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Addgene inc mouse pgc 1α promoter
    Selective ablation of TORC1 reduces TORC1 and <t>PGC-1α</t> mRNA expression, decreases MMP and makes STHdhQ7 and mutant STHdhQ111 striatal cells more susceptible to 3-NP-induced toxicity. Overexpression of PGC-1α partially prevents TORC1 knockdown-mediated
    Mouse Pgc 1α Promoter, supplied by Addgene inc, used in various techniques. Bioz Stars score: 85/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore sv40 mes 13 mouse mesangial cells anti pgc 1α
    Mouse podocyte and renal <t>mesangial</t> cell impairment by high glucose concentrations. (A) Effect of high glucose on <t>PGC-1α,</t> PPRC1, PPARγ, NRF1, NDUFS1 and COX4I1 mRNA expression. Mouse podocytes were cultured in 30 mM glucose medium for 24 or 48 h. Medium containing 5.5 mM glucose with 24.5 mM mannitol was applied as control. *P
    Sv40 Mes 13 Mouse Mesangial Cells Anti Pgc 1α, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Abcam anti mouse pgc 1α antibody
    The relationship between the protein expression levels of <t>PGC-1α</t> and NT-PGC-1α and the doses of metformin in mice after MI. ( A ) The protein expression level of PGC-1α and NT-PGC-1α treated with different doses of metformin (50–200 mg/kg/d) in the MI mice. ( B ) The quantity of protein expression level of PGC-1α and NT-PGC-1α treated with different doses of metformin (50–200 mg/kg/d) in the MI mice.
    Anti Mouse Pgc 1α Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore monoclonal mouse anti pgc1α
    Effect of TPEN on hsp60, SOD2, and OXPHOS proteins, mitochondrial biogenesis regulators, and mtDNA level in human HepG2 cells. Human HepG2 cells were treated with 3 μM TPEN without FBS for 6 h. A : immunoblot bands of hsp60 and SOD2. B : immunoblot bands of OXPHOS proteins, subunit of complex I (CI-NDUFB8), subunit of complex II (CII-SDHB), subunit of complex III (CIII-UQCRC2), subunit of complex IV (CIV-MTCO1), and subunit of complex V (CV-ATP5A). C : immunoblot bands of p-AMPK, AMPK, <t>PGC1α,</t> NRF1, and TFAM. D : mtDNA level was measured with NADH dehydrogenase subunit 6 by qPCR. Data are expressed as means ± SD ( n = 3). Statistical difference (* P
    Monoclonal Mouse Anti Pgc1α, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    The Jackson Laboratory b6 congenic mck pgc 1α mice
    <t>PGC-1α-mediated</t> increase in the muscle oxidative phenotype does not improve survival or motor function in G93A mice G93A mice were mated with <t>MCK-PGC-1α</t> mice to examine the effect of enhanced mitochondrial biogenesis in the muscle on disease progression. (a) Gastrocnemius muscle from G93A/MCK-PGC-1α mouse shows higher SDH staining than S93A mouse demonstrating increased mitochondrial activity in the presence of PGC-1α transgene (scale=500μm). (b) Survival analysis and (c) weekly weight measures (Two-way ANOVA, n=9 G93A; n=7 G93A/MCK-PGC-1α) did not show a genotypic difference between the two groups. (c) Motor function was examined in these mice using the Rotarod apparatus. The difference in the rotarod latency-to-fall values between the two groups were statistically significant (Two-way ANOVA, p
    B6 Congenic Mck Pgc 1α Mice, supplied by The Jackson Laboratory, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/b6 congenic mck pgc 1α mice/product/The Jackson Laboratory
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    91
    The Jackson Laboratory collection muscle specific pgc 1α transgenic c57bl 6 mice
    <t>PGC-1α-mediated</t> increase in the muscle oxidative phenotype does not improve survival or motor function in G93A mice G93A mice were mated with <t>MCK-PGC-1α</t> mice to examine the effect of enhanced mitochondrial biogenesis in the muscle on disease progression. (a) Gastrocnemius muscle from G93A/MCK-PGC-1α mouse shows higher SDH staining than S93A mouse demonstrating increased mitochondrial activity in the presence of PGC-1α transgene (scale=500μm). (b) Survival analysis and (c) weekly weight measures (Two-way ANOVA, n=9 G93A; n=7 G93A/MCK-PGC-1α) did not show a genotypic difference between the two groups. (c) Motor function was examined in these mice using the Rotarod apparatus. The difference in the rotarod latency-to-fall values between the two groups were statistically significant (Two-way ANOVA, p
    Collection Muscle Specific Pgc 1α Transgenic C57bl 6 Mice, supplied by The Jackson Laboratory, used in various techniques. Bioz Stars score: 91/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/collection muscle specific pgc 1α transgenic c57bl 6 mice/product/The Jackson Laboratory
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    90
    The Jackson Laboratory conditional pgc 1α knock out mice
    <t>PGC-1α</t> isoforms. A , The illustration of PGC-1α new alternative exons and known exons in RefSeq/Ensembl/UCSC genome references. Human ESTs and mouse TSS with enhancer signals derived from > 1000 human and mouse primary cells, cell lines, and tissues were mapped using CAGE. B , Diagram and PCR products show four different PGC-1α isoforms from SH-SY5Y and mouse brain and heart. C , RT-PCR for four PGC-1α isoforms, SDHA, Tomm20, and GAPDH RNA 4 weeks after stereotactic delivery of AAV-GFP or AAV-Cre-GFP into PGC-1α flox/flox mice; n = 3/group. D , Quantification of C normalized to GAPDH; n = 3/group. * p
    Conditional Pgc 1α Knock Out Mice, supplied by The Jackson Laboratory, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    The Jackson Laboratory muscle specific pgc 1α tg mice
    TWEAK inhibits the expression of <t>PGC-1α</t> in cultured myotubes. A ) C2C12 myotubes were treated with indicated amounts of soluble TWEAK protein for 24 h, and mRNA levels of PGC-1α, PGC-1β, Cox I, Cox IV, Cyt c, Tfb2m, Tfam, ATP5b,
    Muscle Specific Pgc 1α Tg Mice, supplied by The Jackson Laboratory, used in various techniques. Bioz Stars score: 88/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/muscle specific pgc 1α tg mice/product/The Jackson Laboratory
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    91
    Santa Cruz Biotechnology rabbit antiserum against mouse pgc1α
    <t>PGC1α</t> mRNA (A) and protein (B) expressions in differentiated 3T3L1 cells. (A) Sirt1 mRNA expression was measured by real-time PCR. The data are expressed as mean ± SD of three experiments. * P
    Rabbit Antiserum Against Mouse Pgc1α, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit antiserum against mouse pgc1α/product/Santa Cruz Biotechnology
    Average 91 stars, based on 12 article reviews
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    90
    Addgene inc cdna encoding mouse full length pgc 1α
    <t>PGC1α</t> mRNA (A) and protein (B) expressions in differentiated 3T3L1 cells. (A) Sirt1 mRNA expression was measured by real-time PCR. The data are expressed as mean ± SD of three experiments. * P
    Cdna Encoding Mouse Full Length Pgc 1α, supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cdna encoding mouse full length pgc 1α/product/Addgene inc
    Average 90 stars, based on 6 article reviews
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    92
    OriGene peroxisome proliferator activated receptor gamma coactivator 1 α pgc 1α mouse cdna
    <t>PGC1α</t> mRNA (A) and protein (B) expressions in differentiated 3T3L1 cells. (A) Sirt1 mRNA expression was measured by real-time PCR. The data are expressed as mean ± SD of three experiments. * P
    Peroxisome Proliferator Activated Receptor Gamma Coactivator 1 α Pgc 1α Mouse Cdna, supplied by OriGene, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/peroxisome proliferator activated receptor gamma coactivator 1 α pgc 1α mouse cdna/product/OriGene
    Average 92 stars, based on 8 article reviews
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    88
    Abcam mouse anti human pgc 1α
    Changes in VEGF protein levels Effect of <t>PGC-1α</t> siRNA on VEGF protein production in hRVECs at 16h of normoxia and hypoxia after transfection were detected by ELISA. The VEGF protein production in siPGC-1α groups were significantly downregulated when compared with control siRNA groups under normoxia and hypoxia. b P
    Mouse Anti Human Pgc 1α, supplied by Abcam, used in various techniques. Bioz Stars score: 88/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Hippocampal oxidative stress detected by Western blot and double-immunofluorescence staining in PV interneurons on day 1 post-surgery. (A) Representative Western blot images of PV, IL-1β, 4-HNE and PGC-1α in the hippocampus in the four groups; (B) Quantitative analysis. (C,D) Quantification of PV and 8-OH-dG fluorescence in areas CA1 and CA3. (E,F) Quantification of PV and 4-HNE fluorescence in areas CA1 and CA3. The data are presented as the mean ± S.E.M. (5 mice in each group in A,B , 8 mice in each group in C–F ). * p

    Journal: Frontiers in Aging Neuroscience

    Article Title: Nox-2-Mediated Phenotype Loss of Hippocampal Parvalbumin Interneurons Might Contribute to Postoperative Cognitive Decline in Aging Mice

    doi: 10.3389/fnagi.2016.00234

    Figure Lengend Snippet: Hippocampal oxidative stress detected by Western blot and double-immunofluorescence staining in PV interneurons on day 1 post-surgery. (A) Representative Western blot images of PV, IL-1β, 4-HNE and PGC-1α in the hippocampus in the four groups; (B) Quantitative analysis. (C,D) Quantification of PV and 8-OH-dG fluorescence in areas CA1 and CA3. (E,F) Quantification of PV and 4-HNE fluorescence in areas CA1 and CA3. The data are presented as the mean ± S.E.M. (5 mice in each group in A,B , 8 mice in each group in C–F ). * p

    Article Snippet: After the membranes were blocked with 5% skim milk in Tris-buffered saline with Tween (TBST), they were incubated with rabbit anti-PV (1:1000; Abcam, Cambridge, United Kingdom), goat anti-interleukin-1β (IL-1β; 1:500; R & D systems, Minneapolis, MN, USA), goat anti-p22phox (1:500; Santa Cruz Biotechnology, Dallas, TX, USA), goat anti-gp91phox (1:500; Santa Cruz Biotechnology), rabbit anti-Nox4 (1:1000; Abcam), rabbit anti-4-hydroxy-2-nonenal (4-HNE; 1:500; Abcam), mouse anti PGC-1α (1:500; Calbiochem, San Diego, CA, USA) and mouse anti-β-actin (1:5000; Sigma-Aldrich) overnight at 4°C.

    Techniques: Western Blot, Double Immunofluorescence Staining, Pyrolysis Gas Chromatography, Fluorescence, Mouse Assay

    The activator of PGC-1α/peroxisome proliferator–activated receptor-α cascade, fenofibrate, attenuates LPS-induced ALI in mice. C57BL/6 mice (8 wk old) were instilled intratracheally with saline or LPS (2 mg/kg in 50 μl saline). At 4 hours after the intratracheal treatment, the mice were injected intraperitoneally with vehicle or fenofibrate (100 mg/kg body weight). At 24 hours after saline or LPS instillation, the mice were killed and BALF (0.5 ml for 3 times/mouse) collected. BALF was centrifuged to collect supernatants and cell pellets. Red blood cells in the cell pellets were lysed. Levels of indicated proinflammatory cytokines ( A ), protein concentrations ( B ), and total leukocyte numbers ( C ) in BALF was determined. ( A – C ) n = 3, 5, 3, 5 mice, respectively; mean ± SEM; * P

    Journal: American Journal of Respiratory Cell and Molecular Biology

    Article Title: Impairment of Fatty Acid Oxidation in Alveolar Epithelial Cells Mediates Acute Lung Injury

    doi: 10.1165/rcmb.2018-0152OC

    Figure Lengend Snippet: The activator of PGC-1α/peroxisome proliferator–activated receptor-α cascade, fenofibrate, attenuates LPS-induced ALI in mice. C57BL/6 mice (8 wk old) were instilled intratracheally with saline or LPS (2 mg/kg in 50 μl saline). At 4 hours after the intratracheal treatment, the mice were injected intraperitoneally with vehicle or fenofibrate (100 mg/kg body weight). At 24 hours after saline or LPS instillation, the mice were killed and BALF (0.5 ml for 3 times/mouse) collected. BALF was centrifuged to collect supernatants and cell pellets. Red blood cells in the cell pellets were lysed. Levels of indicated proinflammatory cytokines ( A ), protein concentrations ( B ), and total leukocyte numbers ( C ) in BALF was determined. ( A – C ) n = 3, 5, 3, 5 mice, respectively; mean ± SEM; * P

    Article Snippet: Mouse anti–PGC-1α antibody was from EMD Millipore.

    Techniques: Pyrolysis Gas Chromatography, Mouse Assay, Injection

    Ablation of AEC PGC-1α aggravates LPS-induced ALI. ( A ) AECs were purified from the control PGC-1α fl/fl and AEC PGC-1α −/− mice and levels of the indicated genes determined. n = 3; mean ± SEM; * P

    Journal: American Journal of Respiratory Cell and Molecular Biology

    Article Title: Impairment of Fatty Acid Oxidation in Alveolar Epithelial Cells Mediates Acute Lung Injury

    doi: 10.1165/rcmb.2018-0152OC

    Figure Lengend Snippet: Ablation of AEC PGC-1α aggravates LPS-induced ALI. ( A ) AECs were purified from the control PGC-1α fl/fl and AEC PGC-1α −/− mice and levels of the indicated genes determined. n = 3; mean ± SEM; * P

    Article Snippet: Mouse anti–PGC-1α antibody was from EMD Millipore.

    Techniques: Pyrolysis Gas Chromatography, Purification, Mouse Assay

    Effect of quercetin (Q), isoquercitrin (IQ), rutin (R), and EMIQ on the expression of adiposity-related proteins in WAT. The expression of (A) p-ACC, ACC, CPT1, UCP2, and GAPDH in the tissue lysate of WAT, the expression of (B) C/EBPβ, C/EBPα, PPARγ, SREBP1 and GAPDH in tissue lysate of WAT and the expression of (C) PGC-1α, PRDM16, UCP1,and GAPDH in tissue lysate of WAT were determined by Western blot analysis. Each panel shows a typical blot from five animals. The normalized density of specific protein band shown in the bar graphs. Values were shown as the mean ± SE ( n = 5). Different letters indicate significant differences among the groups by Tukey-Kramer multiple comparison test ( p

    Journal: Journal of Clinical Biochemistry and Nutrition

    Article Title: Prevention effect of quercetin and its glycosides on obesity and hyperglycemia through activating AMPKα in high-fat diet-fed ICR mice

    doi: 10.3164/jcbn.20-47

    Figure Lengend Snippet: Effect of quercetin (Q), isoquercitrin (IQ), rutin (R), and EMIQ on the expression of adiposity-related proteins in WAT. The expression of (A) p-ACC, ACC, CPT1, UCP2, and GAPDH in the tissue lysate of WAT, the expression of (B) C/EBPβ, C/EBPα, PPARγ, SREBP1 and GAPDH in tissue lysate of WAT and the expression of (C) PGC-1α, PRDM16, UCP1,and GAPDH in tissue lysate of WAT were determined by Western blot analysis. Each panel shows a typical blot from five animals. The normalized density of specific protein band shown in the bar graphs. Values were shown as the mean ± SE ( n = 5). Different letters indicate significant differences among the groups by Tukey-Kramer multiple comparison test ( p

    Article Snippet: Anti-PGC-1α mouse mAb, and anti-PRDM16 rabbit IgG, antibodies were from Millipore (Tokyo, Japan).

