rabbit anti phospho akt  (Cell Signaling Technology Inc)

 
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  • 97
    Name:
    Phospho Akt Thr308 244F9H2 Rabbit mAb IHC Specific
    Description:
    Akt also referred to as PKB or Rac plays a critical role in controlling survival and apoptosis 1 3 This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin sensitive pathway involving PI3 kinase 2 3 Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 4 and by phosphorylation within the carboxy terminus at Ser473 The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin mTOR in a rapamycin insensitive complex with rictor and Sin1 5 6 Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets including Bad 7 forkhead transcription factors 8 c Raf 9 and caspase 9 PTEN phosphatase is a major negative regulator of the PI3 kinase Akt signaling pathway 10 LY294002 is a specific PI3 kinase inhibitor 11 Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK 3α and β 12 13 Akt may also play a role in insulin stimulation of glucose transport 12 In addition to its role in survival and glycogen synthesis Akt is involved in cell cycle regulation by preventing GSK 3β mediated phosphorylation and degradation of cyclin D1 14 and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 15 and p21 Waf1 Cip1 16 Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin sensitive complex containing raptor 17 More importantly Akt phosphorylates and inactivates tuberin TSC2 an inhibitor of mTOR within the mTOR raptor complex 18 19
    Catalog Number:
    9266
    Price:
    None
    Applications:
    Immunohistochemistry
    Category:
    Primary Antibodies
    Source:
    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues around Thr308 of mouse Akt.
    Reactivity:
    Human Mouse
    Buy from Supplier


    Structured Review

    Cell Signaling Technology Inc rabbit anti phospho akt
    Changes in <t>Tie-2/Akt/eNOS</t> signaling pathways under HG conditions. (A) Tie-2 phosphorylation was decreased under HG conditions in MHMECs ( n =3). (B) HG inhibited phosphorylation of Akt and eNOS in MHMECs compared with NG groups ( n =5). (C) Ang-1 increased Tie-2 phosphorylation in MHMECs, which was dampened under HG conditions ( n =3). b P
    Akt also referred to as PKB or Rac plays a critical role in controlling survival and apoptosis 1 3 This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin sensitive pathway involving PI3 kinase 2 3 Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 4 and by phosphorylation within the carboxy terminus at Ser473 The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin mTOR in a rapamycin insensitive complex with rictor and Sin1 5 6 Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets including Bad 7 forkhead transcription factors 8 c Raf 9 and caspase 9 PTEN phosphatase is a major negative regulator of the PI3 kinase Akt signaling pathway 10 LY294002 is a specific PI3 kinase inhibitor 11 Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK 3α and β 12 13 Akt may also play a role in insulin stimulation of glucose transport 12 In addition to its role in survival and glycogen synthesis Akt is involved in cell cycle regulation by preventing GSK 3β mediated phosphorylation and degradation of cyclin D1 14 and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 15 and p21 Waf1 Cip1 16 Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin sensitive complex containing raptor 17 More importantly Akt phosphorylates and inactivates tuberin TSC2 an inhibitor of mTOR within the mTOR raptor complex 18 19
    https://www.bioz.com/result/rabbit anti phospho akt/product/Cell Signaling Technology Inc
    Average 97 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    rabbit anti phospho akt - by Bioz Stars, 2020-11
    97/100 stars

    Images

    1) Product Images from "Angiopoietin-1 protects myocardial endothelial cell function blunted by angiopoietin-2 and high glucose condition"

    Article Title: Angiopoietin-1 protects myocardial endothelial cell function blunted by angiopoietin-2 and high glucose condition

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/aps.2010.183

    Changes in Tie-2/Akt/eNOS signaling pathways under HG conditions. (A) Tie-2 phosphorylation was decreased under HG conditions in MHMECs ( n =3). (B) HG inhibited phosphorylation of Akt and eNOS in MHMECs compared with NG groups ( n =5). (C) Ang-1 increased Tie-2 phosphorylation in MHMECs, which was dampened under HG conditions ( n =3). b P
    Figure Legend Snippet: Changes in Tie-2/Akt/eNOS signaling pathways under HG conditions. (A) Tie-2 phosphorylation was decreased under HG conditions in MHMECs ( n =3). (B) HG inhibited phosphorylation of Akt and eNOS in MHMECs compared with NG groups ( n =5). (C) Ang-1 increased Tie-2 phosphorylation in MHMECs, which was dampened under HG conditions ( n =3). b P

    Techniques Used:

    2) Product Images from "D-Pinitol from Ceratonia siliqua Is an Orally Active Natural Inositol That Reduces Pancreas Insulin Secretion and Increases Circulating Ghrelin Levels in Wistar Rats"

    Article Title: D-Pinitol from Ceratonia siliqua Is an Orally Active Natural Inositol That Reduces Pancreas Insulin Secretion and Increases Circulating Ghrelin Levels in Wistar Rats

    Journal: Nutrients

    doi: 10.3390/nu12072030

    Western blot analysis of the phosphorylation status of the enzymes AKT and GSK3β from liver lysates of Wistar rats treated with 500 mg/Kg of D-Pinitol (p.o.), for 60, 120 and 240 min. ( A ) Representative western blot analysis for AKT (upper panels) and p-AKT/AKT ratio and AKT/adaptin ratio (bottom panels), from liver samples of Wistar rats treated with D-Pinitol for times indicated in figure. The blot shows analysis from three independent samples from each treatment group. The corresponding expression of adaptin is shown as a loading control per lane. ( B ) Representative western blot analysis for GSK3β (upper panels) and p-GSK3β/GSK3β ratio and GSK3β/adaptin ratio (bottom panels) of liver samples from Wistar rats treated with D-Pinitol, at times indicated in figure. The blot shows analysis from three independent samples from each treatment group. The corresponding expression of adaptin is shown as a loading control per lane. All samples shown in the figure were derived at the same time and processed in parallel in the corresponding blot. The adjustment to digital images did not alter the information contained therein. Differences between groups were evaluated using one-way Anova + Fisher’s LSD test: † p
    Figure Legend Snippet: Western blot analysis of the phosphorylation status of the enzymes AKT and GSK3β from liver lysates of Wistar rats treated with 500 mg/Kg of D-Pinitol (p.o.), for 60, 120 and 240 min. ( A ) Representative western blot analysis for AKT (upper panels) and p-AKT/AKT ratio and AKT/adaptin ratio (bottom panels), from liver samples of Wistar rats treated with D-Pinitol for times indicated in figure. The blot shows analysis from three independent samples from each treatment group. The corresponding expression of adaptin is shown as a loading control per lane. ( B ) Representative western blot analysis for GSK3β (upper panels) and p-GSK3β/GSK3β ratio and GSK3β/adaptin ratio (bottom panels) of liver samples from Wistar rats treated with D-Pinitol, at times indicated in figure. The blot shows analysis from three independent samples from each treatment group. The corresponding expression of adaptin is shown as a loading control per lane. All samples shown in the figure were derived at the same time and processed in parallel in the corresponding blot. The adjustment to digital images did not alter the information contained therein. Differences between groups were evaluated using one-way Anova + Fisher’s LSD test: † p

    Techniques Used: Western Blot, Expressing, Derivative Assay

    3) Product Images from "The innate immune response in fetal lung mesenchymal cells targets VEGFR2 expression and activity"

    Article Title: The innate immune response in fetal lung mesenchymal cells targets VEGFR2 expression and activity

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    doi: 10.1152/ajplung.00554.2016

    LPS inhibited VEGFR2-mediated signaling in fetal mouse lung mesenchymal cells. E15 primary fetal lung mesenchymal cells were pretreated with LPS for 24 h before stimulation with insulin or VEGF-A (10 ng/ml) for 5 min. A : lysates were analyzed by immunoblotting to detect phosphorylation of VEGFR2, ERK1/2, and AKT. B : densitometry analysis measuring phosphorylated/total AKT ratios demonstrated that AKT phosphorylation following VEGF-A treatment was lower in cells pretreated with LPS (* P
    Figure Legend Snippet: LPS inhibited VEGFR2-mediated signaling in fetal mouse lung mesenchymal cells. E15 primary fetal lung mesenchymal cells were pretreated with LPS for 24 h before stimulation with insulin or VEGF-A (10 ng/ml) for 5 min. A : lysates were analyzed by immunoblotting to detect phosphorylation of VEGFR2, ERK1/2, and AKT. B : densitometry analysis measuring phosphorylated/total AKT ratios demonstrated that AKT phosphorylation following VEGF-A treatment was lower in cells pretreated with LPS (* P

    Techniques Used:

    4) Product Images from "A disease-associated Aifm1 variant induces severe myopathy in knockin mice"

    Article Title: A disease-associated Aifm1 variant induces severe myopathy in knockin mice

    Journal: Molecular Metabolism

    doi: 10.1016/j.molmet.2018.05.002

    AIF deficiency stimulates Akt and mTOR activity. (A–B) Immunoblot analyses were performed on (A) muscle and (B) cerebellar tissues from 3 to 6 month-old animals. Densitometry is relative to wt littermates and reported as mean ± SEM. Antibodies against total and phosphorylated forms of Akt, 40-kDa proline-rich Akt substrate (PRAS40), p70 S6 kinase (P70-S6K), ribosomal Protein S6 (RPS6) were used (n = 4–9 per genotype). GAPDH and actin were used as loading control (*** p
    Figure Legend Snippet: AIF deficiency stimulates Akt and mTOR activity. (A–B) Immunoblot analyses were performed on (A) muscle and (B) cerebellar tissues from 3 to 6 month-old animals. Densitometry is relative to wt littermates and reported as mean ± SEM. Antibodies against total and phosphorylated forms of Akt, 40-kDa proline-rich Akt substrate (PRAS40), p70 S6 kinase (P70-S6K), ribosomal Protein S6 (RPS6) were used (n = 4–9 per genotype). GAPDH and actin were used as loading control (*** p

    Techniques Used: Activity Assay

    5) Product Images from "Targeting the NLRP3 Inflammasome to Reduce Diet-Induced Metabolic Abnormalities in Mice"

    Article Title: Targeting the NLRP3 Inflammasome to Reduce Diet-Induced Metabolic Abnormalities in Mice

    Journal: Molecular Medicine

    doi: 10.2119/molmed.2015.00104

    Effects of diet manipulation and NLRP3 inflammasome inhibition or silencing on insulin signal transduction in liver and skeletal muscle. Western blot analysis of total IRS-1 and phosphorylation (A), total Akt and phosphorylation (B) and total GSK-3β
    Figure Legend Snippet: Effects of diet manipulation and NLRP3 inflammasome inhibition or silencing on insulin signal transduction in liver and skeletal muscle. Western blot analysis of total IRS-1 and phosphorylation (A), total Akt and phosphorylation (B) and total GSK-3β

    Techniques Used: Inhibition, Transduction, Western Blot

    6) Product Images from "Smooth Muscle LDL Receptor-related Protein-1 Inactivation Reduces Vascular Reactivity and Promotes Injury-induced Neointima Formation"

    Article Title: Smooth Muscle LDL Receptor-related Protein-1 Inactivation Reduces Vascular Reactivity and Promotes Injury-induced Neointima Formation

    Journal:

    doi: 10.1161/ATVBAHA.109.194357

    Immunofluorescent detection of Ki-67 ( panels a, b ), phospho-PDGFR-β ( panels c, d ), and phospho-Akt ( e,f ) in control ( a,c,e ) and injured carotid arteries ( b,d,f ) of smLrp1 −/− mice 14 days after endothelial denudation. The elastic
    Figure Legend Snippet: Immunofluorescent detection of Ki-67 ( panels a, b ), phospho-PDGFR-β ( panels c, d ), and phospho-Akt ( e,f ) in control ( a,c,e ) and injured carotid arteries ( b,d,f ) of smLrp1 −/− mice 14 days after endothelial denudation. The elastic

    Techniques Used: Mouse Assay

    7) Product Images from "In Vivo Regulation of Brain-Derived Neurotrophic Factor in Dorsal Root Ganglia Is Mediated by Nerve Growth Factor-Triggered Akt Activation during Cystitis"

    Article Title: In Vivo Regulation of Brain-Derived Neurotrophic Factor in Dorsal Root Ganglia Is Mediated by Nerve Growth Factor-Triggered Akt Activation during Cystitis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0081547

    Co-localization of BDNF with p-Akt in L6 DRG during cystitis. Double immunostaining showed that a subpopulation of BDNF immunoreactive cells in L6 DRG during cystitis (A, green staining, white arrows) was co-localized with p-Akt (B: red staining). A number of BDNF positive cells (C, green arrows) did not express p-Akt. Bar = 60 µm. Five L6 DRGs from animals with cystitis were analyzed and consistent results were achieved.
    Figure Legend Snippet: Co-localization of BDNF with p-Akt in L6 DRG during cystitis. Double immunostaining showed that a subpopulation of BDNF immunoreactive cells in L6 DRG during cystitis (A, green staining, white arrows) was co-localized with p-Akt (B: red staining). A number of BDNF positive cells (C, green arrows) did not express p-Akt. Bar = 60 µm. Five L6 DRGs from animals with cystitis were analyzed and consistent results were achieved.

    Techniques Used: Double Immunostaining, Staining

    Retrograde NGF increased BDNF expression in sensory neurons, which was mediated by the PI3K/Akt pathway. In two-compartmented DRG-nerve culture, NGF (50 ng/mL) was added to the chamber containing the sensory axonal terminals. The ganglia were pre-treated with specific PI3K inhibitors LY294002 and Wortmannin, or vehicle. At 12 h after treatment, NGF increased the number of DRG neurons expressing BDNF (compare B to A) which was reversed by LY294002 treatment (compare C to B), and also by Wortmannin treatment (compare D to B). Histogram (E) showed summary results from 4 independent experiments. Bar= 40 µm. *, p
    Figure Legend Snippet: Retrograde NGF increased BDNF expression in sensory neurons, which was mediated by the PI3K/Akt pathway. In two-compartmented DRG-nerve culture, NGF (50 ng/mL) was added to the chamber containing the sensory axonal terminals. The ganglia were pre-treated with specific PI3K inhibitors LY294002 and Wortmannin, or vehicle. At 12 h after treatment, NGF increased the number of DRG neurons expressing BDNF (compare B to A) which was reversed by LY294002 treatment (compare C to B), and also by Wortmannin treatment (compare D to B). Histogram (E) showed summary results from 4 independent experiments. Bar= 40 µm. *, p

    Techniques Used: Expressing

    8) Product Images from "Differential regulation of proliferation and neuronal differentiation in adult rat spinal cord neural stem/progenitors by ERK1/2, Akt, and PLC?"

    Article Title: Differential regulation of proliferation and neuronal differentiation in adult rat spinal cord neural stem/progenitors by ERK1/2, Akt, and PLC?

