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gapdh-glyceraldehyde-3-phosphate-dehydrogenase

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Impaired in vitro adipogenic differentiation parallels elevated HDAC9 expre...
Published: 13 December 2013
Figure 2 Impaired in vitro adipogenic differentiation parallels elevated HDAC9 expression. HDAC9 mRNA (A) and protein (B) expression were quantified by qPCR and Western blot analyses, respectively, on the indicated days of differentiation. Values represent percentage of change from preadipocytes (0 day) and are expressed as mean ± SEM of three different experiments. C: Western blot images were analyzed utilizing ImageJ software and expressed as percentage of 0 day levels in each condition after normalization to corresponding glyceraldehyde-3-phosphate dehydrogenase values. *P < 0.05. CD, chow diet; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. Figure 2. Impaired in vitro adipogenic differentiation parallels elevated HDAC9 expression. HDAC9 mRNA (A) and protein (B) expression were quantified by qPCR and Western blot analyses, respectively, on the indicated days of differentiation. Values represent percentage of change from preadipocytes (0 day) and are expressed as mean ± SEM of three different experiments. C: Western blot images were analyzed utilizing ImageJ software and expressed as percentage of 0 day levels in each condition after normalization to corresponding glyceraldehyde-3-phosphate dehydrogenase values. *P < 0.05. CD, chow diet; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. More
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Exendin-4 actions on human pancreatic duct cells. <em>A</em> and ...
Published: 13 April 2012
FIG. 7. Exendin-4 actions on human pancreatic duct cells. A and B: Time-course experiments of CREB (A) and ERK1/2 (B) phosphorylation in HPDE cells treated with exendin-4 (10 nmol/L) for 0–30 min as indicated. GAPDH, glyceraldehyde-3-phosphate dehydrogenase. Representative examples of Western blot experiments are shown in the top panels and the corresponding analysis in the bottom panels. C and D: Effect of long-term (0–9 h) stimulation on cyclin D1 (C) and cyclin A (D) protein levels. Data are expressed as the mean ± SD density ratio of total CREB, ERK1/2 (A and B), as well as glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (C and D) from 3 to 5 independent experiments. *P < 0.05; **P < 0.01; ***P < 0.001 vs. untreated control value. FIG. 7. Exendin-4 actions on human pancreatic duct cells. A and B: Time-course experiments of CREB (A) and ERK1/2 (B) phosphorylation in HPDE cells treated with exendin-4 (10 nmol/L) for 0–30 min as indicated. GAPDH, glyceraldehyde-3-phosphate dehydrogenase. Representative examples of Western blot experiments are shown in the top panels and the corresponding analysis in the bottom panels. C and D: Effect of long-term (0–9 h) stimulation on cyclin D1 (C) and cyclin A (D) protein levels. Data are expressed as the mean ± SD density ratio of total CREB, ERK1/2 (A and B), as well as glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (C and D) from 3 to 5 independent experiments. *P < 0.05; **P < 0.01; ***P < 0.001 vs. untreated control value. More
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Insulin-induced phosphorylation of Akt is prevented by delivery of anti-ins...
Published: 18 March 2010
FIG. 1. Insulin-induced phosphorylation of Akt is prevented by delivery of anti-insulin affibodies to differentiated adipocytes in vitro (A) and into the ventromedial hypothalamus in vivo during systemic insulin infusion. Relative change in Akt phosphorylation was normalized to β-actin (B). GAPDH, glyceraldehyde-3-phosphate dehydrogenase. FIG. 1. Insulin-induced phosphorylation of Akt is prevented by delivery of anti-insulin affibodies to differentiated adipocytes in vitro (A) and into the ventromedial hypothalamus in vivo during systemic insulin infusion. Relative change in Akt phosphorylation was normalized to β-actin (B). GAPDH, glyceraldehyde-3-phosphate dehydrogenase. More
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Browning effect of r-irisin on rat primary adipocytes. Primary rat adipocyt...