    Techniques: Expressing, Pyrolysis Gas Chromatography, Western Blot

    PGC-1α induction by GW4064 is FXR dependent in liver but independent in skeletal muscle. A and B, Ten- to 12-wk-old FXRKO or age- and sex-matched WT mice were given GW4064 or vehicle (V) by oral gavage (50 mg/kg body weight) for 3 d (WT: V, n

    Journal: Molecular Endocrinology

    Article Title: Bile Acid Receptor Agonist GW4064 Regulates PPARγ Coactivator-1α Expression Through Estrogen Receptor-Related Receptor α

    doi: 10.1210/me.2010-0512

    Figure Lengend Snippet: PGC-1α induction by GW4064 is FXR dependent in liver but independent in skeletal muscle. A and B, Ten- to 12-wk-old FXRKO or age- and sex-matched WT mice were given GW4064 or vehicle (V) by oral gavage (50 mg/kg body weight) for 3 d (WT: V, n

    Article Snippet: Anti-PGC-1α mouse monoclonal antibody (4C1.3) was from EMD Biosciences (San Diego, CA) (this antibody was selected because it detects a single band of ∼110 kDa and it does not detect any band in PGC-1α knockout tissues).

    Techniques: Pyrolysis Gas Chromatography, Mouse Assay

    GW4064 activates PGC-1α promoter reporter and induces its expression in cell and in vivo . A and B, GW4064 activates PGC-1luc in Huh7 (A) and Cos-7 cells (B). Cells were transfected with indicated plasmids and treated for 24 h. After lysis, luciferase

    Journal: Molecular Endocrinology

    Article Title: Bile Acid Receptor Agonist GW4064 Regulates PPARγ Coactivator-1α Expression Through Estrogen Receptor-Related Receptor α

    doi: 10.1210/me.2010-0512

    Figure Lengend Snippet: GW4064 activates PGC-1α promoter reporter and induces its expression in cell and in vivo . A and B, GW4064 activates PGC-1luc in Huh7 (A) and Cos-7 cells (B). Cells were transfected with indicated plasmids and treated for 24 h. After lysis, luciferase

    Article Snippet: Anti-PGC-1α mouse monoclonal antibody (4C1.3) was from EMD Biosciences (San Diego, CA) (this antibody was selected because it detects a single band of ∼110 kDa and it does not detect any band in PGC-1α knockout tissues).

    Techniques: Pyrolysis Gas Chromatography, Expressing, In Vivo, Transfection, Lysis, Luciferase

    GW4064-mediated PGC-1α up-regulation occurs via ERRα. A, XCT790 represses GW4064 activation of PGC-1luc. Cos-7 cells were transfected and treated as indicated. In cotreatment experiments, GW4064 treatment was preceded by 1-h treatment

    Journal: Molecular Endocrinology

    Article Title: Bile Acid Receptor Agonist GW4064 Regulates PPARγ Coactivator-1α Expression Through Estrogen Receptor-Related Receptor α

    doi: 10.1210/me.2010-0512

    Figure Lengend Snippet: GW4064-mediated PGC-1α up-regulation occurs via ERRα. A, XCT790 represses GW4064 activation of PGC-1luc. Cos-7 cells were transfected and treated as indicated. In cotreatment experiments, GW4064 treatment was preceded by 1-h treatment

    Article Snippet: Anti-PGC-1α mouse monoclonal antibody (4C1.3) was from EMD Biosciences (San Diego, CA) (this antibody was selected because it detects a single band of ∼110 kDa and it does not detect any band in PGC-1α knockout tissues).

    Techniques: Pyrolysis Gas Chromatography, Activation Assay, Transfection

    WT-PGC-1α/L-PGC-1α is involved in HCV RNA replication and HCV assembly. (A) Effect of WT-PGC-1α/L-PGC-1α knockdown on pseudoparticle entry (means ± SEMs; n = 3). (B) Effect of WT-PGC-1α/L-PGC-1α

    Journal: Journal of Virology

    Article Title: Endoplasmic Reticulum Stress Links Hepatitis C Virus RNA Replication to Wild-Type PGC-1α/Liver-Specific PGC-1α Upregulation

    doi: 10.1128/JVI.01202-14

    Figure Lengend Snippet: WT-PGC-1α/L-PGC-1α is involved in HCV RNA replication and HCV assembly. (A) Effect of WT-PGC-1α/L-PGC-1α knockdown on pseudoparticle entry (means ± SEMs; n = 3). (B) Effect of WT-PGC-1α/L-PGC-1α

    Article Snippet: The following primary antibodies were used for Western blotting: monoclonal mouse anti-PGC-1α antibody (4C1.3; Calbiochem), polyclonal rabbit anti-PGC-1α antibody (ab54481; Abcam), monoclonal mouse anti-HCV core antibody (C7-50; Abcam), monoclonal mouse anti-HCV NS3 (H23; Abcam), monoclonal mouse phospho-CREB antibody (10E9; Santa Cruz), monoclonal mouse CREB antibody (X-12; Santa Cruz), polyclonal rabbit phospho-ATF2 (Thr71) antibody (no. 9221; Cell Signaling Technology), monoclonal rabbit phospho-FoxO1 (Thr24) antibody (4G6; Beyotime, China), monoclonal rabbit FoxO1 antibody (C29H4; Beyotime), rabbit Bip antibody (Beyotime), rabbit histone H3 antibody (Beyotime, China), polyclonal rabbit β-actin antibody (MultiSciences, China), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (Kang Xiang, Shanghai, China).

    Techniques: Pyrolysis Gas Chromatography

    Upregulation of both WT-PGC-1α and L-PGC-1α depends on HCV RNA replication. HCV RNA levels (A) and WT-PGC-1α and L-PGC-1α mRNA levels (B) were determined after transfecting Huh7.5.1 cells with full-length HCV-Jc1 RNA for

    Journal: Journal of Virology

    Article Title: Endoplasmic Reticulum Stress Links Hepatitis C Virus RNA Replication to Wild-Type PGC-1α/Liver-Specific PGC-1α Upregulation

    doi: 10.1128/JVI.01202-14

    Figure Lengend Snippet: Upregulation of both WT-PGC-1α and L-PGC-1α depends on HCV RNA replication. HCV RNA levels (A) and WT-PGC-1α and L-PGC-1α mRNA levels (B) were determined after transfecting Huh7.5.1 cells with full-length HCV-Jc1 RNA for

    Article Snippet: The following primary antibodies were used for Western blotting: monoclonal mouse anti-PGC-1α antibody (4C1.3; Calbiochem), polyclonal rabbit anti-PGC-1α antibody (ab54481; Abcam), monoclonal mouse anti-HCV core antibody (C7-50; Abcam), monoclonal mouse anti-HCV NS3 (H23; Abcam), monoclonal mouse phospho-CREB antibody (10E9; Santa Cruz), monoclonal mouse CREB antibody (X-12; Santa Cruz), polyclonal rabbit phospho-ATF2 (Thr71) antibody (no. 9221; Cell Signaling Technology), monoclonal rabbit phospho-FoxO1 (Thr24) antibody (4G6; Beyotime, China), monoclonal rabbit FoxO1 antibody (C29H4; Beyotime), rabbit Bip antibody (Beyotime), rabbit histone H3 antibody (Beyotime, China), polyclonal rabbit β-actin antibody (MultiSciences, China), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (Kang Xiang, Shanghai, China).

    Techniques: Pyrolysis Gas Chromatography

    L-PGC-1α upregulation by HCV is mediated by CREB phosphorylation and FoxO1 dephosphorylation. (A) Effect of H89 on L-PGC-1α mRNA upregulation after HCV infection. The effect of H89 on CREB phosphorylation was shown by Western blotting

    Journal: Journal of Virology

    Article Title: Endoplasmic Reticulum Stress Links Hepatitis C Virus RNA Replication to Wild-Type PGC-1α/Liver-Specific PGC-1α Upregulation

    doi: 10.1128/JVI.01202-14

    Figure Lengend Snippet: L-PGC-1α upregulation by HCV is mediated by CREB phosphorylation and FoxO1 dephosphorylation. (A) Effect of H89 on L-PGC-1α mRNA upregulation after HCV infection. The effect of H89 on CREB phosphorylation was shown by Western blotting

    Article Snippet: The following primary antibodies were used for Western blotting: monoclonal mouse anti-PGC-1α antibody (4C1.3; Calbiochem), polyclonal rabbit anti-PGC-1α antibody (ab54481; Abcam), monoclonal mouse anti-HCV core antibody (C7-50; Abcam), monoclonal mouse anti-HCV NS3 (H23; Abcam), monoclonal mouse phospho-CREB antibody (10E9; Santa Cruz), monoclonal mouse CREB antibody (X-12; Santa Cruz), polyclonal rabbit phospho-ATF2 (Thr71) antibody (no. 9221; Cell Signaling Technology), monoclonal rabbit phospho-FoxO1 (Thr24) antibody (4G6; Beyotime, China), monoclonal rabbit FoxO1 antibody (C29H4; Beyotime), rabbit Bip antibody (Beyotime), rabbit histone H3 antibody (Beyotime, China), polyclonal rabbit β-actin antibody (MultiSciences, China), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (Kang Xiang, Shanghai, China).

    Techniques: Pyrolysis Gas Chromatography, De-Phosphorylation Assay, Infection, Western Blot

    HCV-induced upregulation of WT-PGC-1α is mediated by CREB phosphorylation.

    Journal: Journal of Virology

    Article Title: Endoplasmic Reticulum Stress Links Hepatitis C Virus RNA Replication to Wild-Type PGC-1α/Liver-Specific PGC-1α Upregulation

    doi: 10.1128/JVI.01202-14

    Figure Lengend Snippet: HCV-induced upregulation of WT-PGC-1α is mediated by CREB phosphorylation.

    Article Snippet: The following primary antibodies were used for Western blotting: monoclonal mouse anti-PGC-1α antibody (4C1.3; Calbiochem), polyclonal rabbit anti-PGC-1α antibody (ab54481; Abcam), monoclonal mouse anti-HCV core antibody (C7-50; Abcam), monoclonal mouse anti-HCV NS3 (H23; Abcam), monoclonal mouse phospho-CREB antibody (10E9; Santa Cruz), monoclonal mouse CREB antibody (X-12; Santa Cruz), polyclonal rabbit phospho-ATF2 (Thr71) antibody (no. 9221; Cell Signaling Technology), monoclonal rabbit phospho-FoxO1 (Thr24) antibody (4G6; Beyotime, China), monoclonal rabbit FoxO1 antibody (C29H4; Beyotime), rabbit Bip antibody (Beyotime), rabbit histone H3 antibody (Beyotime, China), polyclonal rabbit β-actin antibody (MultiSciences, China), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (Kang Xiang, Shanghai, China).

    Techniques: Pyrolysis Gas Chromatography

    HCV-induced WT-PGC-1α upregulation is mediated by CREB phosphorylation. (A) Schematic of the three WT-PGC-1α promoter site-specific mutants. IRS, insulin response sequence; CRE, cAMP response element. (B) Different WT-PGC-1α promoter

    Journal: Journal of Virology

    Article Title: Endoplasmic Reticulum Stress Links Hepatitis C Virus RNA Replication to Wild-Type PGC-1α/Liver-Specific PGC-1α Upregulation

    doi: 10.1128/JVI.01202-14

    Figure Lengend Snippet: HCV-induced WT-PGC-1α upregulation is mediated by CREB phosphorylation. (A) Schematic of the three WT-PGC-1α promoter site-specific mutants. IRS, insulin response sequence; CRE, cAMP response element. (B) Different WT-PGC-1α promoter

    Article Snippet: The following primary antibodies were used for Western blotting: monoclonal mouse anti-PGC-1α antibody (4C1.3; Calbiochem), polyclonal rabbit anti-PGC-1α antibody (ab54481; Abcam), monoclonal mouse anti-HCV core antibody (C7-50; Abcam), monoclonal mouse anti-HCV NS3 (H23; Abcam), monoclonal mouse phospho-CREB antibody (10E9; Santa Cruz), monoclonal mouse CREB antibody (X-12; Santa Cruz), polyclonal rabbit phospho-ATF2 (Thr71) antibody (no. 9221; Cell Signaling Technology), monoclonal rabbit phospho-FoxO1 (Thr24) antibody (4G6; Beyotime, China), monoclonal rabbit FoxO1 antibody (C29H4; Beyotime), rabbit Bip antibody (Beyotime), rabbit histone H3 antibody (Beyotime, China), polyclonal rabbit β-actin antibody (MultiSciences, China), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (Kang Xiang, Shanghai, China).

    Techniques: Pyrolysis Gas Chromatography, Sequencing

    WT-PGC-1α and L-PGC-1α are upregulated by HCV infection and promote HCV production. (A) Analysis of HCV RNA levels and WT-PGC-1α and L-PGC-1α mRNA levels after infection of Huh7.5.1 cells with HCV-Jc1 (MOI, 0.02) for different

    Journal: Journal of Virology

    Article Title: Endoplasmic Reticulum Stress Links Hepatitis C Virus RNA Replication to Wild-Type PGC-1α/Liver-Specific PGC-1α Upregulation

    doi: 10.1128/JVI.01202-14

    Figure Lengend Snippet: WT-PGC-1α and L-PGC-1α are upregulated by HCV infection and promote HCV production. (A) Analysis of HCV RNA levels and WT-PGC-1α and L-PGC-1α mRNA levels after infection of Huh7.5.1 cells with HCV-Jc1 (MOI, 0.02) for different

    Article Snippet: The following primary antibodies were used for Western blotting: monoclonal mouse anti-PGC-1α antibody (4C1.3; Calbiochem), polyclonal rabbit anti-PGC-1α antibody (ab54481; Abcam), monoclonal mouse anti-HCV core antibody (C7-50; Abcam), monoclonal mouse anti-HCV NS3 (H23; Abcam), monoclonal mouse phospho-CREB antibody (10E9; Santa Cruz), monoclonal mouse CREB antibody (X-12; Santa Cruz), polyclonal rabbit phospho-ATF2 (Thr71) antibody (no. 9221; Cell Signaling Technology), monoclonal rabbit phospho-FoxO1 (Thr24) antibody (4G6; Beyotime, China), monoclonal rabbit FoxO1 antibody (C29H4; Beyotime), rabbit Bip antibody (Beyotime), rabbit histone H3 antibody (Beyotime, China), polyclonal rabbit β-actin antibody (MultiSciences, China), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (Kang Xiang, Shanghai, China).

    Techniques: Pyrolysis Gas Chromatography, Infection

    HCV RNA replication upregulates WT-PGC-1α/L-PGC-1α through ER stress in Huh7 cells, and hepatic mPGC-1α correlates with ER stress marker mBip in mice. (A) The activation of ER stress and CREB is indicated by the high expression

    Journal: Journal of Virology

    Article Title: Endoplasmic Reticulum Stress Links Hepatitis C Virus RNA Replication to Wild-Type PGC-1α/Liver-Specific PGC-1α Upregulation

    doi: 10.1128/JVI.01202-14

    Figure Lengend Snippet: HCV RNA replication upregulates WT-PGC-1α/L-PGC-1α through ER stress in Huh7 cells, and hepatic mPGC-1α correlates with ER stress marker mBip in mice. (A) The activation of ER stress and CREB is indicated by the high expression

    Article Snippet: The following primary antibodies were used for Western blotting: monoclonal mouse anti-PGC-1α antibody (4C1.3; Calbiochem), polyclonal rabbit anti-PGC-1α antibody (ab54481; Abcam), monoclonal mouse anti-HCV core antibody (C7-50; Abcam), monoclonal mouse anti-HCV NS3 (H23; Abcam), monoclonal mouse phospho-CREB antibody (10E9; Santa Cruz), monoclonal mouse CREB antibody (X-12; Santa Cruz), polyclonal rabbit phospho-ATF2 (Thr71) antibody (no. 9221; Cell Signaling Technology), monoclonal rabbit phospho-FoxO1 (Thr24) antibody (4G6; Beyotime, China), monoclonal rabbit FoxO1 antibody (C29H4; Beyotime), rabbit Bip antibody (Beyotime), rabbit histone H3 antibody (Beyotime, China), polyclonal rabbit β-actin antibody (MultiSciences, China), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (Kang Xiang, Shanghai, China).