    Journal: Frontiers in Molecular Neuroscience

    doi: 10.3389/fnmol.2013.00023

    Cell proliferation in adult spinal cord NSPC cultures requires activation of ERK1/2 and Akt. (A) Quantification of the normalized number of EdU+ cells showed that inhibition of ERK1/2 (with MEK inhibitor, U0126, 10 μ M) and Akt (with PI3K inhibitor, LY294002, 10 μ M) activation suppressed proliferation of adult spinal cord cells at 4 DIV; inhibition of PLCγ activation (with U73122, 2.5 μ M) had no effect (10 random fields with a 40× objective per coverslip were analyzed, n = 3 coverslips; ** P
    Figure Legend Snippet: Cell proliferation in adult spinal cord NSPC cultures requires activation of ERK1/2 and Akt. (A) Quantification of the normalized number of EdU+ cells showed that inhibition of ERK1/2 (with MEK inhibitor, U0126, 10 μ M) and Akt (with PI3K inhibitor, LY294002, 10 μ M) activation suppressed proliferation of adult spinal cord cells at 4 DIV; inhibition of PLCγ activation (with U73122, 2.5 μ M) had no effect (10 random fields with a 40× objective per coverslip were analyzed, n = 3 coverslips; ** P

    Techniques Used: Activation Assay, Inhibition

    9) Product Images from "Lack of Cyp1b1 Promotes the Proliferative and Migratory Phenotype of Perivascular Supporting Cells"

    Article Title: Lack of Cyp1b1 Promotes the Proliferative and Migratory Phenotype of Perivascular Supporting Cells

    Journal: Laboratory investigation; a journal of technical methods and pathology

    doi: 10.1038/labinvest.2013.55

    Alterations in cellular signaling pathways in cyp1b1−/− retinal PC. (a) Cyp1b1+/+ and cyp1b1−/− PC were analyzed by Western blot analysis for expression of phospho -Akt, total Akt, phospho-p38, total p38, phospho-Erk1/2, total Erk1/2, phospho-JNK, total JNK and β-actin. (b) Quantification of band intensity demonstrated a 1.5 fold increase in phospho-Akt (N=3, *P
    Figure Legend Snippet: Alterations in cellular signaling pathways in cyp1b1−/− retinal PC. (a) Cyp1b1+/+ and cyp1b1−/− PC were analyzed by Western blot analysis for expression of phospho -Akt, total Akt, phospho-p38, total p38, phospho-Erk1/2, total Erk1/2, phospho-JNK, total JNK and β-actin. (b) Quantification of band intensity demonstrated a 1.5 fold increase in phospho-Akt (N=3, *P

    Techniques Used: Western Blot, Expressing

    10) Product Images from "Activation of extracellular signal-regulated protein kinase 5 is essential for cystitis- and nerve growth factor-induced calcitonin gene-related peptide expression in sensory neurons"

    Article Title: Activation of extracellular signal-regulated protein kinase 5 is essential for cystitis- and nerve growth factor-induced calcitonin gene-related peptide expression in sensory neurons

    Journal: Molecular Pain

    doi: 10.1186/1744-8069-8-48

    Co-localization of CGRP with phospho-ERK5 but not phospho-Akt in L6 DRG during cystitis. Double immunostaining showed that a subpopulation of CGRP cells (A, green cells indicated by yellow arrows) also expressed phospho-ERK5 (B, red nuclear staining). In contrast, CGRP cells did not express phospho-Akt (D-F, blue arrows indicated CGRP cells, white arrows indicated Akt cells).
    Figure Legend Snippet: Co-localization of CGRP with phospho-ERK5 but not phospho-Akt in L6 DRG during cystitis. Double immunostaining showed that a subpopulation of CGRP cells (A, green cells indicated by yellow arrows) also expressed phospho-ERK5 (B, red nuclear staining). In contrast, CGRP cells did not express phospho-Akt (D-F, blue arrows indicated CGRP cells, white arrows indicated Akt cells).

    Techniques Used: Double Immunostaining, Staining

    Schematic diagram illustrates the putative mechanism for NGF signal transduction that mediates the interaction of the inflamed urinary bladder and bladder sensory neurons in the DRG. Cystitis - induced NGF expression in the urinary bladder binds to TrkA and activates ERK5 and CREB in DRG via retrograde transport. The NGF-ERK5-CREB axis leads to CGRP up-regulation in bladder afferent neurons (A). The NGF-induced Akt activation (B) may contribute to TRPV1 sensitization [ 61 ] but not the CGRP up-regulation in the DRG. In addition to regulating CGRP expression, activation of CREB in bladder afferent neurons may also control gene expression of other neuropeptides (NPP) (C). These multi-branches of signaling pathways triggered by NGF may together mediate cystitis-induced bladder hyperactivity.
    Figure Legend Snippet: Schematic diagram illustrates the putative mechanism for NGF signal transduction that mediates the interaction of the inflamed urinary bladder and bladder sensory neurons in the DRG. Cystitis - induced NGF expression in the urinary bladder binds to TrkA and activates ERK5 and CREB in DRG via retrograde transport. The NGF-ERK5-CREB axis leads to CGRP up-regulation in bladder afferent neurons (A). The NGF-induced Akt activation (B) may contribute to TRPV1 sensitization [ 61 ] but not the CGRP up-regulation in the DRG. In addition to regulating CGRP expression, activation of CREB in bladder afferent neurons may also control gene expression of other neuropeptides (NPP) (C). These multi-branches of signaling pathways triggered by NGF may together mediate cystitis-induced bladder hyperactivity.

    Techniques Used: Transduction, Expressing, Activation Assay

    Co-localization of phospho-CREB with phospho-ERK5 but not phospho-Akt in L6 DRG during cystitis. Double immunostaining showed that phospho-CREB in L6 DRG during cystitis (A, D: red nuclear staining) was co-localized with phospho-ERK5 (B, C: green nuclear staining) but not phospho-Akt (E, F: green cells). Bar = 60 μm.
    Figure Legend Snippet: Co-localization of phospho-CREB with phospho-ERK5 but not phospho-Akt in L6 DRG during cystitis. Double immunostaining showed that phospho-CREB in L6 DRG during cystitis (A, D: red nuclear staining) was co-localized with phospho-ERK5 (B, C: green nuclear staining) but not phospho-Akt (E, F: green cells). Bar = 60 μm.

    Techniques Used: Double Immunostaining, Staining

    11) Product Images from "ATF4 contributes to autophagy and survival in sunitinib treated brain tumor initiating cells (BTICs)"

    Article Title: ATF4 contributes to autophagy and survival in sunitinib treated brain tumor initiating cells (BTICs)

    Journal: Oncotarget

    doi: 10.18632/oncotarget.26569

    Downstream-signaling after treatment with RTK-Is ( A ) BTIC-10 cells were cultured in growth-factor free media overnight. Sunitinib (Su), Cediranib (Cd), Imantinib (Im) or DMSO (Ctr; equimolar) were added concomitantly with PDGF-AB (25 ng/ml) at the indicated concentrations. After 6 hours, cells were harvested in protein lysis buffer to prepare whole cell lysates. Phosphorylation of PDGFR-β and AKT was assessed by Western Blot. Actin was used as loading control. ( B ) BTICs, U87 and HTZ-349 were cultured and treated with indicated Sunitinib concentrations or Tunicamycin (Tm.) at 0.5 μg/ml. Whole cell protein lysates were prepared 24 hours post treatment and expression of ATF4, eIF2α and phosphorylation of eIF2α was assessed by Western Blot. Actin was used as loading control. ( C ) BTIC-10 cells were transfected with two different siRNAs against ATF4 (siATF4_1/siATF4_2) or non-targeting siRNA (NT-Ctr). Expression of ATF4 mRNA was analyzed by qRT-PCR. ( D ) BTIC-10 was transfected with siRNA against ATF4 or non-targeting siRNA (NT-Ctr) and exposed to treatment with Sunitinib (4 μM). Expression of TRB3, ATF6 and XBPS1 mRNA was analyzed by qRT-PCR. All measurements were performed in triplicates and standard curves were used for relative quantification of expression values. Data represent mean ± SD fold changes of expression relative to control treatment.
    Figure Legend Snippet: Downstream-signaling after treatment with RTK-Is ( A ) BTIC-10 cells were cultured in growth-factor free media overnight. Sunitinib (Su), Cediranib (Cd), Imantinib (Im) or DMSO (Ctr; equimolar) were added concomitantly with PDGF-AB (25 ng/ml) at the indicated concentrations. After 6 hours, cells were harvested in protein lysis buffer to prepare whole cell lysates. Phosphorylation of PDGFR-β and AKT was assessed by Western Blot. Actin was used as loading control. ( B ) BTICs, U87 and HTZ-349 were cultured and treated with indicated Sunitinib concentrations or Tunicamycin (Tm.) at 0.5 μg/ml. Whole cell protein lysates were prepared 24 hours post treatment and expression of ATF4, eIF2α and phosphorylation of eIF2α was assessed by Western Blot. Actin was used as loading control. ( C ) BTIC-10 cells were transfected with two different siRNAs against ATF4 (siATF4_1/siATF4_2) or non-targeting siRNA (NT-Ctr). Expression of ATF4 mRNA was analyzed by qRT-PCR. ( D ) BTIC-10 was transfected with siRNA against ATF4 or non-targeting siRNA (NT-Ctr) and exposed to treatment with Sunitinib (4 μM). Expression of TRB3, ATF6 and XBPS1 mRNA was analyzed by qRT-PCR. All measurements were performed in triplicates and standard curves were used for relative quantification of expression values. Data represent mean ± SD fold changes of expression relative to control treatment.

    Techniques Used: Cell Culture, Lysis, Western Blot, Expressing, Transfection, Quantitative RT-PCR

    12) Product Images from "A disease-associated Aifm1 variant induces severe myopathy in knockin mice"

    Article Title: A disease-associated Aifm1 variant induces severe myopathy in knockin mice

    Journal: Molecular Metabolism

    doi: 10.1016/j.molmet.2018.05.002

    AIF deficiency stimulates Akt and mTOR activity. (A–B) Immunoblot analyses were performed on (A) muscle and (B) cerebellar tissues from 3 to 6 month-old animals. Densitometry is relative to wt littermates and reported as mean ± SEM. Antibodies against total and phosphorylated forms of Akt, 40-kDa proline-rich Akt substrate (PRAS40), p70 S6 kinase (P70-S6K), ribosomal Protein S6 (RPS6) were used (n = 4–9 per genotype). GAPDH and actin were used as loading control (*** p
    Figure Legend Snippet: AIF deficiency stimulates Akt and mTOR activity. (A–B) Immunoblot analyses were performed on (A) muscle and (B) cerebellar tissues from 3 to 6 month-old animals. Densitometry is relative to wt littermates and reported as mean ± SEM. Antibodies against total and phosphorylated forms of Akt, 40-kDa proline-rich Akt substrate (PRAS40), p70 S6 kinase (P70-S6K), ribosomal Protein S6 (RPS6) were used (n = 4–9 per genotype). GAPDH and actin were used as loading control (*** p

    Techniques Used: Activity Assay

    13) Product Images from "Transforming Growth Factor-?1 Induces Expression of Human Coagulation Factor XII via Smad3 and JNK Signaling Pathways in Human Lung Fibroblasts *"

    Article Title: Transforming Growth Factor-?1 Induces Expression of Human Coagulation Factor XII via Smad3 and JNK Signaling Pathways in Human Lung Fibroblasts *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M109.045963

    TGF-β1 induces phosphorylation of MAPK, Akt, and Smad3, as well as translocation of phospho-Smad3 into the nucleus of HLF. A , HLF were treated for the indicated time points with TGF-β1, and the activation of p44/42, JNK, p38, and Akt kinases
    Figure Legend Snippet: TGF-β1 induces phosphorylation of MAPK, Akt, and Smad3, as well as translocation of phospho-Smad3 into the nucleus of HLF. A , HLF were treated for the indicated time points with TGF-β1, and the activation of p44/42, JNK, p38, and Akt kinases

    Techniques Used: Translocation Assay, Activation Assay

    14) Product Images from "Baicalein alters PI3K/Akt/GSK3β signaling pathway in rats with diabetes-associated cognitive deficits"

    Article Title: Baicalein alters PI3K/Akt/GSK3β signaling pathway in rats with diabetes-associated cognitive deficits

    Journal: International Journal of Clinical and Experimental Medicine

    doi:

    Effects of BAC on the protein levels of PI3K/Akt/GSK3β in diabetic rats hippocampus (n = 10, mean ± S.D.). ** P
    Figure Legend Snippet: Effects of BAC on the protein levels of PI3K/Akt/GSK3β in diabetic rats hippocampus (n = 10, mean ± S.D.). ** P

    Techniques Used: BAC Assay

    15) Product Images from "Pirfenidone inhibits myofibroblast differentiation and lung fibrosis development during insufficient mitophagy"

    Article Title: Pirfenidone inhibits myofibroblast differentiation and lung fibrosis development during insufficient mitophagy

    Journal: Respiratory Research

    doi: 10.1186/s12931-017-0600-3

    Hypothetical model of the anti-fibrotic mechanisms of PFD. PFD has previously reported anti-fibrotic mechanisms, including anti-inflammation, anti-pro-fibrotic cytokines, and anti-oxidative properties. Now PARK2-mediated autophay/mitophgy can be included in the anti-fibrotic properties of PFD. Although detailed mechanism remains elusive, PFD attenuates lung fibrosis seen during insufficient mitophagy through regulation of PDGFR-PI3K-Akt signaling by inhibiting mitochondrial ROS production
    Figure Legend Snippet: Hypothetical model of the anti-fibrotic mechanisms of PFD. PFD has previously reported anti-fibrotic mechanisms, including anti-inflammation, anti-pro-fibrotic cytokines, and anti-oxidative properties. Now PARK2-mediated autophay/mitophgy can be included in the anti-fibrotic properties of PFD. Although detailed mechanism remains elusive, PFD attenuates lung fibrosis seen during insufficient mitophagy through regulation of PDGFR-PI3K-Akt signaling by inhibiting mitochondrial ROS production

    Techniques Used:

    PFD attenuates myofibroblast differentiation during insufficient mitophagy via inhibiting PDGFR/PI3K/AKT signaling pathway in LF. a Fluorescence intensity of CM-H2DCFDA staining for intracellular ROS production. PFD (500 μg/ml) treatment was started 48 h post-siRNA transfection and incubation with CM-H2DCFDA (10 μM) was started after 24 h treatment in LF. The fluorescence level in the control siRNA transfected cells without PFD was designated as 1.0. The panel is the average (±SEM) taken from five independent experiments shown as relative expression.* p
    Figure Legend Snippet: PFD attenuates myofibroblast differentiation during insufficient mitophagy via inhibiting PDGFR/PI3K/AKT signaling pathway in LF. a Fluorescence intensity of CM-H2DCFDA staining for intracellular ROS production. PFD (500 μg/ml) treatment was started 48 h post-siRNA transfection and incubation with CM-H2DCFDA (10 μM) was started after 24 h treatment in LF. The fluorescence level in the control siRNA transfected cells without PFD was designated as 1.0. The panel is the average (±SEM) taken from five independent experiments shown as relative expression.* p

    Techniques Used: Fluorescence, Staining, Transfection, Incubation, Expressing

    16) Product Images from "Ferulic Acid Ameliorates Lipopolysaccharide-Induced Barrier Dysfunction via MicroRNA-200c-3p-Mediated Activation of PI3K/AKT Pathway in Caco-2 Cells"