Published: 16 January 2014
Figure 3 Browning effect of r-irisin on rat primary adipocytes. Primary rat adipocytes were treated with r-irisin at indicated concentrations for 6 h. A: The expression levels of UCP-1 and PGC-1α genes were measured by RT-qPCR. B: UCP-1 protein expression was measured by Western blotting and quantified by densitometry. GAPDH, glyceraldehyde-3-phosphate dehydrogenase. *P < 0.05; **P < 0.01 vs. untreated. Figure 3. Browning effect of r-irisin on rat primary adipocytes. Primary rat adipocytes were treated with r-irisin at indicated concentrations for 6 h. A: The expression levels of UCP-1 and PGC-1α genes were measured by RT-qPCR. B: UCP-1 protein expression was measured by Western blotting and quantified by densitometry. GAPDH, glyceraldehyde-3-phosphate dehydrogenase. *P < 0.05; **P < 0.01 vs. untreated. More
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The expressions of Ang-1, CSE, and VEGF were decreased in human skin tissue...
Published: 12 April 2014
Figure 8 The expressions of Ang-1, CSE, and VEGF were decreased in human skin tissue of diabetic foot ulcers. A: Representative protein bands of Ang-1, CSE, and VEGF of skin tissue. B: The expression of Ang-1, CSE, and VEGF were lower in the foot ulcer skin tissue of diabetic patients than in nondiabetic controls (n = 7–8 in each group). **P < 0.05 vs. control. GAPDH, glyceraldehyde-3-phosphate dehydrogenase. Figure 8. The expressions of Ang-1, CSE, and VEGF were decreased in human skin tissue of diabetic foot ulcers. A: Representative protein bands of Ang-1, CSE, and VEGF of skin tissue. B: The expression of Ang-1, CSE, and VEGF were lower in the foot ulcer skin tissue of diabetic patients than in nondiabetic controls (n = 7–8 in each group). **P < 0.05 vs. control. GAPDH, glyceraldehyde-3-phosphate dehydrogenase. More
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Mechanism of hyperglycemia-induced Ang-2 regulation. <em>A</em>: Un...
Published: 01 January 2011
FIG. 4. Mechanism of hyperglycemia-induced Ang-2 regulation. A: Under physiological (normoglycemic) conditions, a transcriptional complex (involving the transcriptional corepressor mSin3A) represses Ang-2 transcription by binding to a glucose-sensitive GC box. B: Transcriptional activation of Ang-2 through methylglyoxal (AGE)-induced and hexosamine-propagated modification of SP-3 binding in favor of SP-1 binding. GAPDH, glyceraldehyde-3-phosphate dehydrogenase; UDP, uridine-5-diphosphate. (A high-quality color representation of this figure is available in the online issue.) FIG. 4. Mechanism of hyperglycemia-induced Ang-2 regulation. A: Under physiological (normoglycemic) conditions, a transcriptional complex (involving the transcriptional corepressor mSin3A) represses Ang-2 transcription by binding to a glucose-sensitive GC box. B: Transcriptional activation of Ang-2 through methylglyoxal (AGE)-induced and hexosamine-propagated modification of SP-3 binding in favor of SP-1 binding. GAPDH, glyceraldehyde-3-phosphate dehydrogenase; UDP, uridine-5-diphosphate. (A high-quality color representation of this figure is available in the online issue.) More
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Mitochondrial anaplerosis via sustained cellular pyruvate underpins the ben...