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

    HCV upregulates WT-PGC-1α/L-PGC-1α through ER stress in Huh7.5.1 cells. (A) The activation of ER stress is shown by the activation of the IRE1-XBP1 pathway. Splicing of XBP1 was shown by reverse transcription-PCR (RT-PCR). XBP1(U) and

    Journal: Journal of Virology

    Article Title: Endoplasmic Reticulum Stress Links Hepatitis C Virus RNA Replication to Wild-Type PGC-1α/Liver-Specific PGC-1α Upregulation

    doi: 10.1128/JVI.01202-14

    Figure Lengend Snippet: HCV upregulates WT-PGC-1α/L-PGC-1α through ER stress in Huh7.5.1 cells. (A) The activation of ER stress is shown by the activation of the IRE1-XBP1 pathway. Splicing of XBP1 was shown by reverse transcription-PCR (RT-PCR). XBP1(U) and

    Article Snippet: The following primary antibodies were used for Western blotting: monoclonal mouse anti-PGC-1α antibody (4C1.3; Calbiochem), polyclonal rabbit anti-PGC-1α antibody (ab54481; Abcam), monoclonal mouse anti-HCV core antibody (C7-50; Abcam), monoclonal mouse anti-HCV NS3 (H23; Abcam), monoclonal mouse phospho-CREB antibody (10E9; Santa Cruz), monoclonal mouse CREB antibody (X-12; Santa Cruz), polyclonal rabbit phospho-ATF2 (Thr71) antibody (no. 9221; Cell Signaling Technology), monoclonal rabbit phospho-FoxO1 (Thr24) antibody (4G6; Beyotime, China), monoclonal rabbit FoxO1 antibody (C29H4; Beyotime), rabbit Bip antibody (Beyotime), rabbit histone H3 antibody (Beyotime, China), polyclonal rabbit β-actin antibody (MultiSciences, China), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (Kang Xiang, Shanghai, China).

    Techniques: Pyrolysis Gas Chromatography, Activation Assay, Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction

    SET8 interacts with PGC1. (a) Mass spectrometry was used to analyse protein bands in the purified SET8 complex. (b) Interaction between SET8 and PGC1 α in HCC cells was measured by immunoprecipitation. (c) Colocalization of SET8 and PGC1 α in HCC cells as detected by confocal microscopy.

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Fasting Induces Hepatocellular Carcinoma Cell Apoptosis by Inhibiting SET8 Expression

    doi: 10.1155/2020/3985089

    Figure Lengend Snippet: SET8 interacts with PGC1. (a) Mass spectrometry was used to analyse protein bands in the purified SET8 complex. (b) Interaction between SET8 and PGC1 α in HCC cells was measured by immunoprecipitation. (c) Colocalization of SET8 and PGC1 α in HCC cells as detected by confocal microscopy.

    Article Snippet: Cells were then incubated with primary anti-SET8 (ProteinTech, 14063-1-AP, 1/200) and anti-PGC1α (ProteinTech, 66369-1-Ig, 1/200) antibodies overnight at 4°C.

    Techniques: Mass Spectrometry, Purification, Immunoprecipitation, Confocal Microscopy

    Role of PGC1 α in HCC cell viability and apoptosis in response to fasting. (a) Proliferation of MHCC-97H and HCC-LM3 cells under fasting conditions for 24 h or fasting in combination with overexpressed PGC1 α . (b) Flow cytometry was used to detect the number of apoptotic MHCC-97H and HCC-LM3 cells under fasting conditions for 24 h or fasting in combination with overexpressed PGC1 α . (c) The level of reactive oxygen species in MHCC-97H and HCC-LM3 cells under fasting conditions for 24 h or fasting in combination with overexpressed PGC1 α . (d) Western blot analysis of PGC1 α and Keap1/Nrf2/ARE signalling pathway components in MHCC-97H and HCC-LM3 cells under fasting conditions for 24 h or fasting in combination with overexpressed PGC1 α . (e) qPCR analysis of PGC1 α and Keap1/Nrf2/ARE signalling pathway components in MHCC-97H and HCC-LM3 cells under fasting conditions for 24 h or fasting in combination with overexpressed PGC1 α . (f) ChIP assay of PGC1 α presence at the promoter region of Keap1. Normal IgG was used as a control. (g) PGC1 α knockdown increased Keap1 luciferase activity in HCC-LM3 cells. Data are shown as the mean ± SD of five independent experiments. ∗ P

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Fasting Induces Hepatocellular Carcinoma Cell Apoptosis by Inhibiting SET8 Expression

    doi: 10.1155/2020/3985089

    Figure Lengend Snippet: Role of PGC1 α in HCC cell viability and apoptosis in response to fasting. (a) Proliferation of MHCC-97H and HCC-LM3 cells under fasting conditions for 24 h or fasting in combination with overexpressed PGC1 α . (b) Flow cytometry was used to detect the number of apoptotic MHCC-97H and HCC-LM3 cells under fasting conditions for 24 h or fasting in combination with overexpressed PGC1 α . (c) The level of reactive oxygen species in MHCC-97H and HCC-LM3 cells under fasting conditions for 24 h or fasting in combination with overexpressed PGC1 α . (d) Western blot analysis of PGC1 α and Keap1/Nrf2/ARE signalling pathway components in MHCC-97H and HCC-LM3 cells under fasting conditions for 24 h or fasting in combination with overexpressed PGC1 α . (e) qPCR analysis of PGC1 α and Keap1/Nrf2/ARE signalling pathway components in MHCC-97H and HCC-LM3 cells under fasting conditions for 24 h or fasting in combination with overexpressed PGC1 α . (f) ChIP assay of PGC1 α presence at the promoter region of Keap1. Normal IgG was used as a control. (g) PGC1 α knockdown increased Keap1 luciferase activity in HCC-LM3 cells. Data are shown as the mean ± SD of five independent experiments. ∗ P

    Article Snippet: Cells were then incubated with primary anti-SET8 (ProteinTech, 14063-1-AP, 1/200) and anti-PGC1α (ProteinTech, 66369-1-Ig, 1/200) antibodies overnight at 4°C.

    Techniques: Flow Cytometry, Western Blot, Real-time Polymerase Chain Reaction, Chromatin Immunoprecipitation, Luciferase, Activity Assay

    SET8 interacts with PGC1 α to regulate Keap1 in HCC cells in vitro , and fasting inhibits HCC growth via SET8 inhibition in vivo . (a) The effects of SET8, PGC1 α , and mutant SET8 on Keap1 luciferase activity in HCC-LM3 cells. (b) Western blotting was used to detect the SET8, Keap1, and Nrf2 proteins in MHCC-97 and HCC-LM3 cells overexpressing wild-type or mutant SET8. (c, d) Tumour growth following subcutaneous injection in the right flanks of Balb/c nude mice with 97H control cells, 97H-shSET8 cells, or 97H-SET8 overexpression cells ( n = 6). (e) Western blotting was used to detect proteins SET8 and Keap1/Nrf2/ARE signalling pathway components in mice. (f) The mRNA expression of SET8 and Keap1/Nrf2/ARE signalling pathway components was examined by qPCR in vivo . Data are shown as the mean ± SD of five independent experiments. ∗ P

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Fasting Induces Hepatocellular Carcinoma Cell Apoptosis by Inhibiting SET8 Expression

    doi: 10.1155/2020/3985089

    Figure Lengend Snippet: SET8 interacts with PGC1 α to regulate Keap1 in HCC cells in vitro , and fasting inhibits HCC growth via SET8 inhibition in vivo . (a) The effects of SET8, PGC1 α , and mutant SET8 on Keap1 luciferase activity in HCC-LM3 cells. (b) Western blotting was used to detect the SET8, Keap1, and Nrf2 proteins in MHCC-97 and HCC-LM3 cells overexpressing wild-type or mutant SET8. (c, d) Tumour growth following subcutaneous injection in the right flanks of Balb/c nude mice with 97H control cells, 97H-shSET8 cells, or 97H-SET8 overexpression cells ( n = 6). (e) Western blotting was used to detect proteins SET8 and Keap1/Nrf2/ARE signalling pathway components in mice. (f) The mRNA expression of SET8 and Keap1/Nrf2/ARE signalling pathway components was examined by qPCR in vivo . Data are shown as the mean ± SD of five independent experiments. ∗ P

    Article Snippet: Cells were then incubated with primary anti-SET8 (ProteinTech, 14063-1-AP, 1/200) and anti-PGC1α (ProteinTech, 66369-1-Ig, 1/200) antibodies overnight at 4°C.

    Techniques: In Vitro, Inhibition, In Vivo, Mutagenesis, Luciferase, Activity Assay, Western Blot, Injection, Mouse Assay, Over Expression, Expressing, Real-time Polymerase Chain Reaction

    Selective ablation of TORC1 reduces TORC1 and PGC-1α mRNA expression, decreases MMP and makes STHdhQ7 and mutant STHdhQ111 striatal cells more susceptible to 3-NP-induced toxicity. Overexpression of PGC-1α partially prevents TORC1 knockdown-mediated

    Journal: Human Molecular Genetics

    Article Title: Transducer of regulated CREB-binding proteins (TORCs) transcription and function is impaired in Huntington's disease

    doi: 10.1093/hmg/dds178

    Figure Lengend Snippet: Selective ablation of TORC1 reduces TORC1 and PGC-1α mRNA expression, decreases MMP and makes STHdhQ7 and mutant STHdhQ111 striatal cells more susceptible to 3-NP-induced toxicity. Overexpression of PGC-1α partially prevents TORC1 knockdown-mediated

    Article Snippet: STHdhQ7 and STHdhQ111 cells were transiently transfected with the 2 kb PGC-1α promoter luciferase reporter having the sequences of mouse PGC-1α promoter (pGL3-PGC1α-Luc) between +78 and −2533 (Addgene, USA) using Lipofectamine reagent (Invitrogen).

    Techniques: Pyrolysis Gas Chromatography, Expressing, Mutagenesis, Over Expression

    Overexpression of TORC1 induces CREB and PGC-1α expression and PGC-1α promoter activity in WT and HD striatal cells. ( A ) WT STHdhQ7 (Q7/7) and mutant STHdhQ111 (Q111/111) striatal cell lines were transiently transfected with TORC1 plasmids

    Journal: Human Molecular Genetics

    Article Title: Transducer of regulated CREB-binding proteins (TORCs) transcription and function is impaired in Huntington's disease

    doi: 10.1093/hmg/dds178

    Figure Lengend Snippet: Overexpression of TORC1 induces CREB and PGC-1α expression and PGC-1α promoter activity in WT and HD striatal cells. ( A ) WT STHdhQ7 (Q7/7) and mutant STHdhQ111 (Q111/111) striatal cell lines were transiently transfected with TORC1 plasmids

    Article Snippet: STHdhQ7 and STHdhQ111 cells were transiently transfected with the 2 kb PGC-1α promoter luciferase reporter having the sequences of mouse PGC-1α promoter (pGL3-PGC1α-Luc) between +78 and −2533 (Addgene, USA) using Lipofectamine reagent (Invitrogen).

    Techniques: Over Expression, Pyrolysis Gas Chromatography, Expressing, Activity Assay, Mutagenesis, Transfection

    Knockdown of mutant Htt prevents the transcriptional repression of TORC1, CREB and PGC-1α in Htt striatal cells. ( A ) Increased TORC1, CREB and PGC-1α mRNA expressions in STHdhQ111 HD striatal cells by the knockdown of mutant Htt. Control

    Journal: Human Molecular Genetics

    Article Title: Transducer of regulated CREB-binding proteins (TORCs) transcription and function is impaired in Huntington's disease

    doi: 10.1093/hmg/dds178

    Figure Lengend Snippet: Knockdown of mutant Htt prevents the transcriptional repression of TORC1, CREB and PGC-1α in Htt striatal cells. ( A ) Increased TORC1, CREB and PGC-1α mRNA expressions in STHdhQ111 HD striatal cells by the knockdown of mutant Htt. Control

    Article Snippet: STHdhQ7 and STHdhQ111 cells were transiently transfected with the 2 kb PGC-1α promoter luciferase reporter having the sequences of mouse PGC-1α promoter (pGL3-PGC1α-Luc) between +78 and −2533 (Addgene, USA) using Lipofectamine reagent (Invitrogen).

    Techniques: Mutagenesis, Pyrolysis Gas Chromatography

    TORC1 overexpression induces the expression of PGC-1α target genes (mitochondrial biogenesis genes) and increases mitochondrial DNA content in WT and HD striatal cells. ( A ) WT STHdhQ7 (Q7/7) and mutant STHdhQ111 (Q111/111) striatal cell lines

    Journal: Human Molecular Genetics

    Article Title: Transducer of regulated CREB-binding proteins (TORCs) transcription and function is impaired in Huntington's disease

    doi: 10.1093/hmg/dds178

    Figure Lengend Snippet: TORC1 overexpression induces the expression of PGC-1α target genes (mitochondrial biogenesis genes) and increases mitochondrial DNA content in WT and HD striatal cells. ( A ) WT STHdhQ7 (Q7/7) and mutant STHdhQ111 (Q111/111) striatal cell lines

    Article Snippet: STHdhQ7 and STHdhQ111 cells were transiently transfected with the 2 kb PGC-1α promoter luciferase reporter having the sequences of mouse PGC-1α promoter (pGL3-PGC1α-Luc) between +78 and −2533 (Addgene, USA) using Lipofectamine reagent (Invitrogen).

    Techniques: Over Expression, Expressing, Pyrolysis Gas Chromatography, Mutagenesis

    TFIIH influences PGC-1α deacetylation by SIRT1 by interacting with both. ( panel A ) After immunoprecipitation of PGC-1α from nuclear extracts of WT (lanes 1–2) and TTD (lanes 3–5) hepatocytes, co-immunoprecipitated proteins were visualized by western blots with antibodies raised against PGC-1α (110 kDa), SIRT1 (110 kDa) and the p62 subunit (62 kDa). TTD nuclear extract was supplemented with recombinant TFIIH (rIIH, lane 5). ( panel B ) When indicated (+), GST-PGC-1α purified from bacteria (130 kDa) was incubated with lysate of Sf9 cells overexpressing TFIIH (rIIH). After immunoprecipitation with an anti Flag-Tag antibody (that recognized the flagged XPB subunit, 89 kDa), the bound proteins were visualized by western blots using antibodies raised against PGC-1α and XPB. ( panel C ) Purified SIRT1 (110 kDa) was incubated with lysate of Sf9 cells overexpressing TFIIH (rIIH). Immunoprecipitations were performed as described panel B. The bound proteins were visualized by western blots using antibodies raised against SIRT1 and XPB. ( panel D ) In vitro pull-down assays were performed with GST alone (-, 26 kDa, lanes 2) or GST-PGC-1α (PGC-1α, 130 kDa, lanes 3) incubated with Sf9 cell extracts overexpressing separately each subunit of TFIIH. The bound proteins were visualized by western blots using antibodies directed against each TFIIH subunit. As a reference, the input lanes (IN, lanes 1) represent 10% of the total volume of extract used for each incubation. ( panel E ) Purified SIRT1 was incubated with Sf9 cell extracts overexpressing separately each TFIIH subunit. Immunoprecipitations (IP) were done using antibodies directed against the TFIIH subunits. The bound proteins were revealed by western blots. ( panel F ) Deacetylation profile of PGC-1α in WT (lanes 1–3) and TTD (lanes 4–6) hepatocytes after different times of pyruvate treatment (0, 4 and 6 hours). After immunoprecipitation with specific antibodies (IP Ab-PGC-1α), PGC-1α acetylation has been visualized by western blots with anti-acetyl lysine antibodies. Graph depicts the ratio of acetyl-Lysine (Ac-Lys)/PGC-1α western blots signals. ( panel G ) PGC-1α was immunoprecipitated with specific antibodies (IP Ab-PGC-1α) from nuclear extracts of WT (lanes 1–3) and TTD (lanes 4–6) hepatocytes after different times of pyruvate treatment (0, 4 and 6 hours). Co-immunoprecipitated proteins were visualized by western blots with anti-PGC-1α and -SIRT1 antibodies. Graph depicts the binding ratio between SIRT1 and PGC-1α.