    Article Title: Ferulic Acid Ameliorates Lipopolysaccharide-Induced Barrier Dysfunction via MicroRNA-200c-3p-Mediated Activation of PI3K/AKT Pathway in Caco-2 Cells

    Journal: Frontiers in Pharmacology

    doi: 10.3389/fphar.2020.00376

    FA attenuated LPS-induced intestinal epithelial barrier dysfunction via activating miR-200c-3p-mediated PTEN/AKT pathway in Caco-2 cells. (A) Cells were transfected with Lv-200c, Lv-200c spong and Lv-NC at an MOI of 15 and incubated at 37°C with 5% CO 2 for 48 h, and then cells were pretreated with FA (100 μM) for 2 h and stimulated with LPS for 24 h. The expression levels of PTEN, PI3K, p-PI3K, AKT and p-AKT were evaluated using western blotting. (B) Caco-2 cells were pretreated with 10 μM LY294002 for 1 h and then treated with 100 μM FA for 2 h. The expression levels of occludin and ZO-1 proteins were evaluated using Western blotting. Data were presented as means ± SD from three independent experiments and differences between means were compared using one-way ANOVA with Tukey’s multiple comparisons test. * P
    Figure Legend Snippet: FA attenuated LPS-induced intestinal epithelial barrier dysfunction via activating miR-200c-3p-mediated PTEN/AKT pathway in Caco-2 cells. (A) Cells were transfected with Lv-200c, Lv-200c spong and Lv-NC at an MOI of 15 and incubated at 37°C with 5% CO 2 for 48 h, and then cells were pretreated with FA (100 μM) for 2 h and stimulated with LPS for 24 h. The expression levels of PTEN, PI3K, p-PI3K, AKT and p-AKT were evaluated using western blotting. (B) Caco-2 cells were pretreated with 10 μM LY294002 for 1 h and then treated with 100 μM FA for 2 h. The expression levels of occludin and ZO-1 proteins were evaluated using Western blotting. Data were presented as means ± SD from three independent experiments and differences between means were compared using one-way ANOVA with Tukey’s multiple comparisons test. * P

    Techniques Used: Transfection, Incubation, Expressing, Western Blot

    FA ameliorated lipopolysaccharide-induced barrier dysfunction via miR-200c-3p-mediated activation of PI3K/AKT pathway in Caco-2 cells. FA exhibited the protective effects on LPS-induced barrier dysfunction involving in miR-200c-3p and PTEN/PI3K/Akt signaling pathway. FA promotes activation of PI3K/AKT pathway by miR-200c-3p-mediated suppression of the negative mediator PTEN, which, in turn, maintains TJ function and thus ameliorates LPS-induced intestinal epithelial barrier dysfunction.
    Figure Legend Snippet: FA ameliorated lipopolysaccharide-induced barrier dysfunction via miR-200c-3p-mediated activation of PI3K/AKT pathway in Caco-2 cells. FA exhibited the protective effects on LPS-induced barrier dysfunction involving in miR-200c-3p and PTEN/PI3K/Akt signaling pathway. FA promotes activation of PI3K/AKT pathway by miR-200c-3p-mediated suppression of the negative mediator PTEN, which, in turn, maintains TJ function and thus ameliorates LPS-induced intestinal epithelial barrier dysfunction.

    Techniques Used: Activation Assay

    17) Product Images from "LDL Receptor–Related Protein 6 Modulates Ret Proto-Oncogene Signaling in Renal Development and Cystic Dysplasia"

    Article Title: LDL Receptor–Related Protein 6 Modulates Ret Proto-Oncogene Signaling in Renal Development and Cystic Dysplasia

    Journal: Journal of the American Society of Nephrology : JASN

    doi: 10.1681/ASN.2014100998

    Alterations of Ret downstream factors modulated by Lrp6 knockdown and restored by Wnt agonists. Western blots were carried out for p-MAPK1/3, p-Akt, and p-PLC γ in mIMCD3 (A, B) and Neuro-2a (C, D) cells after Lrp6 -knockdown using siRNAs and treated with or without lithium chloride. Scrambled siRNAs are used as the negative control for the knockdown. Only phosphorylated (p)-MAPK1/3 shows significant changes after different treatments in both cell lines (B, D). * P
    Figure Legend Snippet: Alterations of Ret downstream factors modulated by Lrp6 knockdown and restored by Wnt agonists. Western blots were carried out for p-MAPK1/3, p-Akt, and p-PLC γ in mIMCD3 (A, B) and Neuro-2a (C, D) cells after Lrp6 -knockdown using siRNAs and treated with or without lithium chloride. Scrambled siRNAs are used as the negative control for the knockdown. Only phosphorylated (p)-MAPK1/3 shows significant changes after different treatments in both cell lines (B, D). * P

    Techniques Used: Western Blot, Planar Chromatography, Negative Control

    18) Product Images from "Conditional Knockout of Myocyte Focal Adhesion Kinase Abrogates Ischemic Preconditioning in Adult Murine Hearts"

    Article Title: Conditional Knockout of Myocyte Focal Adhesion Kinase Abrogates Ischemic Preconditioning in Adult Murine Hearts

    Journal: Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

    doi: 10.1161/JAHA.113.000457

    FAK KO abrogates IP‐induced PI3K/Akt signaling. Representative Western blots showing (A) pPI3K p85; (B) pAkt expression in lysates from hearts of WT and FAK KO mice subjected to either the IP protocol or a sham procedure; (C) normalized integrated density data for cardiac pPI3K p85 expression; and (D) pAkt expression. In WT mice IP significantly enhanced pPI3K p85 expression by 67.2% ( P ≤0.01; n=5 hearts, both groups) and pAkt expression by 88.8% ( P ≤0.001; n=4 hearts, both groups) versus WT mice subjected to the sham experimental protocol. pPI3K p85 and pAkt expression in FAK KO mice subjected to the IP protocol was not significantly different from their expression in either WT or FAK KO sham hearts. FAK indicates focal adhesion kinase; IP, ischemic preconditioning; KO, knock out; PI3K, phosphatidylinositol‐3‐kinase; WT, wild‐type.
    Figure Legend Snippet: FAK KO abrogates IP‐induced PI3K/Akt signaling. Representative Western blots showing (A) pPI3K p85; (B) pAkt expression in lysates from hearts of WT and FAK KO mice subjected to either the IP protocol or a sham procedure; (C) normalized integrated density data for cardiac pPI3K p85 expression; and (D) pAkt expression. In WT mice IP significantly enhanced pPI3K p85 expression by 67.2% ( P ≤0.01; n=5 hearts, both groups) and pAkt expression by 88.8% ( P ≤0.001; n=4 hearts, both groups) versus WT mice subjected to the sham experimental protocol. pPI3K p85 and pAkt expression in FAK KO mice subjected to the IP protocol was not significantly different from their expression in either WT or FAK KO sham hearts. FAK indicates focal adhesion kinase; IP, ischemic preconditioning; KO, knock out; PI3K, phosphatidylinositol‐3‐kinase; WT, wild‐type.

    Techniques Used: Western Blot, Expressing, Mouse Assay, Knock-Out

    19) Product Images from "Energy restriction and exercise modulate angiopoietins and vascular endothelial growth factor expression in the cavernous tissue of high-fat diet-fed rats"

    Article Title: Energy restriction and exercise modulate angiopoietins and vascular endothelial growth factor expression in the cavernous tissue of high-fat diet-fed rats

    Journal: Asian Journal of Andrology

    doi: 10.1038/aja.2011.131

    Western blot analysis of total eNOS, phospho-Akt and total-Akt. Representative bands obtained by Western blot analysis of total eNOS ( a ), total-Akt ( b ) and phospho-Akt ( c ) in the rat cavernous tissue of all experimental groups. The graphs below represent the semiquantitative analysis of the aforementioned proteins ( n =4 for each group). The total eNOS and total-Akt were normalized to β-actin, used as the loading control. Phospho-Akt levels were normalized to semiquantified total-Akt in each sample. Error bars represent standard deviation. C, control animal group; ER, energy-restricted animal group; EREx, energy-restricted and exercised animal group; HFD, high-fat diet-fed animal group. * P
    Figure Legend Snippet: Western blot analysis of total eNOS, phospho-Akt and total-Akt. Representative bands obtained by Western blot analysis of total eNOS ( a ), total-Akt ( b ) and phospho-Akt ( c ) in the rat cavernous tissue of all experimental groups. The graphs below represent the semiquantitative analysis of the aforementioned proteins ( n =4 for each group). The total eNOS and total-Akt were normalized to β-actin, used as the loading control. Phospho-Akt levels were normalized to semiquantified total-Akt in each sample. Error bars represent standard deviation. C, control animal group; ER, energy-restricted animal group; EREx, energy-restricted and exercised animal group; HFD, high-fat diet-fed animal group. * P

    Techniques Used: Western Blot, Standard Deviation

    20) Product Images from "c-Met-induced epithelial carcinogenesis is initiated by the serine protease matriptase"

    Article Title: c-Met-induced epithelial carcinogenesis is initiated by the serine protease matriptase

    Journal: Oncogene

    doi: 10.1038/onc.2010.586

    Potentiation of squamous cell carcinogenesis by matriptase 1. Mesenchymal cells located in close proximity to c-Met- and matriptase-expressing basal keratinocytes with high tumorigenic potential secrete single-chain proHGF/SF into the pericellular microenvironment. 2. ProHGF/SF binds c-Met with high affinity on the keratinocyte cell surface. 3. Matriptase cleaves and converts single-chain proHGF/SF to signaling-competent two-chain HGF/SF. 4. Matriptase-cleaved two-chain HGF/SF undergoes a conformational change that enables c-Met activation by autophosphorylation. 5. Activation of c-Met leads to recruitment of Gab1 and other effectors of c-Met signaling. 6. Gab1 recruitment initiates a pro-tumorgenic PI3K-Akt-mTor signaling pathway. 7. Activation of additional unidentified signaling pathway(s) located downstream from c-Met (hatched arrows) induces constitutive keratinocyte proliferation. Matriptase-induced mTor activation and mitogenic signaling, in combination with other epigenetic and genetic changes ( ras -dependent and ras -independent), causes malignant transformation. The model is synthesized on the basis of data obtained in (7), and the current study.
    Figure Legend Snippet: Potentiation of squamous cell carcinogenesis by matriptase 1. Mesenchymal cells located in close proximity to c-Met- and matriptase-expressing basal keratinocytes with high tumorigenic potential secrete single-chain proHGF/SF into the pericellular microenvironment. 2. ProHGF/SF binds c-Met with high affinity on the keratinocyte cell surface. 3. Matriptase cleaves and converts single-chain proHGF/SF to signaling-competent two-chain HGF/SF. 4. Matriptase-cleaved two-chain HGF/SF undergoes a conformational change that enables c-Met activation by autophosphorylation. 5. Activation of c-Met leads to recruitment of Gab1 and other effectors of c-Met signaling. 6. Gab1 recruitment initiates a pro-tumorgenic PI3K-Akt-mTor signaling pathway. 7. Activation of additional unidentified signaling pathway(s) located downstream from c-Met (hatched arrows) induces constitutive keratinocyte proliferation. Matriptase-induced mTor activation and mitogenic signaling, in combination with other epigenetic and genetic changes ( ras -dependent and ras -independent), causes malignant transformation. The model is synthesized on the basis of data obtained in (7), and the current study.

    Techniques Used: Expressing, Activation Assay, Transformation Assay, Synthesized

    21) Product Images from "TRAIL (TNF-related apoptosis-inducing ligand) inhibits human adipocyte differentiation via caspase-mediated downregulation of adipogenic transcription factors"

    Article Title: TRAIL (TNF-related apoptosis-inducing ligand) inhibits human adipocyte differentiation via caspase-mediated downregulation of adipogenic transcription factors

    Journal: Cell Death & Disease

    doi: 10.1038/cddis.2016.286

    TRAIL induces the activation of ERK1/2, but ERK1/2 is not involved in the effect of TRAIL. ( a ) SGBS cells were treated with TRAIL (30 ng/ml) for different time points (15 min, 1, 2, 6, 12, and 24 h). Protein was isolated and the phosphorylation of I κ B α , JNK, p38, Akt, and ERK1/2 was analyzed by western blot. β -Actin was used as a loading control. The positions of the molecular weight markers (kDa) are indicated. One representative out of three experiments performed is presented. ( b – d ) Human SGBS cells were treated with TRAIL (30 ng/ml) during the first 4 days of adipogenic differentiation in the absence or presence of the MEK1/2 inhibitor PD98059 (100 μ M). ( b ) The inhibition of ERK1/2 phosphorylation by PD98059 was confirmed by western blot. Here, cells were stimulated for 6 h. One representative out of three experiments performed is presented. ( c ) The rate of adipogenic differentiation was determined by cell counting on day 10 of differentiation. Displayed are the means and S.E.M. of three independent experiments. ( d ) RNA was isolated and adipocyte marker gene expression (PPAR γ , Glut-4, adiponectin) was determined by qPCR. The mRNA levels were normalized to the gene HPRT. Displayed are the means and S.E.M. of three independent experiments. One-way ANOVA and Turkey's multiple comparison were used to test for statistical significance in ( c and d ). * P
    Figure Legend Snippet: TRAIL induces the activation of ERK1/2, but ERK1/2 is not involved in the effect of TRAIL. ( a ) SGBS cells were treated with TRAIL (30 ng/ml) for different time points (15 min, 1, 2, 6, 12, and 24 h). Protein was isolated and the phosphorylation of I κ B α , JNK, p38, Akt, and ERK1/2 was analyzed by western blot. β -Actin was used as a loading control. The positions of the molecular weight markers (kDa) are indicated. One representative out of three experiments performed is presented. ( b – d ) Human SGBS cells were treated with TRAIL (30 ng/ml) during the first 4 days of adipogenic differentiation in the absence or presence of the MEK1/2 inhibitor PD98059 (100 μ M). ( b ) The inhibition of ERK1/2 phosphorylation by PD98059 was confirmed by western blot. Here, cells were stimulated for 6 h. One representative out of three experiments performed is presented. ( c ) The rate of adipogenic differentiation was determined by cell counting on day 10 of differentiation. Displayed are the means and S.E.M. of three independent experiments. ( d ) RNA was isolated and adipocyte marker gene expression (PPAR γ , Glut-4, adiponectin) was determined by qPCR. The mRNA levels were normalized to the gene HPRT. Displayed are the means and S.E.M. of three independent experiments. One-way ANOVA and Turkey's multiple comparison were used to test for statistical significance in ( c and d ). * P

    Techniques Used: Activation Assay, Isolation, Western Blot, Molecular Weight, Inhibition, Cell Counting, Marker, Expressing, Real-time Polymerase Chain Reaction

    22) Product Images from "TNF‐α promotes invasive growth through the MET signaling pathway), TNF‐α promotes invasive growth through the MET signaling pathway"

    Article Title: TNF‐α promotes invasive growth through the MET signaling pathway), TNF‐α promotes invasive growth through the MET signaling pathway