Published: 17 September 2013
FIG. 5. Mitochondrial anaplerosis via sustained cellular pyruvate underpins the beneficial metabolic effects of glucose withdrawal. A and B: Intracellular levels of G6P (Gluc 6-P) and glyceraldehyde 3-phosphate (glyceraldehyde 3-P) (A) and pyruvate (B) in L6 myotubes treated with 0.5 mmol/L PA (or vehicle control) for 16 h in the absence or presence of 5 mmol/L d-glucose as determined by LCMS analysis. CF: L6 myotubes were incubated with 0.5 mmol/L PA (or vehicle control) for 16 h in the absence or presence of 5 mmol/L d-glucose and different concentrations of PAC (C and D) or aminooxyacetic acid (AOA) (E and F) as shown. After treatments, resulting cell lysates were subjected to SDS-PAGE and immunoblotted for total and phosphorylated Ser473 Akt, IκBα, and GAPDH as indicated. All data are presented as mean ± SEM (n = 3). *P < 0.05 vs. cells treated with d-glucose alone (A). *P < 0.05 vs. PA-treated cells in the presence of 5 mmol/L d-glucose (CF). GAPDH, glyceraldehyde-3-phosphate dehydrogenase. FIG. 5. Mitochondrial anaplerosis via sustained cellular pyruvate underpins the beneficial metabolic effects of glucose withdrawal. A and B: Intracellular levels of G6P (Gluc 6-P) and glyceraldehyde 3-phosphate (glyceraldehyde 3-P) (A) and pyruvate (B) in L6 myotubes treated with 0.5 mmol/L PA (or vehicle control) for 16 h in the absence or presence of 5 mmol/L d-glucose as determined by LCMS analysis. C–F: L6 myotubes were incubated with 0.5 mmol/L PA (or vehicle control) for 16 h in the absence or presence of 5 mmol/L d-glucose and different concentrations of PAC (C and D) or aminooxyacetic acid (AOA) (E and F) as shown. After treatments, resulting cell lysates were subjected to SDS-PAGE and immunoblotted for total and phosphorylated Ser473 Akt, IκBα, and GAPDH as indicated. All data are presented as mean ± SEM (n = 3). *P < 0.05 vs. cells treated with d-glucose alone (A). *P < 0.05 vs. PA-treated cells in the presence of 5 mmol/L d-glucose (C–F). GAPDH, glyceraldehyde-3-phosphate dehydrogenase. More
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The effect of VASP on lipid metabolism in AML12 cells. <em>A</em>: ...
Published: 17 May 2013
FIG. 2. The effect of VASP on lipid metabolism in AML12 cells. A: AML12 cells were transduced with VASP (VASP-OE) or control (ctl) (empty) vector. B: RT-PCR analysis of lipid metabolism–related genes in AML12 cells. Expression of Gapdh as shown by the ratio of CT value (n = 3). C: Rate of [1-14C]palmitate incorporation into acid-soluble metabolites (n = 4). D: Oleic acid (either 0.1 or 0.4 mmol/L)-induced accumulation of TG in AML12 cells. BSA (1.3 mmol/L) was used as a control (n = 3). *P < 0.05. CT, threshold cycle. GAPDH, glyceraldehyde-3-phosphate dehydrogenase; IB, immunoblot. FIG. 2. The effect of VASP on lipid metabolism in AML12 cells. A: AML12 cells were transduced with VASP (VASP-OE) or control (ctl) (empty) vector. B: RT-PCR analysis of lipid metabolism–related genes in AML12 cells. Expression of Gapdh as shown by the ratio of CT value (n = 3). C: Rate of [1-14C]palmitate incorporation into acid-soluble metabolites (n = 4). D: Oleic acid (either 0.1 or 0.4 mmol/L)-induced accumulation of TG in AML12 cells. BSA (1.3 mmol/L) was used as a control (n = 3). *P < 0.05. CT, threshold cycle. GAPDH, glyceraldehyde-3-phosphate dehydrogenase; IB, immunoblot. More
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MMP-9 expression in transplanted liver. <em>A</em>: mRNA levels of ...
Published: 17 July 2012
FIG. 1. MMP-9 expression in transplanted liver. A: mRNA levels of MMP-2 and -9 were analyzed by RT-PCR in total RNA extracts from control liver (lanes 1 and 4) and islet-transplanted liver (lanes 2 and 3). GAPDH, glyceraldehyde-3-phosphate dehydrogenase. B: MMP-9 expressions in transplanted mice were significantly higher in comparison with control mice (*P < 0.05, n = 3). C: MMP-2 mRNA level was not significantly different in control and islet-transplanted liver (P > 0.05, n = 3). FIG. 1. MMP-9 expression in transplanted liver. A: mRNA levels of MMP-2 and -9 were analyzed by RT-PCR in total RNA extracts from control liver (lanes 1 and 4) and islet-transplanted liver (lanes 2 and 3). GAPDH, glyceraldehyde-3-phosphate dehydrogenase. B: MMP-9 expressions in transplanted mice were significantly higher in comparison with control mice (*P < 0.05, n = 3). C: MMP-2 mRNA level was not significantly different in control and islet-transplanted liver (P > 0.05, n = 3). More
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Adiponectin induces p38 MAPK phosphorylation in <em>MKK3</em> and -...