    Journal: PLoS Genetics

    Article Title: Dynamic Partnership between TFIIH, PGC-1α and SIRT1 Is Impaired in Trichothiodystrophy

    doi: 10.1371/journal.pgen.1004732

    Figure Lengend Snippet: TFIIH influences PGC-1α deacetylation by SIRT1 by interacting with both. ( panel A ) After immunoprecipitation of PGC-1α from nuclear extracts of WT (lanes 1–2) and TTD (lanes 3–5) hepatocytes, co-immunoprecipitated proteins were visualized by western blots with antibodies raised against PGC-1α (110 kDa), SIRT1 (110 kDa) and the p62 subunit (62 kDa). TTD nuclear extract was supplemented with recombinant TFIIH (rIIH, lane 5). ( panel B ) When indicated (+), GST-PGC-1α purified from bacteria (130 kDa) was incubated with lysate of Sf9 cells overexpressing TFIIH (rIIH). After immunoprecipitation with an anti Flag-Tag antibody (that recognized the flagged XPB subunit, 89 kDa), the bound proteins were visualized by western blots using antibodies raised against PGC-1α and XPB. ( panel C ) Purified SIRT1 (110 kDa) was incubated with lysate of Sf9 cells overexpressing TFIIH (rIIH). Immunoprecipitations were performed as described panel B. The bound proteins were visualized by western blots using antibodies raised against SIRT1 and XPB. ( panel D ) In vitro pull-down assays were performed with GST alone (-, 26 kDa, lanes 2) or GST-PGC-1α (PGC-1α, 130 kDa, lanes 3) incubated with Sf9 cell extracts overexpressing separately each subunit of TFIIH. The bound proteins were visualized by western blots using antibodies directed against each TFIIH subunit. As a reference, the input lanes (IN, lanes 1) represent 10% of the total volume of extract used for each incubation. ( panel E ) Purified SIRT1 was incubated with Sf9 cell extracts overexpressing separately each TFIIH subunit. Immunoprecipitations (IP) were done using antibodies directed against the TFIIH subunits. The bound proteins were revealed by western blots. ( panel F ) Deacetylation profile of PGC-1α in WT (lanes 1–3) and TTD (lanes 4–6) hepatocytes after different times of pyruvate treatment (0, 4 and 6 hours). After immunoprecipitation with specific antibodies (IP Ab-PGC-1α), PGC-1α acetylation has been visualized by western blots with anti-acetyl lysine antibodies. Graph depicts the ratio of acetyl-Lysine (Ac-Lys)/PGC-1α western blots signals. ( panel G ) PGC-1α was immunoprecipitated with specific antibodies (IP Ab-PGC-1α) from nuclear extracts of WT (lanes 1–3) and TTD (lanes 4–6) hepatocytes after different times of pyruvate treatment (0, 4 and 6 hours). Co-immunoprecipitated proteins were visualized by western blots with anti-PGC-1α and -SIRT1 antibodies. Graph depicts the binding ratio between SIRT1 and PGC-1α.

    Article Snippet: Plasmids and construction of PGC-1α and SIRT1 Full-length human SIRT1 and mouse PGC-1α were obtained from Addgene (plasmid #13735 and #1026, respectively).

    Techniques: Pyrolysis Gas Chromatography, Immunoprecipitation, Western Blot, Recombinant, Purification, Incubation, FLAG-tag, In Vitro, Binding Assay

    Dynamic partnership between TFIIH, PGC-1α and SIRT1. ( panel A ) SIRT1 and TFIIH bind to PGC-1α independently to its acetylation status. After immunoprecipitation with specific antibodies (IP Ab-PGC-1α), non acetylated (PGC-1α, lanes 2–3) and acetylated PGC-1α (Ac-PGC-1α, lanes 4–5) were incubated with purified SIRT1 and recombinant TFIIH (rIIH). When indicated (+), specific SIRT1 inhibitor (SIRT1 inh., 10 µM) was also added. Co-immunoprecipitated proteins were visualized by western blots with anti-PGC-1α, -acetyl-Lysine, -p62 and -SIRT1 antibodies. (panel B) In vitro phosphorylation of SIRT1. When indicated (+), GST-C-terminal domain of the largest subunit of the RNA pol II (GST-CTD, 90 kDa) (used as positive control, lanes 1–2) [53] , PGC-1α (130 kDa, lanes 3–4) and SIRT1 (110 kDa, lanes 5–6) were incubated with recombinant TFIIH (rIIH) in the presence of [γ- 32 P] ATP and CDK7 inhibitor (CDK7 inh.). Coomassie blue staining gel (top panels) and autoradiography (bottom panels) of the incubated fractions are shown. (panels C–G) When indicated (+), SIRT1 (110 kDa), PGC-1α(130 kDa, ATP (100 nM), CDK7 inhibitor (CDK7 inh.) and non-hydrolyzable ATP analog (ATP-γS, 100 nM) were incubated with either immunoprecipitated recombinant TFIIH with WT XPD subunit (rIIH XPD/WT, panel C ), recombinant TFIIH with mutated XPD (rIIH XPD/R722W, panel D ), core-TFIIH without XPD ( panel E ), XPB subunit ( panel F ) or mutated XPB bearing the point mutation K346R (XPB/K346R, panel G ). Co-immunoprecipitated proteins were visualized by western blots using anti-SIRT1, -PGC-1α, -p62 and -XPB antibodies. Graphs depict the binding of PGC-1α and SIRT1.

    Journal: PLoS Genetics

    Article Title: Dynamic Partnership between TFIIH, PGC-1α and SIRT1 Is Impaired in Trichothiodystrophy

    doi: 10.1371/journal.pgen.1004732

    Figure Lengend Snippet: Dynamic partnership between TFIIH, PGC-1α and SIRT1. ( panel A ) SIRT1 and TFIIH bind to PGC-1α independently to its acetylation status. After immunoprecipitation with specific antibodies (IP Ab-PGC-1α), non acetylated (PGC-1α, lanes 2–3) and acetylated PGC-1α (Ac-PGC-1α, lanes 4–5) were incubated with purified SIRT1 and recombinant TFIIH (rIIH). When indicated (+), specific SIRT1 inhibitor (SIRT1 inh., 10 µM) was also added. Co-immunoprecipitated proteins were visualized by western blots with anti-PGC-1α, -acetyl-Lysine, -p62 and -SIRT1 antibodies. (panel B) In vitro phosphorylation of SIRT1. When indicated (+), GST-C-terminal domain of the largest subunit of the RNA pol II (GST-CTD, 90 kDa) (used as positive control, lanes 1–2) [53] , PGC-1α (130 kDa, lanes 3–4) and SIRT1 (110 kDa, lanes 5–6) were incubated with recombinant TFIIH (rIIH) in the presence of [γ- 32 P] ATP and CDK7 inhibitor (CDK7 inh.). Coomassie blue staining gel (top panels) and autoradiography (bottom panels) of the incubated fractions are shown. (panels C–G) When indicated (+), SIRT1 (110 kDa), PGC-1α(130 kDa, ATP (100 nM), CDK7 inhibitor (CDK7 inh.) and non-hydrolyzable ATP analog (ATP-γS, 100 nM) were incubated with either immunoprecipitated recombinant TFIIH with WT XPD subunit (rIIH XPD/WT, panel C ), recombinant TFIIH with mutated XPD (rIIH XPD/R722W, panel D ), core-TFIIH without XPD ( panel E ), XPB subunit ( panel F ) or mutated XPB bearing the point mutation K346R (XPB/K346R, panel G ). Co-immunoprecipitated proteins were visualized by western blots using anti-SIRT1, -PGC-1α, -p62 and -XPB antibodies. Graphs depict the binding of PGC-1α and SIRT1.

    Article Snippet: Plasmids and construction of PGC-1α and SIRT1 Full-length human SIRT1 and mouse PGC-1α were obtained from Addgene (plasmid #13735 and #1026, respectively).

    Techniques: Pyrolysis Gas Chromatography, Immunoprecipitation, Incubation, Purification, Recombinant, Western Blot, In Vitro, Positive Control, Staining, Autoradiography, Mutagenesis, Binding Assay

    Dysregulation of gluconeogenesis-induced proteins in TTD liver. PEPCK ( panel A ) and G6Pase ( panel B ) immunostainings of liver sections from ad libitum (sections 1–2) and 48 h fasted (sections 3–4) WT and TTD mice. PV = Portal Vein; CV = Central vein. Magnification is indicated at the bottom left of each part. Expression of the hepatic fasting-induced Pepck ( panel C ) and G6pase ( panel D ) genes in WT (black boxes, n = 4) and TTD (open boxes, n = 4) fed normally or fasted for 24 h or 48 h. Results are expressed as the mean normalized to 18S RNA. ( panel E ) Western Blot analyses of PGC-1α (110 kDa) levels in the liver of three WT and three TTD fed normally (lanes 1–6) or fasted for 48 h (lanes 7–12). TBP (TATA box Binding Protein, 36 kDa) has been used as an internal control. Diagram represents the mean of the ratios between PGC-1α and TBP for each group. ( panel F ) Expression of the Pgc-1α gene in WT (black boxes, n = 4) and TTD (open boxes, n = 4) fed normally or fasted for 24 h or 48 h. Results are expressed as the mean normalized to 18S RNA. Error bars represent standard deviations. The statistical symbols reflect significant differences between genotypes (**, p

    Journal: PLoS Genetics

    Article Title: Dynamic Partnership between TFIIH, PGC-1α and SIRT1 Is Impaired in Trichothiodystrophy

    doi: 10.1371/journal.pgen.1004732

    Figure Lengend Snippet: Dysregulation of gluconeogenesis-induced proteins in TTD liver. PEPCK ( panel A ) and G6Pase ( panel B ) immunostainings of liver sections from ad libitum (sections 1–2) and 48 h fasted (sections 3–4) WT and TTD mice. PV = Portal Vein; CV = Central vein. Magnification is indicated at the bottom left of each part. Expression of the hepatic fasting-induced Pepck ( panel C ) and G6pase ( panel D ) genes in WT (black boxes, n = 4) and TTD (open boxes, n = 4) fed normally or fasted for 24 h or 48 h. Results are expressed as the mean normalized to 18S RNA. ( panel E ) Western Blot analyses of PGC-1α (110 kDa) levels in the liver of three WT and three TTD fed normally (lanes 1–6) or fasted for 48 h (lanes 7–12). TBP (TATA box Binding Protein, 36 kDa) has been used as an internal control. Diagram represents the mean of the ratios between PGC-1α and TBP for each group. ( panel F ) Expression of the Pgc-1α gene in WT (black boxes, n = 4) and TTD (open boxes, n = 4) fed normally or fasted for 24 h or 48 h. Results are expressed as the mean normalized to 18S RNA. Error bars represent standard deviations. The statistical symbols reflect significant differences between genotypes (**, p

    Article Snippet: Plasmids and construction of PGC-1α and SIRT1 Full-length human SIRT1 and mouse PGC-1α were obtained from Addgene (plasmid #13735 and #1026, respectively).

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

    Defective recruitments of transcription factors on the promoter of gluconeogenic genes in TTD hepatocytes. Expression of Pgc-1α ( panel A1 ) Pepck ( panel B1 ) and G6Pase ( panel C1 ) genes in WT (solid curves), TTD (dashed curves) and TTD overexpressing XPDwt (dotted curves) hepatocytes after pyruvate treatment. The results are presented as n-fold induction relative to non-treated cells. Recruitment of RNA pol II, p62, CDK7, PGC-1α and SIRT1 on the proximal promoter of PGC-1α ( panels A2 to A6 ), PEPCK ( panels B2 to B6 ) and G6Pase ( panels C2 to C6 ) in WT (dotted curves) and TTD (dashed curves) hepatocytes. The results of three independent experiments are presented as percentage of DNA immunoprecipitated relative to the input. The shaded areas underline the concomitant recruitments of the transcription factors with the expression profile of the target genes in WT hepatocytes. ( panel D ) Western blot analyses of TFIIH, illustrated by its p62 (62 kDa) and CDK7 (39 kDa) subunits, PGC-1α (110 kDa) and SIRT1 (110 kDa) with increasing amounts of whole cell extracts isolated from WT (lanes 1–3) and TTD (lanes 4–6) hepatocytes. β-tubulin (β-Tub, 50 kDa) has been used as an internal control. * indicates unspecific band. Measurement of intracellular glucose 6-phosphate ( panel E ) and glucose output ( panel F ) levels from WT (black boxes) and TTD (open boxes) hepatocytes after 0 and 12 hours of pyruvate treatment. Values represent the means ± SEM. The statistical symbols reflect significant differences between genotypes (*, p

    Journal: PLoS Genetics

    Article Title: Dynamic Partnership between TFIIH, PGC-1α and SIRT1 Is Impaired in Trichothiodystrophy

    doi: 10.1371/journal.pgen.1004732

    Figure Lengend Snippet: Defective recruitments of transcription factors on the promoter of gluconeogenic genes in TTD hepatocytes. Expression of Pgc-1α ( panel A1 ) Pepck ( panel B1 ) and G6Pase ( panel C1 ) genes in WT (solid curves), TTD (dashed curves) and TTD overexpressing XPDwt (dotted curves) hepatocytes after pyruvate treatment. The results are presented as n-fold induction relative to non-treated cells. Recruitment of RNA pol II, p62, CDK7, PGC-1α and SIRT1 on the proximal promoter of PGC-1α ( panels A2 to A6 ), PEPCK ( panels B2 to B6 ) and G6Pase ( panels C2 to C6 ) in WT (dotted curves) and TTD (dashed curves) hepatocytes. The results of three independent experiments are presented as percentage of DNA immunoprecipitated relative to the input. The shaded areas underline the concomitant recruitments of the transcription factors with the expression profile of the target genes in WT hepatocytes. ( panel D ) Western blot analyses of TFIIH, illustrated by its p62 (62 kDa) and CDK7 (39 kDa) subunits, PGC-1α (110 kDa) and SIRT1 (110 kDa) with increasing amounts of whole cell extracts isolated from WT (lanes 1–3) and TTD (lanes 4–6) hepatocytes. β-tubulin (β-Tub, 50 kDa) has been used as an internal control. * indicates unspecific band. Measurement of intracellular glucose 6-phosphate ( panel E ) and glucose output ( panel F ) levels from WT (black boxes) and TTD (open boxes) hepatocytes after 0 and 12 hours of pyruvate treatment. Values represent the means ± SEM. The statistical symbols reflect significant differences between genotypes (*, p

    Article Snippet: Plasmids and construction of PGC-1α and SIRT1 Full-length human SIRT1 and mouse PGC-1α were obtained from Addgene (plasmid #13735 and #1026, respectively).

    Techniques: Expressing, Pyrolysis Gas Chromatography, Immunoprecipitation, Western Blot, Isolation

    Model of the dynamic partnership between TFIIH, PGC-1α and SIRT1. SIRT1 and PGC-1α physically interact with various subunits of the TFIIH complex: SIRT1 interacts with XPB, p62, cdk7 and MAT1, while PGC-1α interacts with XPB, p34 and MAT1. SIRT1 binds to TFIIH alone, but its interaction is reinforced by the presence of PGC-1α. The simultaneous interaction between TFIIH, PGC-1α and SIRT1 suggests that TFIIH might contribute to the PGC-1α deacetylation by SIRT1. Such assumption is supported by the fact that i) the integrity of TFIIH is crucial for the optimal binding of PGC-1α and SIRT1 and ii) the PGC-1α deacetylation is disrupted by XPD mutation (such as XPD/R722W) that affects the integrity of TFIIH. In parallel, the CDK7 kinase of TFIIH targets SIRT1, but the function of such phosphorylation(s) remains elusive. Finally, the binding of ATP to the XPB subunit of TFIIH influences the release of PGC-1α, which in turn affects the binding of SIRT1.