    Journal: Molecular Oncology

    doi: 10.1016/j.molonc.2014.09.002

    TNF‐α sustains the MEK‐ERK pathway through MET, and the MEK‐ERK pathway is required for cell invasion. (A) Western blot showing phosphorylation of MEK1/2 (p‐MEK 1/2), p42/44 ERK 1/2 (p‐ERK 1/2), and Akt (p‐Akt), and the respective total proteins, at the indicated time‐points after A549 treatment with TNF‐α (10 ng/ml), in the absence or in the presence of JNJ‐38877605 (500 nM). Vinculin was probed as control of equal protein loading. (B) Western blot showing E‐cadherin and Egr‐1 expression at the indicated time‐points after A549 treatment with TNF‐α (10 ng/ml), in the absence or in the presence of the MEK inhibitor PD 98059 (20 μM). GAPDH was probed as control of equal protein loading. (C) A549 cell migration assessed in Transwell assay 24 h after treatment with TNF‐α (10 ng/ml), in the absence or in the presence of PD 98059 (20 μM). Graphs represent the fold change vs. control (untreated cells) of the number of migrating cells. Bars: mean of three independent experiments ± SEM. (D) A549 cell invasion assessed in Transwell assay 24 h after treatment with TNF‐α (10 ng/ml), in cells transfected 48 h before with siRNA against EGR‐1 (siEGR‐1) or control siRNA (siCTRL). Graphs represent the fold change vs. control (untreated cells) of the number of invading cells. Bars: mean of three independent experiments ± S.E.M.
    Figure Legend Snippet: TNF‐α sustains the MEK‐ERK pathway through MET, and the MEK‐ERK pathway is required for cell invasion. (A) Western blot showing phosphorylation of MEK1/2 (p‐MEK 1/2), p42/44 ERK 1/2 (p‐ERK 1/2), and Akt (p‐Akt), and the respective total proteins, at the indicated time‐points after A549 treatment with TNF‐α (10 ng/ml), in the absence or in the presence of JNJ‐38877605 (500 nM). Vinculin was probed as control of equal protein loading. (B) Western blot showing E‐cadherin and Egr‐1 expression at the indicated time‐points after A549 treatment with TNF‐α (10 ng/ml), in the absence or in the presence of the MEK inhibitor PD 98059 (20 μM). GAPDH was probed as control of equal protein loading. (C) A549 cell migration assessed in Transwell assay 24 h after treatment with TNF‐α (10 ng/ml), in the absence or in the presence of PD 98059 (20 μM). Graphs represent the fold change vs. control (untreated cells) of the number of migrating cells. Bars: mean of three independent experiments ± SEM. (D) A549 cell invasion assessed in Transwell assay 24 h after treatment with TNF‐α (10 ng/ml), in cells transfected 48 h before with siRNA against EGR‐1 (siEGR‐1) or control siRNA (siCTRL). Graphs represent the fold change vs. control (untreated cells) of the number of invading cells. Bars: mean of three independent experiments ± S.E.M.

    Techniques Used: Western Blot, Expressing, Migration, Transwell Assay, Transfection

    23) Product Images from "Protection against Fas-induced fulminant hepatic failure in liver specific integrin linked kinase knockout mice"

    Article Title: Protection against Fas-induced fulminant hepatic failure in liver specific integrin linked kinase knockout mice

    Journal: Comparative Hepatology

    doi: 10.1186/1476-5926-10-11

    ILK KO hepatocytes are protected against Jo-2 induced apoptosis in vitro . A) Caspase 3/7 activity at 6 h after treatment of WT and ILK KO hepatocytes with Jo-2 (0.5 μg/ml) and Actinomycin D (0.05 μg/ml). Fold change is the ratio of luminescence value of treatment group with its corresponding no treatment group. B) Effect of ERK1/2 inhibition using a MEK inhibitor U0126 (20 μM). Representative Western blots of cleaved caspase and PARP 6 h after Jo-2, vehicle or Jo-2+inhibitor administration. (Akt Inh: Akt inhibitor LY-294002, ERK Inh: ERK inhibitor U0126) C) Representative Western blots showing inhibition of phosphorylation of ERK1/2 by U0126 in ILK KO hepatocytes after 6 h after treatment with U0126. D) Representative Western blots of PARP after inhibition of NFκB using a synthetic peptide 6 h after treatment with Control peptide (CP), CP+Jo-2 and NP+Jo-2 (NFκB peptide). (CP: control peptide, NP: NFκB peptide). E) Total FAK and p-FAK at 0 and 6 h after Jo-2 administration in vitro. F) Total FAK and p-FAK at 0 and 6 h after Jo-2 administration in vivo.
    Figure Legend Snippet: ILK KO hepatocytes are protected against Jo-2 induced apoptosis in vitro . A) Caspase 3/7 activity at 6 h after treatment of WT and ILK KO hepatocytes with Jo-2 (0.5 μg/ml) and Actinomycin D (0.05 μg/ml). Fold change is the ratio of luminescence value of treatment group with its corresponding no treatment group. B) Effect of ERK1/2 inhibition using a MEK inhibitor U0126 (20 μM). Representative Western blots of cleaved caspase and PARP 6 h after Jo-2, vehicle or Jo-2+inhibitor administration. (Akt Inh: Akt inhibitor LY-294002, ERK Inh: ERK inhibitor U0126) C) Representative Western blots showing inhibition of phosphorylation of ERK1/2 by U0126 in ILK KO hepatocytes after 6 h after treatment with U0126. D) Representative Western blots of PARP after inhibition of NFκB using a synthetic peptide 6 h after treatment with Control peptide (CP), CP+Jo-2 and NP+Jo-2 (NFκB peptide). (CP: control peptide, NP: NFκB peptide). E) Total FAK and p-FAK at 0 and 6 h after Jo-2 administration in vitro. F) Total FAK and p-FAK at 0 and 6 h after Jo-2 administration in vivo.

    Techniques Used: In Vitro, Activity Assay, Inhibition, Western Blot, In Vivo

    24) Product Images from "Selective activation of epidermal growth factor receptor in renal proximal tubule induces tubulointerstitial fibrosis"

    Article Title: Selective activation of epidermal growth factor receptor in renal proximal tubule induces tubulointerstitial fibrosis

    Journal: The FASEB Journal

    doi: 10.1096/fj.201601359RR

    Expression of epithelial hHB-EGF is sufficient to activate EGFR and the related downstream pathways in hHB-EGF Tg/Tg mice. A ) Immunoblotting revealed increased phosphorylation of EGFR at multiple tyrosine sites (Y845, Y1173, and Y1068) in hHB-EGF Tg/Tg mice compared with wild-type mice. β-Actin acted as loading control ( n = 3 mice in each group). B ) Total EGFR protein expression in hHB-EGF Tg/Tg mice was comparable to wild-type mice. β-Actin acted as loading control ( n = 3 mice in each group). C ) Immunohistochemical analysis demonstrated activated EGFR predominantly in the tubules of 2-mo-old hHB-EGF Tg/Tg kidneys. D ) Immunohistochemical analysis demonstrated an increased activation of ERK (phospho-ERK), SMAD2 (phospho-SMAD2), and SMAD3 (phospho-SMAD3) in the tubules of hHB-EGF Tg/Tg kidneys. E ) Increased phosphorylation of ERK, SMAD2, AKT, p38, 4E-BP, and Src Y416 occurred in hHB-EGF Tg/Tg mice compared with wild-type mice as assessed by immunoblotting ( n = 3 mice in each group). β-Actin acted as loading control. Original magnification, ×160 ( C , D )
    Figure Legend Snippet: Expression of epithelial hHB-EGF is sufficient to activate EGFR and the related downstream pathways in hHB-EGF Tg/Tg mice. A ) Immunoblotting revealed increased phosphorylation of EGFR at multiple tyrosine sites (Y845, Y1173, and Y1068) in hHB-EGF Tg/Tg mice compared with wild-type mice. β-Actin acted as loading control ( n = 3 mice in each group). B ) Total EGFR protein expression in hHB-EGF Tg/Tg mice was comparable to wild-type mice. β-Actin acted as loading control ( n = 3 mice in each group). C ) Immunohistochemical analysis demonstrated activated EGFR predominantly in the tubules of 2-mo-old hHB-EGF Tg/Tg kidneys. D ) Immunohistochemical analysis demonstrated an increased activation of ERK (phospho-ERK), SMAD2 (phospho-SMAD2), and SMAD3 (phospho-SMAD3) in the tubules of hHB-EGF Tg/Tg kidneys. E ) Increased phosphorylation of ERK, SMAD2, AKT, p38, 4E-BP, and Src Y416 occurred in hHB-EGF Tg/Tg mice compared with wild-type mice as assessed by immunoblotting ( n = 3 mice in each group). β-Actin acted as loading control. Original magnification, ×160 ( C , D )

    Techniques Used: Expressing, Mouse Assay, Immunohistochemistry, Activation Assay

    25) Product Images from "HIF-?/MIF and NF-?B/IL-6 Axes Contribute to the Recruitment of CD11b+Gr-1+ Myeloid Cells in Hypoxic Microenvironment of HNSCC 1HIF-?/MIF and NF-?B/IL-6 Axes Contribute to the Recruitment of CD11b+Gr-1+ Myeloid Cells in Hypoxic Microenvironment of HNSCC 1 2"

    Article Title: HIF-?/MIF and NF-?B/IL-6 Axes Contribute to the Recruitment of CD11b+Gr-1+ Myeloid Cells in Hypoxic Microenvironment of HNSCC 1HIF-?/MIF and NF-?B/IL-6 Axes Contribute to the Recruitment of CD11b+Gr-1+ Myeloid Cells in Hypoxic Microenvironment of HNSCC 1 2

    Journal: Neoplasia (New York, N.Y.)

    doi:

    MIF/CD74/CXCR2/CXCR4 complexes contribute to migration of CD11b+Gr-1+ myeloid cells through p38/MAPK and PI3K/AKT signaling pathways. (A) Expression of CD74, CXCR4, and CXCR2 in the CD11b+Gr-1+ myeloid cells was measured by Western blot. Protein samples
    Figure Legend Snippet: MIF/CD74/CXCR2/CXCR4 complexes contribute to migration of CD11b+Gr-1+ myeloid cells through p38/MAPK and PI3K/AKT signaling pathways. (A) Expression of CD74, CXCR4, and CXCR2 in the CD11b+Gr-1+ myeloid cells was measured by Western blot. Protein samples

    Techniques Used: Migration, Expressing, Western Blot

    26) Product Images from "Human Vascular Endothelial Growth Factor Protects Axotomized Retinal Ganglion Cells In Vivo by Activating ERK-1/2 and Akt Pathways"

    Article Title: Human Vascular Endothelial Growth Factor Protects Axotomized Retinal Ganglion Cells In Vivo by Activating ERK-1/2 and Akt Pathways

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.0434-06.2006

    VEGF stimulates ERK-1/2 and Akt and inhibits p38 and caspase-3 pathways after RGC axotomy. Western blots with protein lysates of axotomized and contralateral nonaxotomized retinas of ntg and V1tg mice. Antibodies detecting both total (i.e., nonphosphorylated and phosphorylated) and phosphorylated signal factors were used. Note that VEGF increases phosphorylated (but not total) ERK-1/2 levels both in nonaxotomized and axotomized V1tg retinas. After axotomy, VEGF elevates phosphorylated Akt levels and furthermore reduces phosphorylated p38 and activated caspase-3. C, Nonaxotomized eye; A, axotomized eye. Data are mean ± SD values ( n = 3 different samples per group), normalized with corresponding blots for β-actin. * p
    Figure Legend Snippet: VEGF stimulates ERK-1/2 and Akt and inhibits p38 and caspase-3 pathways after RGC axotomy. Western blots with protein lysates of axotomized and contralateral nonaxotomized retinas of ntg and V1tg mice. Antibodies detecting both total (i.e., nonphosphorylated and phosphorylated) and phosphorylated signal factors were used. Note that VEGF increases phosphorylated (but not total) ERK-1/2 levels both in nonaxotomized and axotomized V1tg retinas. After axotomy, VEGF elevates phosphorylated Akt levels and furthermore reduces phosphorylated p38 and activated caspase-3. C, Nonaxotomized eye; A, axotomized eye. Data are mean ± SD values ( n = 3 different samples per group), normalized with corresponding blots for β-actin. * p

    Techniques Used: Western Blot, Mouse Assay

    27) Product Images from "Lrig2-Deficient Mice Are Protected against PDGFB-Induced Glioma"

    Article Title: Lrig2-Deficient Mice Are Protected against PDGFB-Induced Glioma

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0073635

    PDGF induced phosphorylation events in cells of different Lrig2 genotypes. Wild-type, heterozygous, or Lrig2 -deficient MEFs were serum starved for 24 hours followed by stimulation with 50 ng/ml PDGF-BB for different times. ( A – N ) Cells were untreated or stimulated with 50 ng/ml PDGF-BB for 10 minutes followed by cell fixation and analysis of the phosphorylation status of respective Pdgfr by in situ proximity ligation assay (PLA). Phosphorylated Pdgfr was visualized using fluorescence (red spots). Cell nuclei were counter-stained with DAPI (blue). ( A – F ) Representative PLA images of phosphorylated Pdgfrα (red spots) in un-stimulated ( A – C ) or PDGF-BB stimulated ( D – F ) cells of the indicated Lrig2 genotypes. ( G – L ) Representative PLA images of phosphorylated Pdgfrβ (red spots) in non-stimulated ( G – I ) or PDGF-BB-stimulated ( J – L ) cells of the indicated Lrig2 genotypes. ( M ) Quantification of PLA spots for phosphorylated Pdgfrα. Shown are the means from three independent experiments, including wild-type ( Lrig2E12+/+ , n=8), heterozygous ( Lrig2E12+/- , n=9), and Lrig2 -deficient ( Lrig2E12-/ -, n=6) cell lines from three different litters, with standard deviations indicated by error bars. ( N ) Quantification of PLA spots for phosphorylated Pdgfrβ. Shown are the means from three independent experiments, including wild-type ( Lrig2E12+/+ , n=8), heterozygous ( Lrig2E12+/- , n=9), and Lrig2 -deficient ( Lrig2E12-/ -, n=5) cell lines from three different litters, with standard deviations indicated by error bars. There were no differences observed in the levels of activated Pdgfrα or Pdgfrβ between cells of different genotypes. ( O – Q ) Cell lysates from cells that had been untreated or treated with 50 ng/ml PDGF-BB for 15 minutes were analyzed through Western blotting with antibodies against the indicated proteins. ( O ) A representative Western blot is shown of Akt, Erk1/2, phosphorylated Akt (pAkt), and phosphorylated Erk1/2 (pErk1/2) using cell lysates from cells of the indicated Lrig2 genotypes that had been untreated (-) or treated (+) with PDGF-BB. ( P ) Quantification of pAkt/Akt-ratios for non-stimulated and stimulated cells, respectively. Shown are the means from three independent experiments, including wild-type (n=8), heterozygous (n=9), and Lrig2 -deficient (n=5) cell lines from three different litters, with standard deviations indicated by error bars. ( Q ) Quantification of pErk1/2/Erk1/2-ratios for non-stimulated and stimulated cells, respectively. Shown are the means and corresponding standard deviations as for P .
    Figure Legend Snippet: PDGF induced phosphorylation events in cells of different Lrig2 genotypes. Wild-type, heterozygous, or Lrig2 -deficient MEFs were serum starved for 24 hours followed by stimulation with 50 ng/ml PDGF-BB for different times. ( A – N ) Cells were untreated or stimulated with 50 ng/ml PDGF-BB for 10 minutes followed by cell fixation and analysis of the phosphorylation status of respective Pdgfr by in situ proximity ligation assay (PLA). Phosphorylated Pdgfr was visualized using fluorescence (red spots). Cell nuclei were counter-stained with DAPI (blue). ( A – F ) Representative PLA images of phosphorylated Pdgfrα (red spots) in un-stimulated ( A – C ) or PDGF-BB stimulated ( D – F ) cells of the indicated Lrig2 genotypes. ( G – L ) Representative PLA images of phosphorylated Pdgfrβ (red spots) in non-stimulated ( G – I ) or PDGF-BB-stimulated ( J – L ) cells of the indicated Lrig2 genotypes. ( M ) Quantification of PLA spots for phosphorylated Pdgfrα. Shown are the means from three independent experiments, including wild-type ( Lrig2E12+/+ , n=8), heterozygous ( Lrig2E12+/- , n=9), and Lrig2 -deficient ( Lrig2E12-/ -, n=6) cell lines from three different litters, with standard deviations indicated by error bars. ( N ) Quantification of PLA spots for phosphorylated Pdgfrβ. Shown are the means from three independent experiments, including wild-type ( Lrig2E12+/+ , n=8), heterozygous ( Lrig2E12+/- , n=9), and Lrig2 -deficient ( Lrig2E12-/ -, n=5) cell lines from three different litters, with standard deviations indicated by error bars. There were no differences observed in the levels of activated Pdgfrα or Pdgfrβ between cells of different genotypes. ( O – Q ) Cell lysates from cells that had been untreated or treated with 50 ng/ml PDGF-BB for 15 minutes were analyzed through Western blotting with antibodies against the indicated proteins. ( O ) A representative Western blot is shown of Akt, Erk1/2, phosphorylated Akt (pAkt), and phosphorylated Erk1/2 (pErk1/2) using cell lysates from cells of the indicated Lrig2 genotypes that had been untreated (-) or treated (+) with PDGF-BB. ( P ) Quantification of pAkt/Akt-ratios for non-stimulated and stimulated cells, respectively. Shown are the means from three independent experiments, including wild-type (n=8), heterozygous (n=9), and Lrig2 -deficient (n=5) cell lines from three different litters, with standard deviations indicated by error bars. ( Q ) Quantification of pErk1/2/Erk1/2-ratios for non-stimulated and stimulated cells, respectively. Shown are the means and corresponding standard deviations as for P .