Published: 14 May 2012
FIG. 2. Adiponectin induces p38 MAPK phosphorylation in MKK3 and -6 gene knockout (KO) MEFs. Immortalized MEFs from WT and MKK3 and -6 knockout mice were cocultured overnight with FAO cells, which were transduced with Ad-Acrp30 (+) or Ad-GFP (-). Phosphorylation and total protein levels of p38 MAPK were detected by Western blot. Quantified data represent three separate studies; n = 6. Data are expressed as means ± SEM. GAPDH, glyceraldehyde-3-phosphate dehydrogenase. FIG. 2. Adiponectin induces p38 MAPK phosphorylation in MKK3 and -6 gene knockout (KO) MEFs. Immortalized MEFs from WT and MKK3 and -6 knockout mice were cocultured overnight with FAO cells, which were transduced with Ad-Acrp30 (+) or Ad-GFP (-). Phosphorylation and total protein levels of p38 MAPK were detected by Western blot. Quantified data represent three separate studies; n = 6. Data are expressed as means ± SEM. GAPDH, glyceraldehyde-3-phosphate dehydrogenase. More
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HDAC9 gene deletion prevents accumulation of inefficiently differentiated a...
Published: 13 December 2013
Figure 4 HDAC9 gene deletion prevents accumulation of inefficiently differentiated adipocytes in subcutaneous adipose tissue of HFD mice. A: Adipocytes (in vivo differentiated) were isolated from subcutaneous adipose depots of chow- and HFD-fed mice; HDAC9 mRNA levels in these cells were analyzed by qPCR. HDAC9 protein levels were determined in epididymal adipose tissue of chow- and HFD-fed mice by Western blot analysis. For mRNA expression, values represent mean ± SEM from four groups of mice (*P < 0.001), while ImageJ analysis of Western blot data were normalized to corresponding glyceraldehyde-3-phosphate dehydrogenase values and represent mean ± SEM from three groups of mice. B: Effects of an HFD on mRNA expression of adipogenic differentiation-specific genes C/EBPα, PPARγ, and adiponectin in freshly isolated adipocytes (in vivo differentiated) from subcutaneous adipose tissues of wild-type (+/+) and HDAC9 knockout (−/−) mice. Values are mean ± SEM of four experiments. *P < 0.05; CD, chow diet; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. Figure 4. HDAC9 gene deletion prevents accumulation of inefficiently differentiated adipocytes in subcutaneous adipose tissue of HFD mice. A: Adipocytes (in vivo differentiated) were isolated from subcutaneous adipose depots of chow- and HFD-fed mice; HDAC9 mRNA levels in these cells were analyzed by qPCR. HDAC9 protein levels were determined in epididymal adipose tissue of chow- and HFD-fed mice by Western blot analysis. For mRNA expression, values represent mean ± SEM from four groups of mice (*P < 0.001), while ImageJ analysis of Western blot data were normalized to corresponding glyceraldehyde-3-phosphate dehydrogenase values and represent mean ± SEM from three groups of mice. B: Effects of an HFD on mRNA expression of adipogenic differentiation-specific genes C/EBPα, PPARγ, and adiponectin in freshly isolated adipocytes (in vivo differentiated) from subcutaneous adipose tissues of wild-type (+/+) and HDAC9 knockout (−/−) mice. Values are mean ± SEM of four experiments. *P < 0.05; CD, chow diet; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. More
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Silencing of p38 MAPK by siRNA. siRNA transfection of p38 MAPK in cardiomyo...
Published: 01 January 2008
FIG. 9. Silencing of p38 MAPK by siRNA. siRNA transfection of p38 MAPK in cardiomyocytes was performed using a kit from Santa Cruz. Plated myocytes were exposed to the siRNA (or scrambled, Scr). Inset: Transfection efficiency. After this, AICAR (2 mmol/l) was added to the culture medium for 2 h and p38 MAPK (A), Hsp25 (B), and LPL activity (C) evaluated. Data are means ± SE; n = 3 myocyte preparations from different animals. *Significantly different (P < 0.05) from control; #significantly different (P < 0.05) from AICAR-treated control. GAPDH, glyceraldehyde 3-phosphate dehydrogenase. FIG. 9. Silencing of p38 MAPK by siRNA. siRNA transfection of p38 MAPK in cardiomyocytes was performed using a kit from Santa Cruz. Plated myocytes were exposed to the siRNA (or scrambled, Scr). Inset: Transfection efficiency. After this, AICAR (2 mmol/l) was added to the culture medium for 2 h and p38 MAPK (A), Hsp25 (B), and LPL activity (C) evaluated. Data are means ± SE; n = 3 myocyte preparations from different animals. *Significantly different (P < 0.05) from control; #significantly different (P < 0.05) from AICAR-treated control. GAPDH, glyceraldehyde 3-phosphate dehydrogenase. More
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Liver tissue analysis after food enrichment with MUFAs or SFAs. <em>A</em>...