    Journal: PLoS Genetics

    Article Title: Dynamic Partnership between TFIIH, PGC-1α and SIRT1 Is Impaired in Trichothiodystrophy

    doi: 10.1371/journal.pgen.1004732

    Figure Lengend Snippet: Model of the dynamic partnership between TFIIH, PGC-1α and SIRT1. SIRT1 and PGC-1α physically interact with various subunits of the TFIIH complex: SIRT1 interacts with XPB, p62, cdk7 and MAT1, while PGC-1α interacts with XPB, p34 and MAT1. SIRT1 binds to TFIIH alone, but its interaction is reinforced by the presence of PGC-1α. The simultaneous interaction between TFIIH, PGC-1α and SIRT1 suggests that TFIIH might contribute to the PGC-1α deacetylation by SIRT1. Such assumption is supported by the fact that i) the integrity of TFIIH is crucial for the optimal binding of PGC-1α and SIRT1 and ii) the PGC-1α deacetylation is disrupted by XPD mutation (such as XPD/R722W) that affects the integrity of TFIIH. In parallel, the CDK7 kinase of TFIIH targets SIRT1, but the function of such phosphorylation(s) remains elusive. Finally, the binding of ATP to the XPB subunit of TFIIH influences the release of PGC-1α, which in turn affects the binding of SIRT1.

    Article Snippet: Plasmids and construction of PGC-1α and SIRT1 Full-length human SIRT1 and mouse PGC-1α were obtained from Addgene (plasmid #13735 and #1026, respectively).

    Techniques: Pyrolysis Gas Chromatography, Binding Assay, Mutagenesis

    Mouse podocyte and renal mesangial cell impairment by high glucose concentrations. (A) Effect of high glucose on PGC-1α, PPRC1, PPARγ, NRF1, NDUFS1 and COX4I1 mRNA expression. Mouse podocytes were cultured in 30 mM glucose medium for 24 or 48 h. Medium containing 5.5 mM glucose with 24.5 mM mannitol was applied as control. *P

    Journal: Molecular Medicine Reports

    Article Title: PGC-1α ameliorates kidney fibrosis in mice with diabetic kidney disease through an antioxidative mechanism

    doi: 10.3892/mmr.2018.8433

    Figure Lengend Snippet: Mouse podocyte and renal mesangial cell impairment by high glucose concentrations. (A) Effect of high glucose on PGC-1α, PPRC1, PPARγ, NRF1, NDUFS1 and COX4I1 mRNA expression. Mouse podocytes were cultured in 30 mM glucose medium for 24 or 48 h. Medium containing 5.5 mM glucose with 24.5 mM mannitol was applied as control. *P

    Article Snippet: For nuclear or cytoplasmic proteins of renal cortex tissues and total proteins of SV40 MES 13 mouse mesangial cells anti-PGC-1α (cat. no. ab3242; 1:1,000; EMD Millipore) was used.

    Techniques: Pyrolysis Gas Chromatography, Expressing, Cell Culture

    Effect of PGC-1α knockdown or overexpression on high glucose-induced ROS generation in mesangial cells. (A) Confirmation of PGC-1α expression in SV40 MES 13 cells transfected with pcDNA3.1-vector (lane 1) or pcDNA3.1-PGC-1α (lane 2) by western blotting and the corresponding relative quantification of average band intensity. Data are presented as the mean ± standard deviation (n=3). (B) Intracellular ROS levels were detected in SV40 MES 13 cells following high glucose treatment in the PGC-1α overexpression or control vector transfection groups using a fluorescence microplate reader. Data are presented as a percentage of the control group (pcDNA3.1-vector D-mannitol). The experiment was repeated three times (n=6 per group). (C) Confirmation of PGC-1α mRNA expression by reverse transcription-quantitative polymerase chain reaction in SV40 MES 13 cells transduced with shRNA-control or shRNA-PGC-1α (n=3). (D) ROS levels in SV40 MES 13 cells transduced with control or PGC-1α shRNA and treated with D-glucose or D-mannitol were measured and presented as a percentage of the control group (shRNA-control D-mannitol) Three independent protein preparations were each run in 6 samples. All data are presented as the mean ± standard deviation. *P

    Journal: Molecular Medicine Reports

    Article Title: PGC-1α ameliorates kidney fibrosis in mice with diabetic kidney disease through an antioxidative mechanism

    doi: 10.3892/mmr.2018.8433

    Figure Lengend Snippet: Effect of PGC-1α knockdown or overexpression on high glucose-induced ROS generation in mesangial cells. (A) Confirmation of PGC-1α expression in SV40 MES 13 cells transfected with pcDNA3.1-vector (lane 1) or pcDNA3.1-PGC-1α (lane 2) by western blotting and the corresponding relative quantification of average band intensity. Data are presented as the mean ± standard deviation (n=3). (B) Intracellular ROS levels were detected in SV40 MES 13 cells following high glucose treatment in the PGC-1α overexpression or control vector transfection groups using a fluorescence microplate reader. Data are presented as a percentage of the control group (pcDNA3.1-vector D-mannitol). The experiment was repeated three times (n=6 per group). (C) Confirmation of PGC-1α mRNA expression by reverse transcription-quantitative polymerase chain reaction in SV40 MES 13 cells transduced with shRNA-control or shRNA-PGC-1α (n=3). (D) ROS levels in SV40 MES 13 cells transduced with control or PGC-1α shRNA and treated with D-glucose or D-mannitol were measured and presented as a percentage of the control group (shRNA-control D-mannitol) Three independent protein preparations were each run in 6 samples. All data are presented as the mean ± standard deviation. *P

    Article Snippet: For nuclear or cytoplasmic proteins of renal cortex tissues and total proteins of SV40 MES 13 mouse mesangial cells anti-PGC-1α (cat. no. ab3242; 1:1,000; EMD Millipore) was used.

    Techniques: Pyrolysis Gas Chromatography, Over Expression, Expressing, Transfection, Plasmid Preparation, Western Blot, Standard Deviation, Fluorescence, Real-time Polymerase Chain Reaction, Transduction, shRNA

    The relationship between the protein expression levels of PGC-1α and NT-PGC-1α and the doses of metformin in mice after MI. ( A ) The protein expression level of PGC-1α and NT-PGC-1α treated with different doses of metformin (50–200 mg/kg/d) in the MI mice. ( B ) The quantity of protein expression level of PGC-1α and NT-PGC-1α treated with different doses of metformin (50–200 mg/kg/d) in the MI mice.

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Metformin Increases Cardiac Rupture After Myocardial Infarction via the AMPK-MTOR/PGC-1α Signaling Pathway in Rats with Acute Myocardial Infarction

    doi: 10.12659/MSM.910930

    Figure Lengend Snippet: The relationship between the protein expression levels of PGC-1α and NT-PGC-1α and the doses of metformin in mice after MI. ( A ) The protein expression level of PGC-1α and NT-PGC-1α treated with different doses of metformin (50–200 mg/kg/d) in the MI mice. ( B ) The quantity of protein expression level of PGC-1α and NT-PGC-1α treated with different doses of metformin (50–200 mg/kg/d) in the MI mice.

    Article Snippet: Main reagents Reagents used were pentobarbital sodium (SIGMA, Japan); metformin (purity ≥95%) (SIGMA, Japan); Trizol RNA extraction kit (Invitrogen, USA); RT-PCR two-step kit (TaKaRa, Japan); PCR primers: Synthesized by Shenggong Bio Co. (Guangzhou, China); anti-mouse PGC-1α antibody (Abcam, USA); anti-mouse β-actin antibody (Bioscience, USA); BCA protein quantification kit (Ding Chang Guotai, China); ECL chemiluminescence liquid (Fode, China); HRP-labeled anti-rabbit secondary antibody (Boosen, USA); Masson Staining Kit (Bogu, China); and TUNEL Staining Kit (Roche, Switzerland).

    Techniques: Expressing, Pyrolysis Gas Chromatography, Mouse Assay

    Ratio of NT- PGC-1α/PGC-1α. The proportion of myocardial NT-PGC-1α/PGC-1α in the infarcted area of the MI group was lower than that in the Non-MI group, while the proportion of myocardial NT-PGC-1α/PGC-1α in the junctional and distant myocardial areas was higher than that in the Non-MI group.

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Metformin Increases Cardiac Rupture After Myocardial Infarction via the AMPK-MTOR/PGC-1α Signaling Pathway in Rats with Acute Myocardial Infarction

    doi: 10.12659/MSM.910930

    Figure Lengend Snippet: Ratio of NT- PGC-1α/PGC-1α. The proportion of myocardial NT-PGC-1α/PGC-1α in the infarcted area of the MI group was lower than that in the Non-MI group, while the proportion of myocardial NT-PGC-1α/PGC-1α in the junctional and distant myocardial areas was higher than that in the Non-MI group.

    Article Snippet: Main reagents Reagents used were pentobarbital sodium (SIGMA, Japan); metformin (purity ≥95%) (SIGMA, Japan); Trizol RNA extraction kit (Invitrogen, USA); RT-PCR two-step kit (TaKaRa, Japan); PCR primers: Synthesized by Shenggong Bio Co. (Guangzhou, China); anti-mouse PGC-1α antibody (Abcam, USA); anti-mouse β-actin antibody (Bioscience, USA); BCA protein quantification kit (Ding Chang Guotai, China); ECL chemiluminescence liquid (Fode, China); HRP-labeled anti-rabbit secondary antibody (Boosen, USA); Masson Staining Kit (Bogu, China); and TUNEL Staining Kit (Roche, Switzerland).

    Techniques: Pyrolysis Gas Chromatography

    The relation between PGC-1α NT-PGC-1αexpression and the location of Myocardial area. ( A ) The protein expression level of PGC-1α in infarcted, junctional, and distant myocardial areas of the non-cardiac rupture and MI groups. ( B ) The quantity of protein expression level of PGC-1α in infarcted, junctional, and distant myocardial areas of non-cardiac rupture and MI groups, which was higher in the MI group than in the Non-MI group, and the difference among the levels in the junctional area was the most significant. The expression level of NT-PGC-1α in the junctional area of the MI group was higher than that in the Non-MI group, while it was lower than that in the infarcted and distant myocardial areas of Non-MI.

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Metformin Increases Cardiac Rupture After Myocardial Infarction via the AMPK-MTOR/PGC-1α Signaling Pathway in Rats with Acute Myocardial Infarction

    doi: 10.12659/MSM.910930

    Figure Lengend Snippet: The relation between PGC-1α NT-PGC-1αexpression and the location of Myocardial area. ( A ) The protein expression level of PGC-1α in infarcted, junctional, and distant myocardial areas of the non-cardiac rupture and MI groups. ( B ) The quantity of protein expression level of PGC-1α in infarcted, junctional, and distant myocardial areas of non-cardiac rupture and MI groups, which was higher in the MI group than in the Non-MI group, and the difference among the levels in the junctional area was the most significant. The expression level of NT-PGC-1α in the junctional area of the MI group was higher than that in the Non-MI group, while it was lower than that in the infarcted and distant myocardial areas of Non-MI.

    Article Snippet: Main reagents Reagents used were pentobarbital sodium (SIGMA, Japan); metformin (purity ≥95%) (SIGMA, Japan); Trizol RNA extraction kit (Invitrogen, USA); RT-PCR two-step kit (TaKaRa, Japan); PCR primers: Synthesized by Shenggong Bio Co. (Guangzhou, China); anti-mouse PGC-1α antibody (Abcam, USA); anti-mouse β-actin antibody (Bioscience, USA); BCA protein quantification kit (Ding Chang Guotai, China); ECL chemiluminescence liquid (Fode, China); HRP-labeled anti-rabbit secondary antibody (Boosen, USA); Masson Staining Kit (Bogu, China); and TUNEL Staining Kit (Roche, Switzerland).

    Techniques: Pyrolysis Gas Chromatography, Expressing

    The relationship between the mRNA levels of PGC-1α and NT-PGC-1α and the doses of metformin in mice after MI. ( A ) The results of RT-PCR mRNA level of NT-PGC-1α and PGC-1α after being treated different doses of metformin. ( B ) The ratio of myocardial NT-PGC-1α/PGC-1α after being treated different doses of metformin. ( C ) The ratio of control group NT-PGC-1α/PGC-1α after being treated different doses of metformin. ** P

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Metformin Increases Cardiac Rupture After Myocardial Infarction via the AMPK-MTOR/PGC-1α Signaling Pathway in Rats with Acute Myocardial Infarction

    doi: 10.12659/MSM.910930

    Figure Lengend Snippet: The relationship between the mRNA levels of PGC-1α and NT-PGC-1α and the doses of metformin in mice after MI. ( A ) The results of RT-PCR mRNA level of NT-PGC-1α and PGC-1α after being treated different doses of metformin. ( B ) The ratio of myocardial NT-PGC-1α/PGC-1α after being treated different doses of metformin. ( C ) The ratio of control group NT-PGC-1α/PGC-1α after being treated different doses of metformin. ** P

    Article Snippet: Main reagents Reagents used were pentobarbital sodium (SIGMA, Japan); metformin (purity ≥95%) (SIGMA, Japan); Trizol RNA extraction kit (Invitrogen, USA); RT-PCR two-step kit (TaKaRa, Japan); PCR primers: Synthesized by Shenggong Bio Co. (Guangzhou, China); anti-mouse PGC-1α antibody (Abcam, USA); anti-mouse β-actin antibody (Bioscience, USA); BCA protein quantification kit (Ding Chang Guotai, China); ECL chemiluminescence liquid (Fode, China); HRP-labeled anti-rabbit secondary antibody (Boosen, USA); Masson Staining Kit (Bogu, China); and TUNEL Staining Kit (Roche, Switzerland).

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

    The protein expression of metformin on AMPK-mTORC/PGC-1α signaling pathway in SD- NRVCs. ( A ) Western blot analysis was used to detect the related gene expression levels of the AMPK-mTORC/PGC-1α signaling pathway. Expression levels of NT-PGC-1α/PGC-1α, mTOR, and AMPK p-AMPK protein level after treatment with different doses of metformin. ( B ) The quantity of protein expression level of NT-PGC-1α/PGC-1α, and AMPK p-AMPK protein level after treatment with different doses of metformin. ( C ) The quantity of protein expression level of mTOR protein level after treatment with different doses of metformin. ( D ) The ratio of p-AMPK/AMPK protein level after being treated with different doses of metformin. Data are presented as mean ±SD from 3 independent experiments. ** P

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Metformin Increases Cardiac Rupture After Myocardial Infarction via the AMPK-MTOR/PGC-1α Signaling Pathway in Rats with Acute Myocardial Infarction

    doi: 10.12659/MSM.910930

    Figure Lengend Snippet: The protein expression of metformin on AMPK-mTORC/PGC-1α signaling pathway in SD- NRVCs. ( A ) Western blot analysis was used to detect the related gene expression levels of the AMPK-mTORC/PGC-1α signaling pathway. Expression levels of NT-PGC-1α/PGC-1α, mTOR, and AMPK p-AMPK protein level after treatment with different doses of metformin. ( B ) The quantity of protein expression level of NT-PGC-1α/PGC-1α, and AMPK p-AMPK protein level after treatment with different doses of metformin. ( C ) The quantity of protein expression level of mTOR protein level after treatment with different doses of metformin. ( D ) The ratio of p-AMPK/AMPK protein level after being treated with different doses of metformin. Data are presented as mean ±SD from 3 independent experiments. ** P

    Article Snippet: Main reagents Reagents used were pentobarbital sodium (SIGMA, Japan); metformin (purity ≥95%) (SIGMA, Japan); Trizol RNA extraction kit (Invitrogen, USA); RT-PCR two-step kit (TaKaRa, Japan); PCR primers: Synthesized by Shenggong Bio Co. (Guangzhou, China); anti-mouse PGC-1α antibody (Abcam, USA); anti-mouse β-actin antibody (Bioscience, USA); BCA protein quantification kit (Ding Chang Guotai, China); ECL chemiluminescence liquid (Fode, China); HRP-labeled anti-rabbit secondary antibody (Boosen, USA); Masson Staining Kit (Bogu, China); and TUNEL Staining Kit (Roche, Switzerland).