    Techniques Used: In Situ, Proximity Ligation Assay, Fluorescence, Staining, Western Blot

    28) Product Images from "Phagosomal removal of fungal melanin reprograms macrophage metabolism to promote antifungal immunity"

    Article Title: Phagosomal removal of fungal melanin reprograms macrophage metabolism to promote antifungal immunity

    Journal: Nature Communications

    doi: 10.1038/s41467-020-16120-z

    mTOR and HIF-1α reprogram metabolism in response to A. fumigatus . a Transcriptional profiles of macrophages left untreated (Ctrl) or infected with A. fumigatus (Af) for 2 h ( n = 3). Expression of genes is presented as centered and scaled log 2 fluorescence intensity (blue and red keys). b The total and p-p70S6K and total and p-Akt in macrophages infected with the Δ ku80 or Δ pksP strains for 4 h (representative of three independent experiments, with β-actin used as loading control). c Lactate secretion and d production of IL-1β, TNF, and IL-6 by macrophages left untreated (Ctrl) or infected with the Δ ku80 strain for 24 h without or with 10 mM rapamycin ( n = 6). e Expression of HIF-1α in macrophages left untreated (Ctrl) or infected with the Δ ku80 , Δ rodA/pksP or the melanin-coated Δ rodA/pksP strain for 2 h (representative of three independent experiments). The white arrows indicate accumulation in the nuclei of macrophages. Scale bars, 100 µm. f Lactate secretion and g production of IL-1β by BMDMs from C57BL/6 and HIF-1 c mice left untreated (Ctrl) or infected with the Δ ku80 or Δ pksP strains for 24 h ( n = 4). h Levels of total and p-p70S6K in macrophages left untreated (Ctrl) or infected with the Δ ku80 , Δ pksP , Δ rodA/pksP , or melanin-coated Δ rodA/pksP strains for 3 h (representative of three independent experiments, with β-actin used as loading control). The pixel density of the p-p70S6K/p70S6K ratio was normalized to β-actin. Data are expressed as mean values ± SEM. P -values were calculated using Student’s two-tailed t test or one-way ANOVA with Tukey’s multiple comparisons test.
    Figure Legend Snippet: mTOR and HIF-1α reprogram metabolism in response to A. fumigatus . a Transcriptional profiles of macrophages left untreated (Ctrl) or infected with A. fumigatus (Af) for 2 h ( n = 3). Expression of genes is presented as centered and scaled log 2 fluorescence intensity (blue and red keys). b The total and p-p70S6K and total and p-Akt in macrophages infected with the Δ ku80 or Δ pksP strains for 4 h (representative of three independent experiments, with β-actin used as loading control). c Lactate secretion and d production of IL-1β, TNF, and IL-6 by macrophages left untreated (Ctrl) or infected with the Δ ku80 strain for 24 h without or with 10 mM rapamycin ( n = 6). e Expression of HIF-1α in macrophages left untreated (Ctrl) or infected with the Δ ku80 , Δ rodA/pksP or the melanin-coated Δ rodA/pksP strain for 2 h (representative of three independent experiments). The white arrows indicate accumulation in the nuclei of macrophages. Scale bars, 100 µm. f Lactate secretion and g production of IL-1β by BMDMs from C57BL/6 and HIF-1 c mice left untreated (Ctrl) or infected with the Δ ku80 or Δ pksP strains for 24 h ( n = 4). h Levels of total and p-p70S6K in macrophages left untreated (Ctrl) or infected with the Δ ku80 , Δ pksP , Δ rodA/pksP , or melanin-coated Δ rodA/pksP strains for 3 h (representative of three independent experiments, with β-actin used as loading control). The pixel density of the p-p70S6K/p70S6K ratio was normalized to β-actin. Data are expressed as mean values ± SEM. P -values were calculated using Student’s two-tailed t test or one-way ANOVA with Tukey’s multiple comparisons test.

    Techniques Used: Infection, Expressing, Fluorescence, Mouse Assay, Two Tailed Test

    29) Product Images from "Liver X receptor agonist treatment attenuates cardiac dysfunction in type 2 diabetic db/db mice"

    Article Title: Liver X receptor agonist treatment attenuates cardiac dysfunction in type 2 diabetic db/db mice

    Journal: Cardiovascular Diabetology

    doi: 10.1186/s12933-014-0149-0

    GW3965 differentially regulated Akt and MAP kinases activation. a - c . Western blot analysis shows the phosphorylation and protein expression of Akt, p38 MAPK and JNK expression in the myocardial tissues (n =5-6). ** P
    Figure Legend Snippet: GW3965 differentially regulated Akt and MAP kinases activation. a - c . Western blot analysis shows the phosphorylation and protein expression of Akt, p38 MAPK and JNK expression in the myocardial tissues (n =5-6). ** P

    Techniques Used: Activation Assay, Western Blot, Expressing

    30) Product Images from "A blockade of PD-L1 produced antitumor and antimetastatic effects in an orthotopic mouse pancreatic cancer model via the PI3K/Akt/mTOR signaling pathway"

    Article Title: A blockade of PD-L1 produced antitumor and antimetastatic effects in an orthotopic mouse pancreatic cancer model via the PI3K/Akt/mTOR signaling pathway

    Journal: OncoTargets and therapy

    doi: 10.2147/OTT.S130481

    Effect of anti-PD-L1 antibody on expression of mRNA for components involved in the PI3K/Akt/mTOR pathway. Notes: The levels of PTEN, PI3K, Akt, and mTOR mRNA expression in pancreatic tumor tissue ( A ) and spontaneous liver metastases ( B ) were examined by RT-PCR. The mean levels of PTEN, PI3K, Akt, and mTOR mRNA expression were shown in representative images (left) and quantitative analysis demonstrating the average of three separate experiments (right). Data represent the mean ± SD (n=5). ** P
    Figure Legend Snippet: Effect of anti-PD-L1 antibody on expression of mRNA for components involved in the PI3K/Akt/mTOR pathway. Notes: The levels of PTEN, PI3K, Akt, and mTOR mRNA expression in pancreatic tumor tissue ( A ) and spontaneous liver metastases ( B ) were examined by RT-PCR. The mean levels of PTEN, PI3K, Akt, and mTOR mRNA expression were shown in representative images (left) and quantitative analysis demonstrating the average of three separate experiments (right). Data represent the mean ± SD (n=5). ** P

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction

    Effect of anti-PD-L1 antibody on proteins involved in the PI3K/Akt/mTOR pathway. Notes: The levels of PTEN, PI3K, p-PI3K (Tyr 458 ), Akt, p-Akt (Ser 473 ), mTOR, and p-mTOR (Ser 2448 ) protein expression in pancreatic tumor tissue ( A ) and spontaneous liver metastases ( B ) were detected by Western blotting. The mean levels of PTEN, PI3K, p-PI3K (Tyr 458 ), Akt, p-Akt (Ser 473 ), mTOR, and p-mTOR (Ser 2448 ) protein expression were shown in representative images (left) and quantitative analysis demonstrating the average of three separate experiments (right). Data represent the mean ± standard deviation (n=5). ** P
    Figure Legend Snippet: Effect of anti-PD-L1 antibody on proteins involved in the PI3K/Akt/mTOR pathway. Notes: The levels of PTEN, PI3K, p-PI3K (Tyr 458 ), Akt, p-Akt (Ser 473 ), mTOR, and p-mTOR (Ser 2448 ) protein expression in pancreatic tumor tissue ( A ) and spontaneous liver metastases ( B ) were detected by Western blotting. The mean levels of PTEN, PI3K, p-PI3K (Tyr 458 ), Akt, p-Akt (Ser 473 ), mTOR, and p-mTOR (Ser 2448 ) protein expression were shown in representative images (left) and quantitative analysis demonstrating the average of three separate experiments (right). Data represent the mean ± standard deviation (n=5). ** P

    Techniques Used: Expressing, Western Blot, Standard Deviation

    31) Product Images from "NQO1 potentiates apoptosis evasion and upregulates XIAP via inhibiting proteasome-mediated degradation SIRT6 in hepatocellular carcinoma"

    Article Title: NQO1 potentiates apoptosis evasion and upregulates XIAP via inhibiting proteasome-mediated degradation SIRT6 in hepatocellular carcinoma

    Journal: Cell Communication and Signaling : CCS

    doi: 10.1186/s12964-019-0491-7

    Schematic model of how NQO1 inhibits HCC apoptosis. The working model for oncogenic role of NQO1 in HCC. In HCC cells where NQO1 expression is high, NQO1 interacts physically with SIRT6, stabilizes the protein and prevents it from ubiquitin-dependent proteasomal degradation. Consequently, SIRT6 deacetylated AKT to promote its phosphorylation and activation, thus leading to increasing XIAP phosphorylation and protein stability
    Figure Legend Snippet: Schematic model of how NQO1 inhibits HCC apoptosis. The working model for oncogenic role of NQO1 in HCC. In HCC cells where NQO1 expression is high, NQO1 interacts physically with SIRT6, stabilizes the protein and prevents it from ubiquitin-dependent proteasomal degradation. Consequently, SIRT6 deacetylated AKT to promote its phosphorylation and activation, thus leading to increasing XIAP phosphorylation and protein stability

    Techniques Used: Expressing, Activation Assay

    32) Product Images from "D-Chiro-Inositol Treatment Affects Oocyte and Embryo Quality and Improves Glucose Intolerance in Both Aged Mice and Mouse Models of Polycystic Ovarian Syndrome"

    Article Title: D-Chiro-Inositol Treatment Affects Oocyte and Embryo Quality and Improves Glucose Intolerance in Both Aged Mice and Mouse Models of Polycystic Ovarian Syndrome

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms21176049

    Influence of DCI treatment on the phosphorylation state of the liver metabolic sensors AKT and mTOR, and on that of the glycogen synthesis-related enzymes GSK3β and GS in the aged and PCOS mouse models. ( A ) Normalized phosphorylation state measured as the ratio between phosphorylated/non-phosphorylated forms of the proteins AKT (protein kinase B), GSK3β (glycogen synthase kinase 3-beta), GS (glycogen synthase) and mTOR (mammalian target of rapamycin) in the liver of adult aged animals, or adult animals born from mothers treated with dihydrotestosterone (DHT) or testosterone propionate (TP). Effects of 2 months of supplementation with DCI (20 mg/kg) on the phosphorylation state of the same proteins in ( B ) aged mice, ( C ) DHT-treated mice, and ( D ) TP-treated mice. Values are reported as the mean ± s.e.m. Significant differences between the control and experimental groups (* p
    Figure Legend Snippet: Influence of DCI treatment on the phosphorylation state of the liver metabolic sensors AKT and mTOR, and on that of the glycogen synthesis-related enzymes GSK3β and GS in the aged and PCOS mouse models. ( A ) Normalized phosphorylation state measured as the ratio between phosphorylated/non-phosphorylated forms of the proteins AKT (protein kinase B), GSK3β (glycogen synthase kinase 3-beta), GS (glycogen synthase) and mTOR (mammalian target of rapamycin) in the liver of adult aged animals, or adult animals born from mothers treated with dihydrotestosterone (DHT) or testosterone propionate (TP). Effects of 2 months of supplementation with DCI (20 mg/kg) on the phosphorylation state of the same proteins in ( B ) aged mice, ( C ) DHT-treated mice, and ( D ) TP-treated mice. Values are reported as the mean ± s.e.m. Significant differences between the control and experimental groups (* p

    Techniques Used: Mouse Assay

    33) Product Images from "Rh-relaxin-2 attenuates degranulation of mast cells by inhibiting NF-κB through PI3K-AKT/TNFAIP3 pathway in an experimental germinal matrix hemorrhage rat model"

    Article Title: Rh-relaxin-2 attenuates degranulation of mast cells by inhibiting NF-κB through PI3K-AKT/TNFAIP3 pathway in an experimental germinal matrix hemorrhage rat model

    Journal: Journal of Neuroinflammation

    doi: 10.1186/s12974-020-01926-x

    Knockdown of RXFP1 ( a , c , l ) by specific siRNA significantly inhibited the expression of PI3K ( a , d ), phosphorylated Akt ( a , e ), and TNFAIP3 ( a , f ) on the first day after intracerebroventricular injections. However, the expression of phosphorylated NF-κB ( a , g ) and inflammatory factors chymase ( a , h ), tryptase ( a , i ), IL-6 ( a , j ), and TNF-α ( a , k ) increased on the first day after GMH. * P
    Figure Legend Snippet: Knockdown of RXFP1 ( a , c , l ) by specific siRNA significantly inhibited the expression of PI3K ( a , d ), phosphorylated Akt ( a , e ), and TNFAIP3 ( a , f ) on the first day after intracerebroventricular injections. However, the expression of phosphorylated NF-κB ( a , g ) and inflammatory factors chymase ( a , h ), tryptase ( a , i ), IL-6 ( a , j ), and TNF-α ( a , k ) increased on the first day after GMH. * P