Published: 15 June 2012
FIG. 3. Liver tissue analysis after food enrichment with MUFAs or SFAs. A and B: Attenuated phosphorylation of IR and AKT in liver tissue of SFA-fed animals. Liver lysates were separated by SDS-PAGE, and tyrosine phosphorylation (PY) of IR (A) and AKT (S473) (B) as well as protein expression of IR and AKT was analyzed after intravenous insulin injection (cross-hatched bars) in overnight-fasted MUFA-, SFA-, or chow-fed animals. Densitometric quantification of PY-IR (relative increase of PY-IR compared with insulin-stimulated control mice; n = 6–8/group; ***P < 0.001) is presented in histograms. Ins, insulin; GAPDH, glyceraldehyde 3-phosphate dehydrogenase. FIG. 3. Liver tissue analysis after food enrichment with MUFAs or SFAs. A and B: Attenuated phosphorylation of IR and AKT in liver tissue of SFA-fed animals. Liver lysates were separated by SDS-PAGE, and tyrosine phosphorylation (PY) of IR (A) and AKT (S473) (B) as well as protein expression of IR and AKT was analyzed after intravenous insulin injection (cross-hatched bars) in overnight-fasted MUFA-, SFA-, or chow-fed animals. Densitometric quantification of PY-IR (relative increase of PY-IR compared with insulin-stimulated control mice; n = 6–8/group; ***P < 0.001) is presented in histograms. Ins, insulin; GAPDH, glyceraldehyde 3-phosphate dehydrogenase. More
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Consequence of AMPK activation using AICAR. Cardiomyocytes were plated on l...
Published: 01 January 2008
FIG. 4. Consequence of AMPK activation using AICAR. Cardiomyocytes were plated on laminin-coated culture plates. Cells were maintained using Media-199 and incubated at 37°C under an atmosphere of 95% O2/5% CO2 for 16 h. Subsequently, AICAR (2 mmol/l) was added to the culture medium. At the indicated times, protein was extracted to determine AMPK (A), p38 (B), and Hsp25 (C) (both total and phosphorylated) using Western blotting. Data are means ± SE; n = 3 myocyte preparations from different animals. *Significantly different (P < 0.05) from control (0 min). GAPDH, glyceraldehyde 3-phosphate dehydrogenase. FIG. 4. Consequence of AMPK activation using AICAR. Cardiomyocytes were plated on laminin-coated culture plates. Cells were maintained using Media-199 and incubated at 37°C under an atmosphere of 95% O2/5% CO2 for 16 h. Subsequently, AICAR (2 mmol/l) was added to the culture medium. At the indicated times, protein was extracted to determine AMPK (A), p38 (B), and Hsp25 (C) (both total and phosphorylated) using Western blotting. Data are means ± SE; n = 3 myocyte preparations from different animals. *Significantly different (P < 0.05) from control (0 min). GAPDH, glyceraldehyde 3-phosphate dehydrogenase. More
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p38 MAPK and Hsp25 phosphorylation following incubation of cardiomyocytes w...
Published: 01 January 2008
FIG. 6. p38 MAPK and Hsp25 phosphorylation following incubation of cardiomyocytes with thrombin. Cardiomyocytes were incubated with thrombin (0.05 units/ml), which was added to the culture medium, and myocytes kept for 0–60 min. At the indicated times, cytosolic (A) and nuclear (B) protein was extracted to determine p38 MAPK. Total and phosphorylated Hsp25 were also determined at the indicated times using Western blotting (C). Cytosolic phospho–AMPK-α was also determined after incubation with thrombin (A, inset). Data are means ± SE; n = 3 myocyte preparations from different animals. *Significantly different (P < 0.05) from control. GAPDH, glyceraldehyde 3-phosphate dehydrogenase. FIG. 6. p38 MAPK and Hsp25 phosphorylation following incubation of cardiomyocytes with thrombin. Cardiomyocytes were incubated with thrombin (0.05 units/ml), which was added to the culture medium, and myocytes kept for 0–60 min. At the indicated times, cytosolic (A) and nuclear (B) protein was extracted to determine p38 MAPK. Total and phosphorylated Hsp25 were also determined at the indicated times using Western blotting (C). Cytosolic phospho–AMPK-α was also determined after incubation with thrombin (A, inset). Data are means ± SE; n = 3 myocyte preparations from different animals. *Significantly different (P < 0.05) from control. GAPDH, glyceraldehyde 3-phosphate dehydrogenase. More
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Microtubule levels are reduced in <em>Ide</em> KO islets. Immunoblo...