    Techniques: Expressing, Pyrolysis Gas Chromatography, Western Blot

    The mRNA level of metformin on AMPK-mTORC/PGC-1α signaling pathway in SD-NRVCs. ( A–D ) RT-PCR was used to detect the related gene expression levels of AMPK-mTORC/PGC-1α signaling pathway. Expression levels of NT-PGC-1α/PGC-1α, mTOR, and mRNA after treatment with different doses of metformin.

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Metformin Increases Cardiac Rupture After Myocardial Infarction via the AMPK-MTOR/PGC-1α Signaling Pathway in Rats with Acute Myocardial Infarction

    doi: 10.12659/MSM.910930

    Figure Lengend Snippet: The mRNA level of metformin on AMPK-mTORC/PGC-1α signaling pathway in SD-NRVCs. ( A–D ) RT-PCR was used to detect the related gene expression levels of AMPK-mTORC/PGC-1α signaling pathway. Expression levels of NT-PGC-1α/PGC-1α, mTOR, and mRNA after treatment with different doses of metformin.

    Article Snippet: Main reagents Reagents used were pentobarbital sodium (SIGMA, Japan); metformin (purity ≥95%) (SIGMA, Japan); Trizol RNA extraction kit (Invitrogen, USA); RT-PCR two-step kit (TaKaRa, Japan); PCR primers: Synthesized by Shenggong Bio Co. (Guangzhou, China); anti-mouse PGC-1α antibody (Abcam, USA); anti-mouse β-actin antibody (Bioscience, USA); BCA protein quantification kit (Ding Chang Guotai, China); ECL chemiluminescence liquid (Fode, China); HRP-labeled anti-rabbit secondary antibody (Boosen, USA); Masson Staining Kit (Bogu, China); and TUNEL Staining Kit (Roche, Switzerland).

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

    In old mice, the soleus remains more oxidative than the tibialis anterior, and expresses higher levels of mitochondrial biogenesis, fission/fusion and autophagy markers. Markers for oxidative metabolism, mitochondrial biogenesis, fission/fusion and autophagy were evaluated in tibialis anterior and soleus muscles from old mice (28-29 mo). ( A-B ) Myoglobin and representative electron transport chain enzymes (OXPHOS) in whole muscle lysates were assessed by Western blotting and normalized to Ponceau-stained total protein (see Figure S3 ). The mean plus standard deviation of 3 technical replicates of lysates from 4 mice/group is shown. ( C-D ) Succinate dehydrogenase (SDH i.e. OXPHOS Complex II) activity was assessed by histochemical staining. Representative images are shown (C; tibialis anterior scale bar = 400 µm, soleus scale bar = 200 µm) and the SDH activity of the entire muscle sections (indicated by the red dotted lines i.e. the EDL and gastrocnemius were excluded) was evaluated by assessing pixel intensities (D; mean plus standard deviation of 3 mice/group, 2 sections per mouse). ( E ) PGC-1α, PGC-1β, Mfn2, short (S)- and long (L)-OPA1, LC3-II/I and APG5 in whole muscle lysates were evaluated by Western blotting and normalized to Ponceau-stained total protein (see Figure S3 ). The mean plus standard deviation of 3 technical replicates of lysates from 4 mice/group is shown. ( F ) Mfn2 and OPA1 in mitochondrial fractions were evaluated by Western blotting and normalized to Ponceau-stained total protein (see Figure S3 ). The mean plus standard deviation of lysates from 4 mice/group is shown. *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001, ****p ≤ 0.0001.

    Journal: Aging (Albany NY)

    Article Title: Oxidative muscles have better mitochondrial homeostasis than glycolytic muscles throughout life and maintain mitochondrial function during aging

    doi: 10.18632/aging.101643

    Figure Lengend Snippet: In old mice, the soleus remains more oxidative than the tibialis anterior, and expresses higher levels of mitochondrial biogenesis, fission/fusion and autophagy markers. Markers for oxidative metabolism, mitochondrial biogenesis, fission/fusion and autophagy were evaluated in tibialis anterior and soleus muscles from old mice (28-29 mo). ( A-B ) Myoglobin and representative electron transport chain enzymes (OXPHOS) in whole muscle lysates were assessed by Western blotting and normalized to Ponceau-stained total protein (see Figure S3 ). The mean plus standard deviation of 3 technical replicates of lysates from 4 mice/group is shown. ( C-D ) Succinate dehydrogenase (SDH i.e. OXPHOS Complex II) activity was assessed by histochemical staining. Representative images are shown (C; tibialis anterior scale bar = 400 µm, soleus scale bar = 200 µm) and the SDH activity of the entire muscle sections (indicated by the red dotted lines i.e. the EDL and gastrocnemius were excluded) was evaluated by assessing pixel intensities (D; mean plus standard deviation of 3 mice/group, 2 sections per mouse). ( E ) PGC-1α, PGC-1β, Mfn2, short (S)- and long (L)-OPA1, LC3-II/I and APG5 in whole muscle lysates were evaluated by Western blotting and normalized to Ponceau-stained total protein (see Figure S3 ). The mean plus standard deviation of 3 technical replicates of lysates from 4 mice/group is shown. ( F ) Mfn2 and OPA1 in mitochondrial fractions were evaluated by Western blotting and normalized to Ponceau-stained total protein (see Figure S3 ). The mean plus standard deviation of lysates from 4 mice/group is shown. *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001, ****p ≤ 0.0001.

    Article Snippet: Primary antibodies were incubated overnight at the following dilutions/concentrations: anti-mouse total OXPHOS rodent WB Antibody (EPR12370, Abcam, Burlingame, CA; 1:1000 (1.5 nM)), anti-mouse Myoglobin (A-9) (sc-74525, Santa Cruz Biotechnology, Santa Cruz, CA; 1:1000 (0.2 nM)), anti-mouse OPA1 (BD Transduction LaboratoriesTM , La Jolla, CA; 1:500 (0.5 nM)), anti-mouse PGC-1α (Abcam, Burlingame, CA; 1:1000 (0.1 nM)), anti-mouse PGC-1β (Abcam, Burlingame, CA; 1:500 0.2 nM), Mfn2 (sc-100560, Santa Cruz Biotechnology, Santa Cruz, CA; 1:500 (0.2 nM)), LC3A/B (Cell Signaling, Danvers, MA; 1:1000), APG5 (C-1, sc-133158, Santa Cruz Biotechnology, Santa Cruz, CA; 1:1000 (0.2 nM)), p62 (BD Transduction LaboratoriesTM ; 1:500 (0.5 nM)).

    Techniques: Mouse Assay, Western Blot, Staining, Standard Deviation, Activity Assay, Pyrolysis Gas Chromatography

    Upon aging, the tibialis anterior and soleus undergo similar changes in mitochondrial biogenesis, fission/fusion, disposal and autophagy marker expression. Markers of mitochondrial biogenesis, fission/fusion, disposal and autophagy were evaluated in tibialis anterior ( A, C ) and soleus ( B, D ) muscles isolated from young (3 mo) and old (29 mo) mice. A-B) Representative OXPHOS subunits, PGC-1α, PGC-1β, Mfn2, short (S)- and long (L)-OPA1, LC3-II/I, and APG5 in whole muscle lysates were evaluated by Western blotting and normalized to Ponceau-stained total protein (see Figures S6 , S7 ). The mean plus standard deviation of 3 technical replicates of lysates from 4-5 mice/group is shown; 3 mo (n=5), 29 mo (n=4). C-D) Mfn2, OPA1, and p62 levels in mitochondrial fractions were evaluated by Western blotting and normalized to Ponceau-stained total protein (see Figure S7 ). The mean plus standard deviation of lysates from 4 mice/group run on 2 separate gels is shown. *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001, ****p ≤ 0.0001.

    Journal: Aging (Albany NY)

    Article Title: Oxidative muscles have better mitochondrial homeostasis than glycolytic muscles throughout life and maintain mitochondrial function during aging

    doi: 10.18632/aging.101643

    Figure Lengend Snippet: Upon aging, the tibialis anterior and soleus undergo similar changes in mitochondrial biogenesis, fission/fusion, disposal and autophagy marker expression. Markers of mitochondrial biogenesis, fission/fusion, disposal and autophagy were evaluated in tibialis anterior ( A, C ) and soleus ( B, D ) muscles isolated from young (3 mo) and old (29 mo) mice. A-B) Representative OXPHOS subunits, PGC-1α, PGC-1β, Mfn2, short (S)- and long (L)-OPA1, LC3-II/I, and APG5 in whole muscle lysates were evaluated by Western blotting and normalized to Ponceau-stained total protein (see Figures S6 , S7 ). The mean plus standard deviation of 3 technical replicates of lysates from 4-5 mice/group is shown; 3 mo (n=5), 29 mo (n=4). C-D) Mfn2, OPA1, and p62 levels in mitochondrial fractions were evaluated by Western blotting and normalized to Ponceau-stained total protein (see Figure S7 ). The mean plus standard deviation of lysates from 4 mice/group run on 2 separate gels is shown. *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001, ****p ≤ 0.0001.

    Article Snippet: Primary antibodies were incubated overnight at the following dilutions/concentrations: anti-mouse total OXPHOS rodent WB Antibody (EPR12370, Abcam, Burlingame, CA; 1:1000 (1.5 nM)), anti-mouse Myoglobin (A-9) (sc-74525, Santa Cruz Biotechnology, Santa Cruz, CA; 1:1000 (0.2 nM)), anti-mouse OPA1 (BD Transduction LaboratoriesTM , La Jolla, CA; 1:500 (0.5 nM)), anti-mouse PGC-1α (Abcam, Burlingame, CA; 1:1000 (0.1 nM)), anti-mouse PGC-1β (Abcam, Burlingame, CA; 1:500 0.2 nM), Mfn2 (sc-100560, Santa Cruz Biotechnology, Santa Cruz, CA; 1:500 (0.2 nM)), LC3A/B (Cell Signaling, Danvers, MA; 1:1000), APG5 (C-1, sc-133158, Santa Cruz Biotechnology, Santa Cruz, CA; 1:1000 (0.2 nM)), p62 (BD Transduction LaboratoriesTM ; 1:500 (0.5 nM)).

    Techniques: Marker, Expressing, Isolation, Mouse Assay, Pyrolysis Gas Chromatography, Western Blot, Staining, Standard Deviation

    In young mice, the soleus is more oxidative than the tibialis anterior, and expresses higher levels of mitochondrial biogenesis, fission/fusion and autophagy markers. Markers of oxidative metabolism, mitochondrial biogenesis, fission/fusion and autophagy were evaluated in tibialis anterior and soleus muscles from young (3 mo) mice. ( A-B ) Myoglobin and representative electron transport chain enzymes (OXPHOS) in whole muscle lysates were assessed by Western blotting and normalized to Ponceau-stained total protein (see Figure S1 ). The mean plus standard deviation of 3 technical replicates of lysates from 5 mice/group is shown. ( C-D ) Succinate dehydrogenase (SDH i.e. OXPHOS Complex II) activity was assessed by histochemical staining. Representative images are shown (C; tibialis anterior scale bar = 400 µm, soleus scale bar = 200 µm) and the SDH activity of the entire muscle sections (indicated by the red dotted lines i.e. the EDL and gastrocnemius were excluded) was evaluated by assessing pixel intensities (D; mean plus standard deviation of 3 mice/group, 2 sections per mouse). ( E ) PGC-1α, PGC-1β, Mfn2, short (S)- and long (L)-OPA1, LC3-II/I and APG5 in whole muscle lysates were evaluated by Western blotting and normalized to Ponceau-stained total protein (see Figure S1 ). The mean plus standard deviation of 3 technical replicates of lysates from 5 mice/group is shown. ( F ) Mfn2 and OPA1 in mitochondrial fractions were evaluated by Western blotting and normalized to Ponceau-stained total protein (see Figure S1 ). The mean plus standard deviation of lysates from 4 mice/group is shown. *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001, ****p ≤ 0.0001.

    Journal: Aging (Albany NY)

    Article Title: Oxidative muscles have better mitochondrial homeostasis than glycolytic muscles throughout life and maintain mitochondrial function during aging

    doi: 10.18632/aging.101643

    Figure Lengend Snippet: In young mice, the soleus is more oxidative than the tibialis anterior, and expresses higher levels of mitochondrial biogenesis, fission/fusion and autophagy markers. Markers of oxidative metabolism, mitochondrial biogenesis, fission/fusion and autophagy were evaluated in tibialis anterior and soleus muscles from young (3 mo) mice. ( A-B ) Myoglobin and representative electron transport chain enzymes (OXPHOS) in whole muscle lysates were assessed by Western blotting and normalized to Ponceau-stained total protein (see Figure S1 ). The mean plus standard deviation of 3 technical replicates of lysates from 5 mice/group is shown. ( C-D ) Succinate dehydrogenase (SDH i.e. OXPHOS Complex II) activity was assessed by histochemical staining. Representative images are shown (C; tibialis anterior scale bar = 400 µm, soleus scale bar = 200 µm) and the SDH activity of the entire muscle sections (indicated by the red dotted lines i.e. the EDL and gastrocnemius were excluded) was evaluated by assessing pixel intensities (D; mean plus standard deviation of 3 mice/group, 2 sections per mouse). ( E ) PGC-1α, PGC-1β, Mfn2, short (S)- and long (L)-OPA1, LC3-II/I and APG5 in whole muscle lysates were evaluated by Western blotting and normalized to Ponceau-stained total protein (see Figure S1 ). The mean plus standard deviation of 3 technical replicates of lysates from 5 mice/group is shown. ( F ) Mfn2 and OPA1 in mitochondrial fractions were evaluated by Western blotting and normalized to Ponceau-stained total protein (see Figure S1 ). The mean plus standard deviation of lysates from 4 mice/group is shown. *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001, ****p ≤ 0.0001.

    Article Snippet: Primary antibodies were incubated overnight at the following dilutions/concentrations: anti-mouse total OXPHOS rodent WB Antibody (EPR12370, Abcam, Burlingame, CA; 1:1000 (1.5 nM)), anti-mouse Myoglobin (A-9) (sc-74525, Santa Cruz Biotechnology, Santa Cruz, CA; 1:1000 (0.2 nM)), anti-mouse OPA1 (BD Transduction LaboratoriesTM , La Jolla, CA; 1:500 (0.5 nM)), anti-mouse PGC-1α (Abcam, Burlingame, CA; 1:1000 (0.1 nM)), anti-mouse PGC-1β (Abcam, Burlingame, CA; 1:500 0.2 nM), Mfn2 (sc-100560, Santa Cruz Biotechnology, Santa Cruz, CA; 1:500 (0.2 nM)), LC3A/B (Cell Signaling, Danvers, MA; 1:1000), APG5 (C-1, sc-133158, Santa Cruz Biotechnology, Santa Cruz, CA; 1:1000 (0.2 nM)), p62 (BD Transduction LaboratoriesTM ; 1:500 (0.5 nM)).