    Techniques Used: Expressing

    LY294002 significantly decreased PI3K ( a , d , l ), phosphorylated Akt ( a , e ), and TNFAIP3 ( a , f ) expression, which was accompanied by the increase of phosphorylated NF-κB ( a , g ), chymase ( a , h ), tryptase ( a , i ), IL-6 ( a , j ), and TNF-α ( a , k ) on the first day after GMH. * P
    Figure Legend Snippet: LY294002 significantly decreased PI3K ( a , d , l ), phosphorylated Akt ( a , e ), and TNFAIP3 ( a , f ) expression, which was accompanied by the increase of phosphorylated NF-κB ( a , g ), chymase ( a , h ), tryptase ( a , i ), IL-6 ( a , j ), and TNF-α ( a , k ) on the first day after GMH. * P

    Techniques Used: Expressing

    34) Product Images from "Clusterin Is a Ligand for Apolipoprotein E Receptor 2 (ApoER2) and Very Low Density Lipoprotein Receptor (VLDLR) and Signals via the Reelin-signaling Pathway *"

    Article Title: Clusterin Is a Ligand for Apolipoprotein E Receptor 2 (ApoER2) and Very Low Density Lipoprotein Receptor (VLDLR) and Signals via the Reelin-signaling Pathway *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.529271

    Clusterin activates PI3K/Akt and cofilin. A , primary rat E16.5 WT neurons were incubated with mock-conditioned medium (MCM, lane 1 ), Reelin-conditioned medium ( RCM , lane 2 ), OptiMEM ( lane 3 ), or 2.5 n m clusterin ( lane 4 ) for 15 min. Total cell extracts
    Figure Legend Snippet: Clusterin activates PI3K/Akt and cofilin. A , primary rat E16.5 WT neurons were incubated with mock-conditioned medium (MCM, lane 1 ), Reelin-conditioned medium ( RCM , lane 2 ), OptiMEM ( lane 3 ), or 2.5 n m clusterin ( lane 4 ) for 15 min. Total cell extracts

    Techniques Used: Incubation

    35) Product Images from "Loss of mTOR repressors Tsc1 or Pten has divergent effects on excitatory and inhibitory synaptic transmission in single hippocampal neuron cultures"

    Article Title: Loss of mTOR repressors Tsc1 or Pten has divergent effects on excitatory and inhibitory synaptic transmission in single hippocampal neuron cultures

    Journal: Frontiers in Molecular Neuroscience

    doi: 10.3389/fnmol.2014.00001

    Loss of Pten or Tsc1 has opposite effects on GABAergic synaptic transmission in hippocampal GABAergic neurons. (A) Representative responses of voltage-clamped Pten-ko (red trace) and Tsc1-ko (blue traces) neurons and their controls (overlaid black traces) to a 2 ms depolarization to 0 mV from -70 mV. (B) Bar graph showing AP-evoked IPSC peak amplitudes (mean ± SEM) of Pten-ko (red bars) and Tsc1-ko (blue bars) neurons and their respective controls (black bars). (C) Representative traces showing the average of mIPSCs collected from one Pten-ko neuron (red trace), one Tsc1-ko neuron (blue trace) and their respective controls (overlaid black traces). (D) Bar graph showing mIPSC peak amplitudes (mean ± SEM) of Pten-ko (red bars) and Tsc1-ko (blue bars) neurons and their respective controls (black bars) (E) Representative traces showing control (black trace), Pten-ko (red trace), and Tsc1-ko (blue trace) miniature postsynaptic current activity from hippocampal GABAergic neurons. (F) Bar graph showing mIPSC frequencies (mean ± SEM) of Pten-ko (red bars) and Tsc1-ko (blue bars) neurons and their respective controls (black bars). (G) Representative images showing immunofluorescence from Map2 (green) and p-Akt S473 (blue) from control (left column), Pten-ko (middle column) and Tsc1-ko (right column) neurons. Red fluorescence in Pten- and Tsc1-ko neurons is from the Cre-RFP fusion protein. (H) Intensity values (mean ± SEM) for pAkt measured from Pten-ko (red bar) and Tsc1-ko (blue bar) relative to their respective controls (black dashed line). * p ≤ 0.05, * * p ≤ 0.01, *** p ≤ 0.001, n.s. = not significant.
    Figure Legend Snippet: Loss of Pten or Tsc1 has opposite effects on GABAergic synaptic transmission in hippocampal GABAergic neurons. (A) Representative responses of voltage-clamped Pten-ko (red trace) and Tsc1-ko (blue traces) neurons and their controls (overlaid black traces) to a 2 ms depolarization to 0 mV from -70 mV. (B) Bar graph showing AP-evoked IPSC peak amplitudes (mean ± SEM) of Pten-ko (red bars) and Tsc1-ko (blue bars) neurons and their respective controls (black bars). (C) Representative traces showing the average of mIPSCs collected from one Pten-ko neuron (red trace), one Tsc1-ko neuron (blue trace) and their respective controls (overlaid black traces). (D) Bar graph showing mIPSC peak amplitudes (mean ± SEM) of Pten-ko (red bars) and Tsc1-ko (blue bars) neurons and their respective controls (black bars) (E) Representative traces showing control (black trace), Pten-ko (red trace), and Tsc1-ko (blue trace) miniature postsynaptic current activity from hippocampal GABAergic neurons. (F) Bar graph showing mIPSC frequencies (mean ± SEM) of Pten-ko (red bars) and Tsc1-ko (blue bars) neurons and their respective controls (black bars). (G) Representative images showing immunofluorescence from Map2 (green) and p-Akt S473 (blue) from control (left column), Pten-ko (middle column) and Tsc1-ko (right column) neurons. Red fluorescence in Pten- and Tsc1-ko neurons is from the Cre-RFP fusion protein. (H) Intensity values (mean ± SEM) for pAkt measured from Pten-ko (red bar) and Tsc1-ko (blue bar) relative to their respective controls (black dashed line). * p ≤ 0.05, * * p ≤ 0.01, *** p ≤ 0.001, n.s. = not significant.

    Techniques Used: Transmission Assay, Mass Spectrometry, Activity Assay, Immunofluorescence, Fluorescence

    36) Product Images from "Phosphorylation of Akt and ERK1/2 Is Required for VEGF-A/VEGFR2-Induced Proliferation and Migration of Lymphatic Endothelium"

    Article Title: Phosphorylation of Akt and ERK1/2 Is Required for VEGF-A/VEGFR2-Induced Proliferation and Migration of Lymphatic Endothelium

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0028947

    VEGFR2, not VEGFR1, regulates VEGF-A-induced activation of PLC-γ, ERK1/2, and Akt in LECs. A : Diagram adapted from [43] depicting phosphorylation sites of the intracellular domain of VEGFR2. B,C : Lysates of primary human dermal LECs were made after stimulating LECs with recombinant human VEGF-A (100 ng/ml) for 2, 5, or 10 minutes. The activation of VEGFR2, PLC-γ, ERK1/2 and Akt was detected by Western blotting using phospho-specific antibodies. D : Lysates were generated of LECs stimulated with VEGF-A (100 ng/ml, 10 minutes) in the presence or absence of r84 (500 molar excess) or control IgG (500 molar excess). The activation of VEGFR2, PLCγ, ERK1/2 and Akt was detected by Western blotting. r84 suppressed phosphorylation of PLC-γ, ERK1/2, and Akt in LECs.
    Figure Legend Snippet: VEGFR2, not VEGFR1, regulates VEGF-A-induced activation of PLC-γ, ERK1/2, and Akt in LECs. A : Diagram adapted from [43] depicting phosphorylation sites of the intracellular domain of VEGFR2. B,C : Lysates of primary human dermal LECs were made after stimulating LECs with recombinant human VEGF-A (100 ng/ml) for 2, 5, or 10 minutes. The activation of VEGFR2, PLC-γ, ERK1/2 and Akt was detected by Western blotting using phospho-specific antibodies. D : Lysates were generated of LECs stimulated with VEGF-A (100 ng/ml, 10 minutes) in the presence or absence of r84 (500 molar excess) or control IgG (500 molar excess). The activation of VEGFR2, PLCγ, ERK1/2 and Akt was detected by Western blotting. r84 suppressed phosphorylation of PLC-γ, ERK1/2, and Akt in LECs.

    Techniques Used: Activation Assay, Planar Chromatography, Recombinant, Western Blot, Generated

    37) Product Images from "WAVE3-NFκB Interplay Is Essential for the Survival and Invasion of Cancer Cells"

    Article Title: WAVE3-NFκB Interplay Is Essential for the Survival and Invasion of Cancer Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0110627

    Down-regulation of WAVE3 sensitizes MDA-MB-231 cells to TNFα induced apoptosis through Akt signaling. Representative histograms using flow cytometry of control shRNA (ctrl-sh, green)- or sh-WAVE3-expressing (red) MDA-MB-231 cells after TNFα treatment stained by Annexin V for apoptosis (A) and by Propidium Iodide for cell death (B). (C) Representative confocal images of Ctrl-sh and sh-W3 MDA-MB-231 cells stained Annexin V (Green) and cleaved caspase3 (Red) before and after TNFα treatment (50 ng/μl for 15 min). The bright field images in the right panels indicate healthy cells. High resolution enlarged images are shown in the insets. (D E) Quantification of Annexin V staining levels (D) and Caspase 3 staining levels. (F) Western blot analysis with the indicated antibodies of cell lysates form the Ctrl-sh and sh-W3 cells after treatment with TNFα at the indicated times. The numbers below the p-AKT and the p-p38 panels indicate their respective fold change with respect to the untreated Ctrl-sh cells. All data are representative of 3 independent experiments, or are the mean (±SE; n = 3; *, p
    Figure Legend Snippet: Down-regulation of WAVE3 sensitizes MDA-MB-231 cells to TNFα induced apoptosis through Akt signaling. Representative histograms using flow cytometry of control shRNA (ctrl-sh, green)- or sh-WAVE3-expressing (red) MDA-MB-231 cells after TNFα treatment stained by Annexin V for apoptosis (A) and by Propidium Iodide for cell death (B). (C) Representative confocal images of Ctrl-sh and sh-W3 MDA-MB-231 cells stained Annexin V (Green) and cleaved caspase3 (Red) before and after TNFα treatment (50 ng/μl for 15 min). The bright field images in the right panels indicate healthy cells. High resolution enlarged images are shown in the insets. (D E) Quantification of Annexin V staining levels (D) and Caspase 3 staining levels. (F) Western blot analysis with the indicated antibodies of cell lysates form the Ctrl-sh and sh-W3 cells after treatment with TNFα at the indicated times. The numbers below the p-AKT and the p-p38 panels indicate their respective fold change with respect to the untreated Ctrl-sh cells. All data are representative of 3 independent experiments, or are the mean (±SE; n = 3; *, p

    Techniques Used: Multiple Displacement Amplification, Flow Cytometry, Cytometry, shRNA, Expressing, Staining, Western Blot

    38) Product Images from "Insulin receptor signaling regulates renal collecting duct and intercalated cell antibacterial defenses"

    Article Title: Insulin receptor signaling regulates renal collecting duct and intercalated cell antibacterial defenses

    Journal: The Journal of Clinical Investigation

    doi: 10.1172/JCI98595

    Insulin-mediated PI3K/AKT activation regulates AMP expression. ( A and B ) Lcn2 and RNase4 mRNA expression in mOMCD1, mIMCD3, and human renal epithelial cells treated with vehicle control (gray bars) or insulin (white bars) for 24 hours. AMP expression is derived from 3 independent experiments performed in triplicate ( n = 3). Columns represent mean and SEM. Asterisks denote significant P values for the indicated pairwise comparisons (Student’s t test). ( C ) Representative Western blots probed for pAKT (ser473), RNase4, and GAPDH from human renal epithelial cells treated with insulin with or without wortmannin (wort). ( D ) ELISA quantitated Lcn2 concentrations in renal epithelial cell culture media following insulin with or without wortmannin treatment ( n = 3). Columns represent mean and SEM. Asterisks indicate significant P values for the indicated pairwise comparison as determined by 1-way ANOVA with Tukey’s test. ( E ) Relative Lcn2 and Rnase4 mRNA expression in noninfected kidneys from wortmannin (striped bars) or vehicle-treated (white bars) C57BL/6J mice ( n = 6 mice/treatment). ( F ) One hour before UPEC challenge, female C57BL/6J mice were treated with intraperitoneal wortmannin (squares) or vehicle control (circles). At 6 HPI, urine was collected, bladders were harvested, and UPEC colonies were enumerated. The horizontal line indicates the geometric mean. ( E , F ) Asterisks denote significant P values for the pairwise comparisons (Mann-Whitney U test). ( G ) Representative Western blots confirm wortmannin suppression of renal AKT (ser473) phosphorylation. Each lane shows kidney pAKT activity from a separate mouse. * P
    Figure Legend Snippet: Insulin-mediated PI3K/AKT activation regulates AMP expression. ( A and B ) Lcn2 and RNase4 mRNA expression in mOMCD1, mIMCD3, and human renal epithelial cells treated with vehicle control (gray bars) or insulin (white bars) for 24 hours. AMP expression is derived from 3 independent experiments performed in triplicate ( n = 3). Columns represent mean and SEM. Asterisks denote significant P values for the indicated pairwise comparisons (Student’s t test). ( C ) Representative Western blots probed for pAKT (ser473), RNase4, and GAPDH from human renal epithelial cells treated with insulin with or without wortmannin (wort). ( D ) ELISA quantitated Lcn2 concentrations in renal epithelial cell culture media following insulin with or without wortmannin treatment ( n = 3). Columns represent mean and SEM. Asterisks indicate significant P values for the indicated pairwise comparison as determined by 1-way ANOVA with Tukey’s test. ( E ) Relative Lcn2 and Rnase4 mRNA expression in noninfected kidneys from wortmannin (striped bars) or vehicle-treated (white bars) C57BL/6J mice ( n = 6 mice/treatment). ( F ) One hour before UPEC challenge, female C57BL/6J mice were treated with intraperitoneal wortmannin (squares) or vehicle control (circles). At 6 HPI, urine was collected, bladders were harvested, and UPEC colonies were enumerated. The horizontal line indicates the geometric mean. ( E , F ) Asterisks denote significant P values for the pairwise comparisons (Mann-Whitney U test). ( G ) Representative Western blots confirm wortmannin suppression of renal AKT (ser473) phosphorylation. Each lane shows kidney pAKT activity from a separate mouse. * P

    Techniques Used: Activation Assay, Expressing, Derivative Assay, Western Blot, Enzyme-linked Immunosorbent Assay, Cell Culture, Mouse Assay, MANN-WHITNEY, Activity Assay