Published: 17 May 2013
FIG. 4. Microtubule levels are reduced in Ide KO islets. Immunoblot (A) and quantification (B) analyses of monomeric and polymeric tubulin fractions from starved and glucose-stimulated Ide KO and Ide WT islets (n = 8 mice per genotype). C: Insulin secretion from isolated Ide KO (n = 4 mice) and Ide WT (n = 4 mice) islets after exposure to latrunculin-B at low (2.8 mmol/L) and high (16.8 mmol/L) glucose concentrations. Data are presented as mean ± SEM. *P < 0.05; ***P < 0.001 (Student t test). GAPDH, glyceraldehyde-3-phosphate dehydrogenase; Veh, Vehicle; Latr, Latrunculin B. FIG. 4. Microtubule levels are reduced in Ide KO islets. Immunoblot (A) and quantification (B) analyses of monomeric and polymeric tubulin fractions from starved and glucose-stimulated Ide KO and Ide WT islets (n = 8 mice per genotype). C: Insulin secretion from isolated Ide KO (n = 4 mice) and Ide WT (n = 4 mice) islets after exposure to latrunculin-B at low (2.8 mmol/L) and high (16.8 mmol/L) glucose concentrations. Data are presented as mean ± SEM. *P < 0.05; ***P < 0.001 (Student t test). GAPDH, glyceraldehyde-3-phosphate dehydrogenase; Veh, Vehicle; Latr, Latrunculin B. More
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AMPK signaling is regulated by VASP in the liver. <em>A</em>: Phosp...
Published: 17 May 2013
FIG. 3. AMPK signaling is regulated by VASP in the liver. A: Phosphorylation of AMPK (Thr172) and ACC (Ser79) in AML12 cells with VASP overexpression. AICAR was used as a positive control. Western blot from one of three independent experiments is shown. B: Primary hepatocytes were isolated from WT or Vasp−/− mice and cultured. p-AMPK (Thr172) and p-ACC (Ser79) as measured by Western blot. Representative blots are shown. Rate of [1-14C]palmitate incorporation into acid-soluble metabolites (n = 3). C: p-AMPK and p-ACC in the liver collected after an overnight fast (n = 6). Representative blots are shown. *P < 0.05. GAPDH, glyceraldehyde-3-phosphate dehydrogenase; IB, immunoblot. FIG. 3. AMPK signaling is regulated by VASP in the liver. A: Phosphorylation of AMPK (Thr172) and ACC (Ser79) in AML12 cells with VASP overexpression. AICAR was used as a positive control. Western blot from one of three independent experiments is shown. B: Primary hepatocytes were isolated from WT or Vasp−/− mice and cultured. p-AMPK (Thr172) and p-ACC (Ser79) as measured by Western blot. Representative blots are shown. Rate of [1-14C]palmitate incorporation into acid-soluble metabolites (n = 3). C: p-AMPK and p-ACC in the liver collected after an overnight fast (n = 6). Representative blots are shown. *P < 0.05. GAPDH, glyceraldehyde-3-phosphate dehydrogenase; IB, immunoblot. More
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Gene expression of NOX components in mouse islets and purified β-cells. ...