    Techniques: Mouse Assay, Western Blot, Staining, Standard Deviation, Activity Assay, Pyrolysis Gas Chromatography

    Effect of TPEN on hsp60, SOD2, and OXPHOS proteins, mitochondrial biogenesis regulators, and mtDNA level in human HepG2 cells. Human HepG2 cells were treated with 3 μM TPEN without FBS for 6 h. A : immunoblot bands of hsp60 and SOD2. B : immunoblot bands of OXPHOS proteins, subunit of complex I (CI-NDUFB8), subunit of complex II (CII-SDHB), subunit of complex III (CIII-UQCRC2), subunit of complex IV (CIV-MTCO1), and subunit of complex V (CV-ATP5A). C : immunoblot bands of p-AMPK, AMPK, PGC1α, NRF1, and TFAM. D : mtDNA level was measured with NADH dehydrogenase subunit 6 by qPCR. Data are expressed as means ± SD ( n = 3). Statistical difference (* P

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Defect of mitochondrial respiratory chain is a mechanism of ROS overproduction in a rat model of alcoholic liver disease: role of zinc deficiency

    doi: 10.1152/ajpgi.00270.2015

    Figure Lengend Snippet: Effect of TPEN on hsp60, SOD2, and OXPHOS proteins, mitochondrial biogenesis regulators, and mtDNA level in human HepG2 cells. Human HepG2 cells were treated with 3 μM TPEN without FBS for 6 h. A : immunoblot bands of hsp60 and SOD2. B : immunoblot bands of OXPHOS proteins, subunit of complex I (CI-NDUFB8), subunit of complex II (CII-SDHB), subunit of complex III (CIII-UQCRC2), subunit of complex IV (CIV-MTCO1), and subunit of complex V (CV-ATP5A). C : immunoblot bands of p-AMPK, AMPK, PGC1α, NRF1, and TFAM. D : mtDNA level was measured with NADH dehydrogenase subunit 6 by qPCR. Data are expressed as means ± SD ( n = 3). Statistical difference (* P

    Article Snippet: Tissue sections were then incubated with a polyclonal rabbit anti-MPO (LSBio, Seattle, WA, no. LS-B6699, 1:100), a monoclonal mouse anti-4HNE antibody (Northwest Life Science Specialties, Vancouver, WA, no. NWA-HNE020, 1:100), a monoclonal mouse anti-OXPHOS (Abcam, Cambridge, MA, no. ab110413, 1:100), a monoclonal mouse anti-MTCO1 (Abcam, no. ab14705, 1:100), a monoclonal rabbit anti-p-AMPK (Cell Signaling Technology, Danvers, MA, no. 2537, 1:100), a monoclonal mouse anti-PGC1α (Calbiochem, no. ST1202, 1:100), a polyclonal rabbit anti-NRF1 (Boster, Pleasanton, CA, no. PA1948, 1:200), or a monoclonal mouse anti-TFAM (Novus Biological, Littleton, CO, no. NBP1-71648, 1:100).

    Techniques: Real-time Polymerase Chain Reaction

    Schematic hypothesis on zinc deprivation-induced accumulation of ROS based on the results of the present study. Alcohol consumption induces a decrease in zinc level in the liver. Zinc deficiency downregulates expression of PGC1α, NRF1, and TFAM, which results in reduced mitochondrial biogenesis and mtDNA replication. Impairment of mtDNA leads to defect of mitochondrial respiratory complexes, namely complexes I, III, and IV. As a result, defective complexes I, III, and IV causes ROS overproduction in alcoholic liver disease.

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Defect of mitochondrial respiratory chain is a mechanism of ROS overproduction in a rat model of alcoholic liver disease: role of zinc deficiency

    doi: 10.1152/ajpgi.00270.2015

    Figure Lengend Snippet: Schematic hypothesis on zinc deprivation-induced accumulation of ROS based on the results of the present study. Alcohol consumption induces a decrease in zinc level in the liver. Zinc deficiency downregulates expression of PGC1α, NRF1, and TFAM, which results in reduced mitochondrial biogenesis and mtDNA replication. Impairment of mtDNA leads to defect of mitochondrial respiratory complexes, namely complexes I, III, and IV. As a result, defective complexes I, III, and IV causes ROS overproduction in alcoholic liver disease.

    Article Snippet: Tissue sections were then incubated with a polyclonal rabbit anti-MPO (LSBio, Seattle, WA, no. LS-B6699, 1:100), a monoclonal mouse anti-4HNE antibody (Northwest Life Science Specialties, Vancouver, WA, no. NWA-HNE020, 1:100), a monoclonal mouse anti-OXPHOS (Abcam, Cambridge, MA, no. ab110413, 1:100), a monoclonal mouse anti-MTCO1 (Abcam, no. ab14705, 1:100), a monoclonal rabbit anti-p-AMPK (Cell Signaling Technology, Danvers, MA, no. 2537, 1:100), a monoclonal mouse anti-PGC1α (Calbiochem, no. ST1202, 1:100), a polyclonal rabbit anti-NRF1 (Boster, Pleasanton, CA, no. PA1948, 1:200), or a monoclonal mouse anti-TFAM (Novus Biological, Littleton, CO, no. NBP1-71648, 1:100).

    Techniques: Expressing

    Protein level of mitochondrial biogenesis regulators and mtDNA level in the liver of rats chronically fed alcohol for 5 mo. A : immunoblot bands of p-AMPK, AMPK, PGC1α, NRF1, and TFAM. B : immunohistochemical staining of p-AMPK, PGC1α, NRF1, and TFAM proteins. Arrows indicate positive staining. C : fold change of immunohistochemical staining intensity. The quantification was conducted by Image J. D : mtDNA level was measured with NADH dehydrogenase subunit 6 by quantitative PCR (qPCR). Data are expressed as means ± SD from 6 rats. Statistical difference (* P

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Defect of mitochondrial respiratory chain is a mechanism of ROS overproduction in a rat model of alcoholic liver disease: role of zinc deficiency

    doi: 10.1152/ajpgi.00270.2015

    Figure Lengend Snippet: Protein level of mitochondrial biogenesis regulators and mtDNA level in the liver of rats chronically fed alcohol for 5 mo. A : immunoblot bands of p-AMPK, AMPK, PGC1α, NRF1, and TFAM. B : immunohistochemical staining of p-AMPK, PGC1α, NRF1, and TFAM proteins. Arrows indicate positive staining. C : fold change of immunohistochemical staining intensity. The quantification was conducted by Image J. D : mtDNA level was measured with NADH dehydrogenase subunit 6 by quantitative PCR (qPCR). Data are expressed as means ± SD from 6 rats. Statistical difference (* P

    Article Snippet: Tissue sections were then incubated with a polyclonal rabbit anti-MPO (LSBio, Seattle, WA, no. LS-B6699, 1:100), a monoclonal mouse anti-4HNE antibody (Northwest Life Science Specialties, Vancouver, WA, no. NWA-HNE020, 1:100), a monoclonal mouse anti-OXPHOS (Abcam, Cambridge, MA, no. ab110413, 1:100), a monoclonal mouse anti-MTCO1 (Abcam, no. ab14705, 1:100), a monoclonal rabbit anti-p-AMPK (Cell Signaling Technology, Danvers, MA, no. 2537, 1:100), a monoclonal mouse anti-PGC1α (Calbiochem, no. ST1202, 1:100), a polyclonal rabbit anti-NRF1 (Boster, Pleasanton, CA, no. PA1948, 1:200), or a monoclonal mouse anti-TFAM (Novus Biological, Littleton, CO, no. NBP1-71648, 1:100).

    Techniques: Immunohistochemistry, Staining, Real-time Polymerase Chain Reaction

    PGC-1α-mediated increase in the muscle oxidative phenotype does not improve survival or motor function in G93A mice G93A mice were mated with MCK-PGC-1α mice to examine the effect of enhanced mitochondrial biogenesis in the muscle on disease progression. (a) Gastrocnemius muscle from G93A/MCK-PGC-1α mouse shows higher SDH staining than S93A mouse demonstrating increased mitochondrial activity in the presence of PGC-1α transgene (scale=500μm). (b) Survival analysis and (c) weekly weight measures (Two-way ANOVA, n=9 G93A; n=7 G93A/MCK-PGC-1α) did not show a genotypic difference between the two groups. (c) Motor function was examined in these mice using the Rotarod apparatus. The difference in the rotarod latency-to-fall values between the two groups were statistically significant (Two-way ANOVA, p

    Journal: Nature communications

    Article Title: Postnatal muscle modification by myogenic factors modulates neuropathology and survival in an ALS mouse model

    doi: 10.1038/ncomms3906

    Figure Lengend Snippet: PGC-1α-mediated increase in the muscle oxidative phenotype does not improve survival or motor function in G93A mice G93A mice were mated with MCK-PGC-1α mice to examine the effect of enhanced mitochondrial biogenesis in the muscle on disease progression. (a) Gastrocnemius muscle from G93A/MCK-PGC-1α mouse shows higher SDH staining than S93A mouse demonstrating increased mitochondrial activity in the presence of PGC-1α transgene (scale=500μm). (b) Survival analysis and (c) weekly weight measures (Two-way ANOVA, n=9 G93A; n=7 G93A/MCK-PGC-1α) did not show a genotypic difference between the two groups. (c) Motor function was examined in these mice using the Rotarod apparatus. The difference in the rotarod latency-to-fall values between the two groups were statistically significant (Two-way ANOVA, p

    Article Snippet: For PGC-1α muscle overexpression study, B6 congenic G93A mice (Jackson Laboratory, Bar Harbor, ME) were crossed to B6 congenic MCK-PGC-1α mice (Jackson Laboratory, Bar Harbor, ME) to generate G93A/MCK-PGC-1α mice.

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

    PGC-1α isoforms. A , The illustration of PGC-1α new alternative exons and known exons in RefSeq/Ensembl/UCSC genome references. Human ESTs and mouse TSS with enhancer signals derived from > 1000 human and mouse primary cells, cell lines, and tissues were mapped using CAGE. B , Diagram and PCR products show four different PGC-1α isoforms from SH-SY5Y and mouse brain and heart. C , RT-PCR for four PGC-1α isoforms, SDHA, Tomm20, and GAPDH RNA 4 weeks after stereotactic delivery of AAV-GFP or AAV-Cre-GFP into PGC-1α flox/flox mice; n = 3/group. D , Quantification of C normalized to GAPDH; n = 3/group. * p

    Journal: eNeuro

    Article Title: Adult Conditional Knockout of PGC-1α Leads to Loss of Dopamine Neurons

    doi: 10.1523/ENEURO.0183-16.2016

    Figure Lengend Snippet: PGC-1α isoforms. A , The illustration of PGC-1α new alternative exons and known exons in RefSeq/Ensembl/UCSC genome references. Human ESTs and mouse TSS with enhancer signals derived from > 1000 human and mouse primary cells, cell lines, and tissues were mapped using CAGE. B , Diagram and PCR products show four different PGC-1α isoforms from SH-SY5Y and mouse brain and heart. C , RT-PCR for four PGC-1α isoforms, SDHA, Tomm20, and GAPDH RNA 4 weeks after stereotactic delivery of AAV-GFP or AAV-Cre-GFP into PGC-1α flox/flox mice; n = 3/group. D , Quantification of C normalized to GAPDH; n = 3/group. * p

    Article Snippet: Conditional PGC-1α knock-out mice were purchased from The Jackson Laboratory ( https://www.jax.org/strain/009666 ).

    Techniques: Pyrolysis Gas Chromatography, Derivative Assay, Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction, Mouse Assay

    Adult conditional gene deletion of PGC-1α. A , Experimental schematic of stereotaxic intranigral virus injection and experimental time line. B , Representative GFP and TH-positive immunostaining of midbrain section from SNpc of PGC-1α flox/flox mice injected with AAV-GFP or AAV-Cre-GFP 6 months after the injection of virus. Scale Bar, 100 µm. C , Immunoblots of PGC-1α, SDHA, Tomm20, and β-actin 4 weeks after stereotactic delivery of AAV-GFP and AAV-Cre-GFP into PGC-1α flox/flox mice; n = 3/group. D , Quantification of C normalized to β-actin; n = 3/group. * p

    Journal: eNeuro

    Article Title: Adult Conditional Knockout of PGC-1α Leads to Loss of Dopamine Neurons

    doi: 10.1523/ENEURO.0183-16.2016

    Figure Lengend Snippet: Adult conditional gene deletion of PGC-1α. A , Experimental schematic of stereotaxic intranigral virus injection and experimental time line. B , Representative GFP and TH-positive immunostaining of midbrain section from SNpc of PGC-1α flox/flox mice injected with AAV-GFP or AAV-Cre-GFP 6 months after the injection of virus. Scale Bar, 100 µm. C , Immunoblots of PGC-1α, SDHA, Tomm20, and β-actin 4 weeks after stereotactic delivery of AAV-GFP and AAV-Cre-GFP into PGC-1α flox/flox mice; n = 3/group. D , Quantification of C normalized to β-actin; n = 3/group. * p

    Article Snippet: Conditional PGC-1α knock-out mice were purchased from The Jackson Laboratory ( https://www.jax.org/strain/009666 ).

    Techniques: Pyrolysis Gas Chromatography, Injection, Immunostaining, Mouse Assay, Western Blot

    Gene deletion of PGC-1α leads to the loss of dopamine neurons in the SNpc. A , Representative TH immunohistochemistry and Nissl staining of midbrain sections from SNpc of PGC-1α flox/flox mice injected with AAV-GFP or AAV-Cre-GFP 6 months after the injection of virus. Scale bar, 100 µm. B , Stereological assessment of TH- and Nissl-positive neurons in the SNpc of PGC-1α flox/flox mice injected with AAV-GFP or AAV-Cre-GFP ( n = 3/group). C , HPLC assessment of the striatal content of dopamine. D , HPLC assessment of the striatal content of dopamine metabolites DOPAC and HVA. E , Amphetamine-induced ipsilateral rotations ( n = 3/group). Data are expressed as the mean ± SEM. * p

    Journal: eNeuro

    Article Title: Adult Conditional Knockout of PGC-1α Leads to Loss of Dopamine Neurons

    doi: 10.1523/ENEURO.0183-16.2016

    Figure Lengend Snippet: Gene deletion of PGC-1α leads to the loss of dopamine neurons in the SNpc. A , Representative TH immunohistochemistry and Nissl staining of midbrain sections from SNpc of PGC-1α flox/flox mice injected with AAV-GFP or AAV-Cre-GFP 6 months after the injection of virus. Scale bar, 100 µm. B , Stereological assessment of TH- and Nissl-positive neurons in the SNpc of PGC-1α flox/flox mice injected with AAV-GFP or AAV-Cre-GFP ( n = 3/group). C , HPLC assessment of the striatal content of dopamine. D , HPLC assessment of the striatal content of dopamine metabolites DOPAC and HVA. E , Amphetamine-induced ipsilateral rotations ( n = 3/group). Data are expressed as the mean ± SEM. * p

    Article Snippet: Conditional PGC-1α knock-out mice were purchased from The Jackson Laboratory ( https://www.jax.org/strain/009666 ).

    Techniques: Pyrolysis Gas Chromatography, Immunohistochemistry, Staining, Mouse Assay, Injection, High Performance Liquid Chromatography

    Reduction of PGC-1α isoforms, SDHA, and Tomm20 in PD. A , Immunoblots of PGC-1α, SDHA, Tomm20, and β-actin in SN of PD mouse compared with an age-matched control. B , Quantitation of the immunoblots in A normalized to β-actin: Control, n = 4; PD mouse, n = 3. * p

    Journal: eNeuro

    Article Title: Adult Conditional Knockout of PGC-1α Leads to Loss of Dopamine Neurons

    doi: 10.1523/ENEURO.0183-16.2016

    Figure Lengend Snippet: Reduction of PGC-1α isoforms, SDHA, and Tomm20 in PD. A , Immunoblots of PGC-1α, SDHA, Tomm20, and β-actin in SN of PD mouse compared with an age-matched control. B , Quantitation of the immunoblots in A normalized to β-actin: Control, n = 4; PD mouse, n = 3. * p

    Article Snippet: Conditional PGC-1α knock-out mice were purchased from The Jackson Laboratory ( https://www.jax.org/strain/009666 ).

    Techniques: Pyrolysis Gas Chromatography, Western Blot, Quantitation Assay

    TWEAK inhibits the expression of PGC-1α in cultured myotubes. A ) C2C12 myotubes were treated with indicated amounts of soluble TWEAK protein for 24 h, and mRNA levels of PGC-1α, PGC-1β, Cox I, Cox IV, Cyt c, Tfb2m, Tfam, ATP5b,

    Journal: The FASEB Journal

    Article Title: Regulatory circuitry of TWEAK-Fn14 system and PGC-1α in skeletal muscle atrophy program

    doi: 10.1096/fj.13-242123

    Figure Lengend Snippet: TWEAK inhibits the expression of PGC-1α in cultured myotubes. A ) C2C12 myotubes were treated with indicated amounts of soluble TWEAK protein for 24 h, and mRNA levels of PGC-1α, PGC-1β, Cox I, Cox IV, Cyt c, Tfb2m, Tfam, ATP5b,

    Article Snippet: Muscle-specific PGC-1α-Tg mice as described previously ( ) were purchased from Jackson Laboratory (Bar Harbor, ME, USA).