    39) Product Images from "PACAP and VIP Inhibit the Invasiveness of Glioblastoma Cells Exposed to Hypoxia through the Regulation of HIFs and EGFR Expression"

    Article Title: PACAP and VIP Inhibit the Invasiveness of Glioblastoma Cells Exposed to Hypoxia through the Regulation of HIFs and EGFR Expression

    Journal: Frontiers in Pharmacology

    doi: 10.3389/fphar.2016.00139

    Expression of HIF-1α, HIF-2α, and EGFR following inhibition of PI3K/Akt or MAPPK/Erk kinase signaling pathway. (A) Representative immunoblot of HIF-1α, HIF-2α, and EGFR expression on U87MG cells treated with 10 μM Wortmannin or with 50 μM PD98059 and grown normoxia or exposed to hypoxia. (B) Relative density of each band was quantified using ImageJ software. Each signal was normalized on correspondent β-tubulin signal. Data are expressed as mean ± SEM (** p
    Figure Legend Snippet: Expression of HIF-1α, HIF-2α, and EGFR following inhibition of PI3K/Akt or MAPPK/Erk kinase signaling pathway. (A) Representative immunoblot of HIF-1α, HIF-2α, and EGFR expression on U87MG cells treated with 10 μM Wortmannin or with 50 μM PD98059 and grown normoxia or exposed to hypoxia. (B) Relative density of each band was quantified using ImageJ software. Each signal was normalized on correspondent β-tubulin signal. Data are expressed as mean ± SEM (** p

    Techniques Used: Expressing, Inhibition, Software

    Phosphorylation of AKT and ERK1/2 in U87-MG cells under normoxia and hypoxia. (A) Representative immunoblots of Ser473-p Akt or p-Erk1/2 expression on U87MG cells treated with PACAP or VIP under normoxia or hypoxia. (B) The bar graphs show quantitative analysis of signals obtained by immunoblots resulting from three independent experiments. Relative band densities were quantified by using ImageJ software. Each signal of phosphorylated protein was normalized to total protein expression. Data are expressed as mean ± SEM (** p
    Figure Legend Snippet: Phosphorylation of AKT and ERK1/2 in U87-MG cells under normoxia and hypoxia. (A) Representative immunoblots of Ser473-p Akt or p-Erk1/2 expression on U87MG cells treated with PACAP or VIP under normoxia or hypoxia. (B) The bar graphs show quantitative analysis of signals obtained by immunoblots resulting from three independent experiments. Relative band densities were quantified by using ImageJ software. Each signal of phosphorylated protein was normalized to total protein expression. Data are expressed as mean ± SEM (** p

    Techniques Used: Western Blot, Expressing, Software

    40) Product Images from "MAPK/ERK1/2 and PI3-kinase signalling pathways are required for vitreous-induced lens fibre cell differentiation"

    Article Title: MAPK/ERK1/2 and PI3-kinase signalling pathways are required for vitreous-induced lens fibre cell differentiation

    Journal: Experimental eye research

    doi: 10.1016/j.exer.2008.08.023

    Maintenance of the fibre differentiation process is dependent on ERK1/2 and Akt activation. Representative micrographs of lens explants cultured with no growth factor (A, D) or 100 ng/ml of FGF (B, E) for 16 h, followed with treatment of inhibitor SU5402
    Figure Legend Snippet: Maintenance of the fibre differentiation process is dependent on ERK1/2 and Akt activation. Representative micrographs of lens explants cultured with no growth factor (A, D) or 100 ng/ml of FGF (B, E) for 16 h, followed with treatment of inhibitor SU5402

    Techniques Used: Activation Assay, Cell Culture

    FGF- and vitreous-induced phosphorylation of Akt and ERK1/2 during lens fibre differentiation. Immunofluorescent labelling of β-crystallin (D, E, F) or γ-crystallin (G, H, I) in lens explants cultured without growth factors (A, D, G),
    Figure Legend Snippet: FGF- and vitreous-induced phosphorylation of Akt and ERK1/2 during lens fibre differentiation. Immunofluorescent labelling of β-crystallin (D, E, F) or γ-crystallin (G, H, I) in lens explants cultured without growth factors (A, D, G),

    Techniques Used: Cell Culture

    (i) Representative western blots of explants cultured with no growth factors (control) or 50% vitreous, from 5 min up to 24 h, assayed for phosphorylated Akt (pAkt, upper panel), phosphorylated ERK1/2 (pERK1/2, middle panel) or total ERK1/2 (lower panel).
    Figure Legend Snippet: (i) Representative western blots of explants cultured with no growth factors (control) or 50% vitreous, from 5 min up to 24 h, assayed for phosphorylated Akt (pAkt, upper panel), phosphorylated ERK1/2 (pERK1/2, middle panel) or total ERK1/2 (lower panel).

    Techniques Used: Western Blot, Cell Culture

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    Western Blot:

    Article Title: Essential role for SphK1/S1P signaling to regulate hypoxia-inducible factor 2α expression and activity in cancer
    Article Snippet: .. Western-blot analysis and antibodies Rabbit anti-HIF-2α (Novus, Littleton, CO, USA), mouse anti-HIF-1α (BD, San Jose, CA, USA), rabbit anti-GLUT-1 (ThermoScientific, Villebon-sur-Yvette, France), mouse anti-cyclin D1, rabbit anti-p70S6K, rabbit anti-phospho-p70S6K (Thr389), rabbit anti-phospho-p70S6K (Thr421/Ser424), rabbit anti-mTOR, rabbit anti-phospho-mTOR (Ser2448), rabbit anti-4E-BP1, rabbit anti-phospho 4E-BP1 (Ser65), rabbit anti-Akt, rabbit anti-phospho-Akt (Ser473) (Cell Signaling Technology, Danvers, MA, USA), rabbit anti-Spns2 (Sigma), anti-tubulin (Santa Cruz Biotechnology, Santa Cruz, CA, USA), mouse anti-puromycin (Millipore, 12D10) were used as primary antibodies. .. Proteins were visualized by an ECL detection system (Perbio, Villebon-sur-Yvette, France) using anti-rabbit or anti-mouse horseradish peroxidase-conjugated IgG (Bio-Rad, Marnes-la-Coquette, France).

    Incubation:

    Article Title: Hydrogen Sulfide Prevents Formation of Reactive Oxygen Species through PI3K/Akt Signaling and Limits Ventilator-Induced Lung Injury
    Article Snippet: .. Membranes were incubated with antibodies against NADPH oxidases 1 and 4 (Nox1; Nox4; Santa Cruz Biotechnology Inc., Heidelberg, Germany), Nox2 (Becton Dickinson GmbH, Heidelberg, Germany), phosphorylated Akt, or Akt (Cell Signaling, Leiden, The Netherlands). .. Normalization in order to control equal protein loading was performed by stripping and reblotting of the membranes with glyceraldehyde-3-phosphate-dehydrogenase (GAPDH; Enzo Life Sciences GmbH, Lörrach, Germany).

    other:

    Article Title: Angiopoietin-1 protects myocardial endothelial cell function blunted by angiopoietin-2 and high glucose condition
    Article Snippet: The following primary antibodies were used: anti-phosphotyrosine (Upstate Co, NJ, USA), mouse anti-phospho-eNOS, mouse anti-eNOS (BD Co, CA, USA), rabbit anti-Ang-1 (Santa Cruz, CA, USA), rabbit anti-phospho-AKT, rabbit anti-Akt, mouse anti-cleaved caspase-3, mouse anti-Tie-2, and rabbit anti-β-actin (Cell Signaling, MA, USA).

    SDS Page:

    Article Title: Atorvastatin prevents Aβ oligomer-induced neurotoxicity in cultured rat hippocampal neurons by inhibiting Tau cleavage
    Article Snippet: .. Equal amounts of protein were then separated by SDS-PAGE, transferred onto nitrocellulose membranes, and probed with primary antibodies against the following proteins: mouse monoclonal anti-spectrin αII (Santa Cruz Biotechnology, Santa Cruz, CA, USA), rabbit monoclonal anti-vimentin (1:1000, Abcam, New Territories, HK, USA), mouse monoclonal anti-Tau (Tau-5, 1:500, Abcam, New Territories, HK, USA), rabbit polyclonal anti-p35 (C-19, 1:500, Santa Cruz Biotechnology, Santa Cruz, CA, USA), rabbit monoclonal anti-phospho-GSK3β (Ser9, 1:1000, Cell Signaling Technology, Beverly, MA, USA), rabbit monoclonal anti-phospho-Erk1/2 (Thr202/Tyr204, 1:1000, Cell Signaling Technology, Beverly, MA, USA), and rabbit monoclonal anti-phospho-Akt (Ser473, 1:1000, Cell Signaling Technology, Beverly, MA, USA). .. After being washed with PBS, membranes were incubated with horseradish peroxidase-conjugated anti-rabbit IgG secondary antibody (1:2000, Cell Signaling Technology, Beverly, MA, USA).

    Article Title: High Density Lipoprotein Stimulated Migration of Macrophages Depends on the Scavenger Receptor Class B, Type I, PDZK1 and Akt1 and Is Blocked by Sphingosine 1 Phosphate Receptor Antagonists
    Article Snippet: .. After boiling, the samples were subjected to SDS-PAGE followed by immunoblotting with rabbit anti-Akt, rabbit anti-phospho-Akt (Ser473) (Cell Signaling Technology, Danvers, MA, USA). .. HRP-conjugated donkey-anti-rabbit and donkey-anti-mouse antibodies (Jackson ImmunoResearch Labs Inc, West Grove PA, USA) were used as secondary antibodies and were detected using Western Lightning ECL reagent kit (PerkinElmer Canada, Woodbridge ON, Canada).

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    Cell Signaling Technology Inc rabbit anti human pan 4ebp1
    PRE, W3, and W6 mTORc1 signaling marker differences between LOW and HIGH responders. (A–D) Phosphorylated (p-) mTORc1 targets. There were no significant cluster effects or cluster × time interactions for said markers. p-mTOR and <t>p-4EBP1</t> demonstrated significant time effects. (E–H) Total (pan) mTOR, p70s6k, 4EBP1, and AMPKα. Again, there were no significant cluster effects or cluster × time interactions for said markers, although there were significant time effects for pan mTOR, pan p70s6k, and pan AMPKα. Values presented in line graphs are mean (standard deviation) values. (I) Representative Western blot images for a low and high responder.
    Rabbit Anti Human Pan 4ebp1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit anti akt
    Loss of FlnB induces Cdk1 activity changes through β1 <t>integrin-Pi3k/Akt</t> pathway. (A, B) Immunostaining of total and phospho-β1 integrin (pS785)(postnatal day 1 radius). Phospho-β1 integrin (pS785) levels are down-regulated in FlnB knockout chondrocytes (arrows) (B). (C, E) Western blotting results show that Pi3k(p85 subunit) and phospho-Akt(pS473), as well as phospho-Cdk1(pY15) are down-regulated in FlnB knockdown (Bsh) ATDC5 cells. Total Akt levels are not changed. Total β1 integrin levels are up-regulated but phospho-β1 integrsin (pS785) are down-regulated. Results are quantified in (E). (D, F) β1 integrin activation (Itgb1) in ATDC5 cells regulates Pi3k/Akt and Cdk1 activation. Pretreatment of ATCD5 cells with fibronectin and laminin I but not collagen (col) induces up-regulation of total β1 integrin levels but down-regulation of phospho-β1 integrin (pS785) levels. Pi3k, pAkt and Cdk1(pY15) levels are down-regulated by fibronectin and laminin I. Total Akt levels are not changed. ATDC5 cells are incubated in the presence of extracellular matrix molecules: fibronectin, laminin, and collagen, which serve as ligands for the β1 integrin receptor, and activation of the downstream pathways are assessed by Western blot analyses. Con = control, Col = collagen, Fib = fibronectin, and Lam = laminin. (G) Pretreatment of ATDC5 cells with Akt inhibitor VIII decreases Akt(pS473), Cdk1(pY15) and Sox9 levels, but increases protein levels of hypertrophic markers such as Runx2 and Col0a1. * = p
    Rabbit Anti Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 586 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit anti phosphorylated ser505 akt
    Dgk regulates dILP secretion and insulin signaling pathway activity. ( A ) Knockdown of Dgk using dIlp2-Gal4 shows elevated TAG, glucose, and glycogen phenotypes. ( B ) dIlp2-Gal4 -driven overexpression of kinase-dead Dgk but not wild-type Dgk also decreases glucose and glycogen levels. These phenotypes in ( A–B ) are similar to those seen using fru-Gal4 . ( C ) fru > Dgk RNAi increases dILP2 and dILP5 levels in the hemolymph. ( D ) Overexpression of either Dgk.V5 or Dgk G509D .V5 using fru-Gal4 does not affect hemolymph dILP2 or dILP5 levels. ( A–D ) Data is represented as percent or fold-change relative to a Gal4/+ control ± SD, n = 5. Assays were performed three times but results from only one representative assay are shown. ( E–F ) Knockdown or overexpression of Dgk with fru-Gal4 doesn't affect dIlp2 or dIlp5 transcript levels. Overexpression of Dgk G509D .V5 increases dIlp3 levels. ( G ) fru-Gal4 -driven Dgk RNAi or overexpression of Dgk G509D .V5 result in lowered insulin pathway activity as measured by <t>p-Ser505</t> <t>Akt/total</t> Akt levels. fru > Dgk . V5 did not affect pAkt/Akt levels. Quantification is from 3 biological replicates and is normalized to a fru-Gal4/+ control ±SD. Asterisks denote p-values based on student's t-test: *p
    Rabbit Anti Phosphorylated Ser505 Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit anti phospho akt ser473
    HDL stimulated macrophage migration involves Rho kinase and <t>PI3K-Akt</t> 1 signaling. A. RAW 264.7 cells were cultured in media containing 3% NCLPDS for 18 hrs. Cells were pre-incubated with 10 µM of either the Rho Kinase inhibitor, Y-27632, or the PI3K inhibitor LY294002, or with DMSO vehicle for 30 min and then the migration in response to HDL (100 µg protein/ml), FTY720 (2 ng/ml) or MCP-1 (100 ng/ml) was measured in the continued presence or absence of the indicated inhibitors. B. RAW 264.7 cells were serum starved for 18 hrs, washed and treated with or without HDL (100 µg protein/ml) for 10, 30 or 60 min. Equal amounts of proteins were analyzed by SDS-PAGE and immunoblotting for either <t>phospho-Ser473-</t> or total-Akt. C. MPM's were harvested from 6 independent WT, Akt1 KO, Akt2 KO or Akt3 KO mice. Migration in response to no stimulus, HDL (100 µg protein/ml), FTY720 (2 ng/ml) or MCP-1 (100 ng/ml) was measured. Data from A and C are means ± standard deviations of 6 replicates done over two independent experiments. Values identified with different letters are statistically significantly different (P
    Rabbit Anti Phospho Akt Ser473, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 76 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    PRE, W3, and W6 mTORc1 signaling marker differences between LOW and HIGH responders. (A–D) Phosphorylated (p-) mTORc1 targets. There were no significant cluster effects or cluster × time interactions for said markers. p-mTOR and p-4EBP1 demonstrated significant time effects. (E–H) Total (pan) mTOR, p70s6k, 4EBP1, and AMPKα. Again, there were no significant cluster effects or cluster × time interactions for said markers, although there were significant time effects for pan mTOR, pan p70s6k, and pan AMPKα. Values presented in line graphs are mean (standard deviation) values. (I) Representative Western blot images for a low and high responder.