Published: 16 October 2012
FIG. 2. Gene expression of NOX components in mouse islets and purified β-cells. A, B, and C: Expression of catalytic Nox subunits in mouse islets (left panels of AC) was detected at the mRNA level by RT-PCR (for each gene, 35 and 40 cycles for the left and right lanes, respectively). Positive controls (right panels of AC) were performed with cDNA from mouse colon for Nox1, Noxa1 (homolog of p67phox), and Noxo1 (homolog of p47phox); from spleen for Nox2, p22phox, p40phox, p47phox, and p67phox; and from kidney for Nox4. D: Nox2 expression (40 cycles of PCR) in purified β-cells from two C57BL/6J mice with cDNA from mouse spleen as positive control. Gapdh, glyceraldehyde-3-phosphate dehydrogenase. FIG. 2. Gene expression of NOX components in mouse islets and purified β-cells. A, B, and C: Expression of catalytic Nox subunits in mouse islets (left panels of A–C) was detected at the mRNA level by RT-PCR (for each gene, 35 and 40 cycles for the left and right lanes, respectively). Positive controls (right panels of A–C) were performed with cDNA from mouse colon for Nox1, Noxa1 (homolog of p67phox), and Noxo1 (homolog of p47phox); from spleen for Nox2, p22phox, p40phox, p47phox, and p67phox; and from kidney for Nox4. D: Nox2 expression (40 cycles of PCR) in purified β-cells from two C57BL/6J mice with cDNA from mouse spleen as positive control. Gapdh, glyceraldehyde-3-phosphate dehydrogenase. More
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Collagen mRNA expression is increased in diabetic mice after treatment with...
Published: 01 February 2006
FIG. 4. Collagen mRNA expression is increased in diabetic mice after treatment with caspase inhibitor (Inh). Bacteria were inoculated into diabetic mice, diabetic mice treated with caspase inhibitor, and normoglycemic controls. Mice were killed 8 days after bacterial inoculation. There were six mice per group (n = 6). Procollagen I (A) and III (B) mRNA levels were measured by the RNase protection assay. The densitometric values of procollagen I and III were normalized by GAPDH (glyceraldehyde-3-phosphate dehydrogenase) levels in the same lane. Each assay was carried out three times and the values combined to give the means ± SE. *Significant difference between diabetic and diabetic mice treated with inhibitor (P < 0.05). FIG. 4. Collagen mRNA expression is increased in diabetic mice after treatment with caspase inhibitor (Inh). Bacteria were inoculated into diabetic mice, diabetic mice treated with caspase inhibitor, and normoglycemic controls. Mice were killed 8 days after bacterial inoculation. There were six mice per group (n = 6). Procollagen I (A) and III (B) mRNA levels were measured by the RNase protection assay. The densitometric values of procollagen I and III were normalized by GAPDH (glyceraldehyde-3-phosphate dehydrogenase) levels in the same lane. Each assay was carried out three times and the values combined to give the means ± SE. *Significant difference between diabetic and diabetic mice treated with inhibitor (P < 0.05). More
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Selectivity and abundance of PPP1R1A in rat and human β-cells. <em>A</em>...
Published: 17 July 2013
FIG. 1. Selectivity and abundance of PPP1R1A in rat and human β-cells. A: Human pancreas stained for PPP1R1A (green) and insulin (INS) or glucagon (GLUC) (red). Selected images are representative for three different organs. B: Western blotting of PPP1R1A expression in rat tissues. Bars represent mean ± SD of three biological replicates. C: Relative molar protein abundances in rat α- and β-cells (n = 3) measured by label-free quantitative liquid chromatography–tandem mass spectrometry ( 16 ). Proteins are denoted by their official National Center for Biotechnology Information gene symbol: Actb, β-actin; Chga, chromogranin A; fmolr, relative femtomolar amount; Gapdh, glyceraldehyde-3-phosphate dehydrogenase; Pcsk1, prohormone convertase 1; Pcsk2, prohormone convertase 2; Ppia, cyclophilin-A. FIG. 1. Selectivity and abundance of PPP1R1A in rat and human β-cells. A: Human pancreas stained for PPP1R1A (green) and insulin (INS) or glucagon (GLUC) (red). Selected images are representative for three different organs. B: Western blotting of PPP1R1A expression in rat tissues. Bars represent mean ± SD of three biological replicates. C: Relative molar protein abundances in rat α- and β-cells (n = 3) measured by label-free quantitative liquid chromatography–tandem mass spectrometry (16). Proteins are denoted by their official National Center for Biotechnology Information gene symbol: Actb, β-actin; Chga, chromogranin A; fmolr, relative femtomolar amount; Gapdh, glyceraldehyde-3-phosphate dehydrogenase; Pcsk1, prohormone convertase 1; Pcsk2, prohormone convertase 2; Ppia, cyclophilin-A. More