    Techniques: Expressing, Pyrolysis Gas Chromatography, Cell Culture

    Tg overexpression of PGC-1α inhibits the progressive muscle atrophy in TWEAK-Tg mice. A ) TA muscle isolated from 15-mo-old littermate WT, TWEAK-Tg, PGC-1α-Tg, and TWEAK-PGC-1α double-Tg mice were processed for H E staining.

    Journal: The FASEB Journal

    Article Title: Regulatory circuitry of TWEAK-Fn14 system and PGC-1α in skeletal muscle atrophy program

    doi: 10.1096/fj.13-242123

    Figure Lengend Snippet: Tg overexpression of PGC-1α inhibits the progressive muscle atrophy in TWEAK-Tg mice. A ) TA muscle isolated from 15-mo-old littermate WT, TWEAK-Tg, PGC-1α-Tg, and TWEAK-PGC-1α double-Tg mice were processed for H E staining.

    Article Snippet: Muscle-specific PGC-1α-Tg mice as described previously ( ) were purchased from Jackson Laboratory (Bar Harbor, ME, USA).

    Techniques: Over Expression, Pyrolysis Gas Chromatography, Mouse Assay, Isolation, Staining

    Overexpression of PGC-1α inhibits TWEAK-induced atrophy in cultured muscle cells. Myofiber cultures established from EDL muscle of WT and PGC-1α Tg mice were treated with indicated concentration of soluble TWEAK protein for 72 h. A ) Representative

    Journal: The FASEB Journal

    Article Title: Regulatory circuitry of TWEAK-Fn14 system and PGC-1α in skeletal muscle atrophy program

    doi: 10.1096/fj.13-242123

    Figure Lengend Snippet: Overexpression of PGC-1α inhibits TWEAK-induced atrophy in cultured muscle cells. Myofiber cultures established from EDL muscle of WT and PGC-1α Tg mice were treated with indicated concentration of soluble TWEAK protein for 72 h. A ) Representative

    Article Snippet: Muscle-specific PGC-1α-Tg mice as described previously ( ) were purchased from Jackson Laboratory (Bar Harbor, ME, USA).

    Techniques: Over Expression, Pyrolysis Gas Chromatography, Cell Culture, Mouse Assay, Concentration Assay

    TWEAK represses PGC-1α levels in denervated skeletal muscle of mice. Quantitative estimation of mRNA levels of different genes in TA muscle by QRT-PCR assay. A ) Relative mRNA levels of TWEAK receptor Fn14 and PGC-1α in undenervated and

    Journal: The FASEB Journal

    Article Title: Regulatory circuitry of TWEAK-Fn14 system and PGC-1α in skeletal muscle atrophy program

    doi: 10.1096/fj.13-242123

    Figure Lengend Snippet: TWEAK represses PGC-1α levels in denervated skeletal muscle of mice. Quantitative estimation of mRNA levels of different genes in TA muscle by QRT-PCR assay. A ) Relative mRNA levels of TWEAK receptor Fn14 and PGC-1α in undenervated and

    Article Snippet: Muscle-specific PGC-1α-Tg mice as described previously ( ) were purchased from Jackson Laboratory (Bar Harbor, ME, USA).

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

    Overexpression of PGC-1α blunts the expression of atrogenes and augments the levels of mitochondria-related genes in TWEAK-treated myotubes. Primary myoblasts prepared from littermate WT and PGC-1α Tg mice were differentiated into myotubes,

    Journal: The FASEB Journal

    Article Title: Regulatory circuitry of TWEAK-Fn14 system and PGC-1α in skeletal muscle atrophy program

    doi: 10.1096/fj.13-242123

    Figure Lengend Snippet: Overexpression of PGC-1α blunts the expression of atrogenes and augments the levels of mitochondria-related genes in TWEAK-treated myotubes. Primary myoblasts prepared from littermate WT and PGC-1α Tg mice were differentiated into myotubes,

    Article Snippet: Muscle-specific PGC-1α-Tg mice as described previously ( ) were purchased from Jackson Laboratory (Bar Harbor, ME, USA).

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

    Overexpression of PGC-1α inhibits the expression of Fn14 in denervated muscle of mice. A ) Relative mRNA levels of Fn14, TWEAK, and MuRF1 in undenervated and denervated TA muscle of WT and PGC-1α-Tg mice, measured by performing QRT-PCR

    Journal: The FASEB Journal

    Article Title: Regulatory circuitry of TWEAK-Fn14 system and PGC-1α in skeletal muscle atrophy program

    doi: 10.1096/fj.13-242123

    Figure Lengend Snippet: Overexpression of PGC-1α inhibits the expression of Fn14 in denervated muscle of mice. A ) Relative mRNA levels of Fn14, TWEAK, and MuRF1 in undenervated and denervated TA muscle of WT and PGC-1α-Tg mice, measured by performing QRT-PCR

    Article Snippet: Muscle-specific PGC-1α-Tg mice as described previously ( ) were purchased from Jackson Laboratory (Bar Harbor, ME, USA).

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

    PGC-1α inhibits the TWEAK-induced activation of NF-κB in myotubes. Primary myotubes prepared from WT and PGC-1α Tg mice were treated with 100 ng/ml TWEAK protein for indicated time period and analyzed for the activation of NF-κB.

    Journal: The FASEB Journal

    Article Title: Regulatory circuitry of TWEAK-Fn14 system and PGC-1α in skeletal muscle atrophy program

    doi: 10.1096/fj.13-242123

    Figure Lengend Snippet: PGC-1α inhibits the TWEAK-induced activation of NF-κB in myotubes. Primary myotubes prepared from WT and PGC-1α Tg mice were treated with 100 ng/ml TWEAK protein for indicated time period and analyzed for the activation of NF-κB.

    Article Snippet: Muscle-specific PGC-1α-Tg mice as described previously ( ) were purchased from Jackson Laboratory (Bar Harbor, ME, USA).

    Techniques: Pyrolysis Gas Chromatography, Activation Assay, Mouse Assay

    PGC1α mRNA (A) and protein (B) expressions in differentiated 3T3L1 cells. (A) Sirt1 mRNA expression was measured by real-time PCR. The data are expressed as mean ± SD of three experiments. * P

    Journal: Molecular Genetics and Metabolism Reports

    Article Title: Resveratrol attenuates triglyceride accumulation associated with upregulation of Sirt1 and lipoprotein lipase in 3T3-L1 adipocytes

    doi: 10.1016/j.ymgmr.2017.05.003

    Figure Lengend Snippet: PGC1α mRNA (A) and protein (B) expressions in differentiated 3T3L1 cells. (A) Sirt1 mRNA expression was measured by real-time PCR. The data are expressed as mean ± SD of three experiments. * P

    Article Snippet: The membranes were incubated with the following primary antibodies: goat antiserum against mouse Sirt1 (1:1000; Santa Cruz Biotechnology), rabbit antiserum against mouse LPL (1:1000; Santa Cruz Biotechnology), rabbit antiserum against mouse PGC1α (1:1000; Santa Cruz Biotechnology), and mouse antiserum against β-actin (1:2000; Santa Cruz Biotechnology) as negative control; and the following secondary antibodies: donkey antiserum against goat IgG (1:2000; R & D system), donkey antiserum against rabbit IgG (1:2000; GE Healthcare), and sheep antiserum against mouse IgG (1:2000; GE Healthcare).

    Techniques: Expressing, Real-time Polymerase Chain Reaction

    Changes in VEGF protein levels Effect of PGC-1α siRNA on VEGF protein production in hRVECs at 16h of normoxia and hypoxia after transfection were detected by ELISA. The VEGF protein production in siPGC-1α groups were significantly downregulated when compared with control siRNA groups under normoxia and hypoxia. b P

    Journal: International Journal of Ophthalmology

    Article Title: Small interfering RNA targeting PGC-1α inhibits VEGF expression and tube formation in human retinal vascular endothelial cells

    doi: 10.3980/j.issn.2222-3959.2015.05.05

    Figure Lengend Snippet: Changes in VEGF protein levels Effect of PGC-1α siRNA on VEGF protein production in hRVECs at 16h of normoxia and hypoxia after transfection were detected by ELISA. The VEGF protein production in siPGC-1α groups were significantly downregulated when compared with control siRNA groups under normoxia and hypoxia. b P

    Article Snippet: The primary antibodies used were as follows: mouse anti-human PGC-1α (Abcam, Cambridge, MA, USA) 1:1000, mouse anti-human β-actin (Santa Cruz Biotechnology, Dallas, TX, USA) 1:800.

    Techniques: Pyrolysis Gas Chromatography, Transfection, Enzyme-linked Immunosorbent Assay

    Changes in PGC-1α mRNA expression PGC-1α siRNA-mediated downregulation of PGC-1α mRNA expression in hRVECs at 16h of normoxia and hypoxia after transfection were examined by real-time PCR. The expression of PGC-1α mRNA were significantly downregulated in cells in the siPGC-1α groups relative to cells in the control siRNA groups under normoxia and hypoxia. b P

    Journal: International Journal of Ophthalmology

    Article Title: Small interfering RNA targeting PGC-1α inhibits VEGF expression and tube formation in human retinal vascular endothelial cells

    doi: 10.3980/j.issn.2222-3959.2015.05.05

    Figure Lengend Snippet: Changes in PGC-1α mRNA expression PGC-1α siRNA-mediated downregulation of PGC-1α mRNA expression in hRVECs at 16h of normoxia and hypoxia after transfection were examined by real-time PCR. The expression of PGC-1α mRNA were significantly downregulated in cells in the siPGC-1α groups relative to cells in the control siRNA groups under normoxia and hypoxia. b P

    Article Snippet: The primary antibodies used were as follows: mouse anti-human PGC-1α (Abcam, Cambridge, MA, USA) 1:1000, mouse anti-human β-actin (Santa Cruz Biotechnology, Dallas, TX, USA) 1:800.

    Techniques: Pyrolysis Gas Chromatography, Expressing, Transfection, Real-time Polymerase Chain Reaction

    PGC-1α siRNA inhibits cell tube formation in hRVECs Tubular structures were photographed (A-F) and then quantified by counting the number of branch points (G) and calculating total tube length (H) in cultured hRVECs. A: Normoxia siPGC-1α group; B: Normoxia control siRNA group; C: Normoxia without siRNA group; D: Hypoxia siPGC-1α group; E: Hypoxia control siRNA group; F: Hypoxia without siRNA group. PGC-1α siRNA significantly reduced tubular-like formation (A and D), branch points (G), and total tube length (H) in cells compared with control siRNA group under normoxia (B) and hypoxia (E). Cells in the hypoxia without siRNA group and the hypoxia control siRNA group formed significantly more tubes than cells in their corresponding normoxia groups. b P

    Journal: International Journal of Ophthalmology

    Article Title: Small interfering RNA targeting PGC-1α inhibits VEGF expression and tube formation in human retinal vascular endothelial cells

    doi: 10.3980/j.issn.2222-3959.2015.05.05

    Figure Lengend Snippet: PGC-1α siRNA inhibits cell tube formation in hRVECs Tubular structures were photographed (A-F) and then quantified by counting the number of branch points (G) and calculating total tube length (H) in cultured hRVECs. A: Normoxia siPGC-1α group; B: Normoxia control siRNA group; C: Normoxia without siRNA group; D: Hypoxia siPGC-1α group; E: Hypoxia control siRNA group; F: Hypoxia without siRNA group. PGC-1α siRNA significantly reduced tubular-like formation (A and D), branch points (G), and total tube length (H) in cells compared with control siRNA group under normoxia (B) and hypoxia (E). Cells in the hypoxia without siRNA group and the hypoxia control siRNA group formed significantly more tubes than cells in their corresponding normoxia groups. b P

    Article Snippet: The primary antibodies used were as follows: mouse anti-human PGC-1α (Abcam, Cambridge, MA, USA) 1:1000, mouse anti-human β-actin (Santa Cruz Biotechnology, Dallas, TX, USA) 1:800.

    Techniques: Pyrolysis Gas Chromatography, Cell Culture

    Changes in PGC-1α protein levels A: PGC-1α siRNA-mediated downregulation of PGC-1α protein production in hRVECs at 16h of normoxia and hypoxia after transfection were detected by Western blot; B: Quantitative results of the Western blot analysis in A.The levels of PGC-1α protein were significantly lower in cells in the siPGC-1α groups compared with cells in the control siRNA groups under normoxia and hypoxia. b P

    Journal: International Journal of Ophthalmology

    Article Title: Small interfering RNA targeting PGC-1α inhibits VEGF expression and tube formation in human retinal vascular endothelial cells

    doi: 10.3980/j.issn.2222-3959.2015.05.05

    Figure Lengend Snippet: Changes in PGC-1α protein levels A: PGC-1α siRNA-mediated downregulation of PGC-1α protein production in hRVECs at 16h of normoxia and hypoxia after transfection were detected by Western blot; B: Quantitative results of the Western blot analysis in A.The levels of PGC-1α protein were significantly lower in cells in the siPGC-1α groups compared with cells in the control siRNA groups under normoxia and hypoxia. b P

    Article Snippet: The primary antibodies used were as follows: mouse anti-human PGC-1α (Abcam, Cambridge, MA, USA) 1:1000, mouse anti-human β-actin (Santa Cruz Biotechnology, Dallas, TX, USA) 1:800.

    Techniques: Pyrolysis Gas Chromatography, Transfection, Western Blot

    Changes in VEGF mRNA expression Effect of PGC-1α siRNA on VEGF mRNA expression in hRVECs at 16h of normoxia and hypoxia after transfection were examined by real-time PCR. The VEGF mRNA levels of siPGC-1α groups were significantly downregulated when compared with control siRNA groups during normoxia and hypoxia. b P

    Journal: International Journal of Ophthalmology

    Article Title: Small interfering RNA targeting PGC-1α inhibits VEGF expression and tube formation in human retinal vascular endothelial cells

    doi: 10.3980/j.issn.2222-3959.2015.05.05

    Figure Lengend Snippet: Changes in VEGF mRNA expression Effect of PGC-1α siRNA on VEGF mRNA expression in hRVECs at 16h of normoxia and hypoxia after transfection were examined by real-time PCR. The VEGF mRNA levels of siPGC-1α groups were significantly downregulated when compared with control siRNA groups during normoxia and hypoxia. b P

    Article Snippet: The primary antibodies used were as follows: mouse anti-human PGC-1α (Abcam, Cambridge, MA, USA) 1:1000, mouse anti-human β-actin (Santa Cruz Biotechnology, Dallas, TX, USA) 1:800.

    Techniques: Expressing, Pyrolysis Gas Chromatography, Transfection, Real-time Polymerase Chain Reaction

    PGC-1α siRNA inhibits cell proliferation in hRVECs Effect of PGC-1α siRNA on cell proliferation in hRVECs at 16h of normoxia and hypoxia after transfection. The percentage of BrdU-labeled cells in siPGC-1α groups significantly decreased compared with control siRNA groups under normoxia and hypoxia. b P

    Journal: International Journal of Ophthalmology

    Article Title: Small interfering RNA targeting PGC-1α inhibits VEGF expression and tube formation in human retinal vascular endothelial cells

    doi: 10.3980/j.issn.2222-3959.2015.05.05

    Figure Lengend Snippet: PGC-1α siRNA inhibits cell proliferation in hRVECs Effect of PGC-1α siRNA on cell proliferation in hRVECs at 16h of normoxia and hypoxia after transfection. The percentage of BrdU-labeled cells in siPGC-1α groups significantly decreased compared with control siRNA groups under normoxia and hypoxia. b P

    Article Snippet: The primary antibodies used were as follows: mouse anti-human PGC-1α (Abcam, Cambridge, MA, USA) 1:1000, mouse anti-human β-actin (Santa Cruz Biotechnology, Dallas, TX, USA) 1:800.

    Techniques: Pyrolysis Gas Chromatography, Transfection, Labeling