    Journal: Frontiers in Physiology

    Article Title: Pre-training Skeletal Muscle Fiber Size and Predominant Fiber Type Best Predict Hypertrophic Responses to 6 Weeks of Resistance Training in Previously Trained Young Men

    doi: 10.3389/fphys.2019.00297

    Figure Lengend Snippet: PRE, W3, and W6 mTORc1 signaling marker differences between LOW and HIGH responders. (A–D) Phosphorylated (p-) mTORc1 targets. There were no significant cluster effects or cluster × time interactions for said markers. p-mTOR and p-4EBP1 demonstrated significant time effects. (E–H) Total (pan) mTOR, p70s6k, 4EBP1, and AMPKα. Again, there were no significant cluster effects or cluster × time interactions for said markers, although there were significant time effects for pan mTOR, pan p70s6k, and pan AMPKα. Values presented in line graphs are mean (standard deviation) values. (I) Representative Western blot images for a low and high responder.

    Article Snippet: Rabbit anti-human phospho-p70s6k (Thr389) (1:1,000; catalog #: 9234; Cell Signaling), rabbit anti-human pan p70s6k (1:1,000; catalog #: 2708; Cell Signaling), rabbit anti-human phospho-4EBP1 (Thr37/46) (1:1,000; catalog #: 2855; Cell Signaling), rabbit anti-human pan 4EBP1 (1:1,000; catalog #: 9644; Cell Signaling), rabbit anti-human phospho-mTOR (Ser2448) (1:1,000; catalog #: 2971; Cell Signaling), rabbit anti-human pan mTOR (1:1,000; catalog #: 2972; Cell Signaling), rabbit anti-human phospho-AMPKα (Thr172) (1:1,000; catalog #: 2535; Cell Signaling), rabbit anti-human pan AMPKα (1:1,000; catalog #: 2532; Cell Signaling), rabbit anti-human androgen receptor (1:1,000; catalog #: 5153; Cell Signaling) and rabbit anti-human ubiquitin (1:1,000; catalog #: 3933; Cell Signaling) were incubated with membranes overnight at 4°C in TBST with 5% bovine serum albumin (BSA).

    Techniques: Marker, Standard Deviation, Western Blot

    Loss of FlnB induces Cdk1 activity changes through β1 integrin-Pi3k/Akt pathway. (A, B) Immunostaining of total and phospho-β1 integrin (pS785)(postnatal day 1 radius). Phospho-β1 integrin (pS785) levels are down-regulated in FlnB knockout chondrocytes (arrows) (B). (C, E) Western blotting results show that Pi3k(p85 subunit) and phospho-Akt(pS473), as well as phospho-Cdk1(pY15) are down-regulated in FlnB knockdown (Bsh) ATDC5 cells. Total Akt levels are not changed. Total β1 integrin levels are up-regulated but phospho-β1 integrsin (pS785) are down-regulated. Results are quantified in (E). (D, F) β1 integrin activation (Itgb1) in ATDC5 cells regulates Pi3k/Akt and Cdk1 activation. Pretreatment of ATCD5 cells with fibronectin and laminin I but not collagen (col) induces up-regulation of total β1 integrin levels but down-regulation of phospho-β1 integrin (pS785) levels. Pi3k, pAkt and Cdk1(pY15) levels are down-regulated by fibronectin and laminin I. Total Akt levels are not changed. ATDC5 cells are incubated in the presence of extracellular matrix molecules: fibronectin, laminin, and collagen, which serve as ligands for the β1 integrin receptor, and activation of the downstream pathways are assessed by Western blot analyses. Con = control, Col = collagen, Fib = fibronectin, and Lam = laminin. (G) Pretreatment of ATDC5 cells with Akt inhibitor VIII decreases Akt(pS473), Cdk1(pY15) and Sox9 levels, but increases protein levels of hypertrophic markers such as Runx2 and Col0a1. * = p

    Journal: PLoS ONE

    Article Title: Filamin B Regulates Chondrocyte Proliferation and Differentiation through Cdk1 Signaling

    doi: 10.1371/journal.pone.0089352

    Figure Lengend Snippet: Loss of FlnB induces Cdk1 activity changes through β1 integrin-Pi3k/Akt pathway. (A, B) Immunostaining of total and phospho-β1 integrin (pS785)(postnatal day 1 radius). Phospho-β1 integrin (pS785) levels are down-regulated in FlnB knockout chondrocytes (arrows) (B). (C, E) Western blotting results show that Pi3k(p85 subunit) and phospho-Akt(pS473), as well as phospho-Cdk1(pY15) are down-regulated in FlnB knockdown (Bsh) ATDC5 cells. Total Akt levels are not changed. Total β1 integrin levels are up-regulated but phospho-β1 integrsin (pS785) are down-regulated. Results are quantified in (E). (D, F) β1 integrin activation (Itgb1) in ATDC5 cells regulates Pi3k/Akt and Cdk1 activation. Pretreatment of ATCD5 cells with fibronectin and laminin I but not collagen (col) induces up-regulation of total β1 integrin levels but down-regulation of phospho-β1 integrin (pS785) levels. Pi3k, pAkt and Cdk1(pY15) levels are down-regulated by fibronectin and laminin I. Total Akt levels are not changed. ATDC5 cells are incubated in the presence of extracellular matrix molecules: fibronectin, laminin, and collagen, which serve as ligands for the β1 integrin receptor, and activation of the downstream pathways are assessed by Western blot analyses. Con = control, Col = collagen, Fib = fibronectin, and Lam = laminin. (G) Pretreatment of ATDC5 cells with Akt inhibitor VIII decreases Akt(pS473), Cdk1(pY15) and Sox9 levels, but increases protein levels of hypertrophic markers such as Runx2 and Col0a1. * = p

    Article Snippet: The primary antibodies (for immunostaining and some also for western blotting) were: rabbit anti-FlnA monoclonal antibody (1∶300, Cat.# 2242, Epitomics, Burlingame, CA, USA); rabbit anti-FlnB polyclonal antibody (Gifted by Dr. Kao, CWRU); mouse anti-Col2a1 (Cat.# Ab3092, ABCAM, USA); rabbit anti-Col10a1 (kindly gifted by Dr. Horton and Dr. Lunstrum, Shriners Hospital for Children, Portland, OR, USA; ); rabbit anti-Pthr1 (Cat.# Ab75150, ABCAM, USA);rabbit anti-Ihh (Cat.# sc-13088, Santa Cruz); rabbit anti-Runx2 (Cat.# sc-10758, Santa Cruz); rabbit anti-Sox9 pab (1∶300, AB5535, Millipore); rabbit anti-Sox9 pab (O9-1, gift of Professor Dr. Michael Wegner, Institute of Biochemistry, Friedrich-Alexander-University, Erlangen-Nurnberg, Germany); rat anti-BrdU (1∶150, Cat.# MCA2060, AbD Serotec, Raleigh, NC, USA); rabbit anti-Ki-67 mab (1∶200, Cat.# 4203, Epitomics); rabbit anti-PH3 pab (1∶250, Cat:# 06-570, Millipore, Billerica, MA, USA); mouse and rabbit anti-Wee1 (1∶50, Cat.# sc-5285 and sc-325, Santa Cruz); rabbit anti-Pkmyt1 (1∶100, Cat.# 3303, Epitomics); anti-pan 14-3-3 (Santa Cruz, sc-629); mouse and rabbit anti-cyclin B1 (1∶100, Cat.# sc-245 and sc-752, Santa Cruz); mouse anti-Cdc20 (1∶100, Cat.# sc-13162, Santa Cruz); mouse and rabbit anti-cdc25c (1∶100, Cat.# sc-55513 and sc-327, Santa Cruz); rabbit-anti-Cdk1 (Cat.# PC25,Calbiochem, San Diego, CA, USA); mouse anti-Cdk1(pY15) (Cat.# BD612306, BD, Franklin Lakes, NJ USA); rabbit anti-Pi3k (p85 subunit alpha, Cat#: 1675, Epitomics); rabbit anti-Akt (phospho-S473, Cat# 4060, Cell Signaling); rabbit anti-Erk1/2 (phospho-T202/Y204, Cat.# 4370, Cell Signaling); rat anti-β1 integrin (Cat.# mab1997, Millipore); rabbit anti- β1 integrin(pS785) (Cat.# OPA1-03177, Affinity BioReagents).

    Techniques: Activity Assay, Immunostaining, Knock-Out, Western Blot, Activation Assay, Incubation, Laser Capture Microdissection

    Dgk regulates dILP secretion and insulin signaling pathway activity. ( A ) Knockdown of Dgk using dIlp2-Gal4 shows elevated TAG, glucose, and glycogen phenotypes. ( B ) dIlp2-Gal4 -driven overexpression of kinase-dead Dgk but not wild-type Dgk also decreases glucose and glycogen levels. These phenotypes in ( A–B ) are similar to those seen using fru-Gal4 . ( C ) fru > Dgk RNAi increases dILP2 and dILP5 levels in the hemolymph. ( D ) Overexpression of either Dgk.V5 or Dgk G509D .V5 using fru-Gal4 does not affect hemolymph dILP2 or dILP5 levels. ( A–D ) Data is represented as percent or fold-change relative to a Gal4/+ control ± SD, n = 5. Assays were performed three times but results from only one representative assay are shown. ( E–F ) Knockdown or overexpression of Dgk with fru-Gal4 doesn't affect dIlp2 or dIlp5 transcript levels. Overexpression of Dgk G509D .V5 increases dIlp3 levels. ( G ) fru-Gal4 -driven Dgk RNAi or overexpression of Dgk G509D .V5 result in lowered insulin pathway activity as measured by p-Ser505 Akt/total Akt levels. fru > Dgk . V5 did not affect pAkt/Akt levels. Quantification is from 3 biological replicates and is normalized to a fru-Gal4/+ control ±SD. Asterisks denote p-values based on student's t-test: *p

    Journal: Molecular Metabolism

    Article Title: An in vivo screen for neuronal genes involved in obesity identifies Diacylglycerol kinase as a regulator of insulin secretion

    doi: 10.1016/j.molmet.2018.10.006

    Figure Lengend Snippet: Dgk regulates dILP secretion and insulin signaling pathway activity. ( A ) Knockdown of Dgk using dIlp2-Gal4 shows elevated TAG, glucose, and glycogen phenotypes. ( B ) dIlp2-Gal4 -driven overexpression of kinase-dead Dgk but not wild-type Dgk also decreases glucose and glycogen levels. These phenotypes in ( A–B ) are similar to those seen using fru-Gal4 . ( C ) fru > Dgk RNAi increases dILP2 and dILP5 levels in the hemolymph. ( D ) Overexpression of either Dgk.V5 or Dgk G509D .V5 using fru-Gal4 does not affect hemolymph dILP2 or dILP5 levels. ( A–D ) Data is represented as percent or fold-change relative to a Gal4/+ control ± SD, n = 5. Assays were performed three times but results from only one representative assay are shown. ( E–F ) Knockdown or overexpression of Dgk with fru-Gal4 doesn't affect dIlp2 or dIlp5 transcript levels. Overexpression of Dgk G509D .V5 increases dIlp3 levels. ( G ) fru-Gal4 -driven Dgk RNAi or overexpression of Dgk G509D .V5 result in lowered insulin pathway activity as measured by p-Ser505 Akt/total Akt levels. fru > Dgk . V5 did not affect pAkt/Akt levels. Quantification is from 3 biological replicates and is normalized to a fru-Gal4/+ control ±SD. Asterisks denote p-values based on student's t-test: *p

    Article Snippet: Primary antibodies used: mouse anti-V5 (1:2000, Invitrogen), rabbit anti-Akt (1:500, Cell Signalling Technology), rabbit anti-phosphorylated Ser505 Akt (1:1000, Cell Signalling Technology) and mouse anti-actin (1:4000, Abcam).

    Techniques: Activity Assay, Over Expression

    HDL stimulated macrophage migration involves Rho kinase and PI3K-Akt 1 signaling. A. RAW 264.7 cells were cultured in media containing 3% NCLPDS for 18 hrs. Cells were pre-incubated with 10 µM of either the Rho Kinase inhibitor, Y-27632, or the PI3K inhibitor LY294002, or with DMSO vehicle for 30 min and then the migration in response to HDL (100 µg protein/ml), FTY720 (2 ng/ml) or MCP-1 (100 ng/ml) was measured in the continued presence or absence of the indicated inhibitors. B. RAW 264.7 cells were serum starved for 18 hrs, washed and treated with or without HDL (100 µg protein/ml) for 10, 30 or 60 min. Equal amounts of proteins were analyzed by SDS-PAGE and immunoblotting for either phospho-Ser473- or total-Akt. C. MPM's were harvested from 6 independent WT, Akt1 KO, Akt2 KO or Akt3 KO mice. Migration in response to no stimulus, HDL (100 µg protein/ml), FTY720 (2 ng/ml) or MCP-1 (100 ng/ml) was measured. Data from A and C are means ± standard deviations of 6 replicates done over two independent experiments. Values identified with different letters are statistically significantly different (P

    Journal: PLoS ONE

    Article Title: High Density Lipoprotein Stimulated Migration of Macrophages Depends on the Scavenger Receptor Class B, Type I, PDZK1 and Akt1 and Is Blocked by Sphingosine 1 Phosphate Receptor Antagonists

    doi: 10.1371/journal.pone.0106487

    Figure Lengend Snippet: HDL stimulated macrophage migration involves Rho kinase and PI3K-Akt 1 signaling. A. RAW 264.7 cells were cultured in media containing 3% NCLPDS for 18 hrs. Cells were pre-incubated with 10 µM of either the Rho Kinase inhibitor, Y-27632, or the PI3K inhibitor LY294002, or with DMSO vehicle for 30 min and then the migration in response to HDL (100 µg protein/ml), FTY720 (2 ng/ml) or MCP-1 (100 ng/ml) was measured in the continued presence or absence of the indicated inhibitors. B. RAW 264.7 cells were serum starved for 18 hrs, washed and treated with or without HDL (100 µg protein/ml) for 10, 30 or 60 min. Equal amounts of proteins were analyzed by SDS-PAGE and immunoblotting for either phospho-Ser473- or total-Akt. C. MPM's were harvested from 6 independent WT, Akt1 KO, Akt2 KO or Akt3 KO mice. Migration in response to no stimulus, HDL (100 µg protein/ml), FTY720 (2 ng/ml) or MCP-1 (100 ng/ml) was measured. Data from A and C are means ± standard deviations of 6 replicates done over two independent experiments. Values identified with different letters are statistically significantly different (P

    Article Snippet: After boiling, the samples were subjected to SDS-PAGE followed by immunoblotting with rabbit anti-Akt, rabbit anti-phospho-Akt (Ser473) (Cell Signaling Technology, Danvers, MA, USA).

    Techniques: Migration, Cell Culture, Incubation, SDS Page, Mouse Assay