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acc-acetyl-coa-carboxylase

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Meeting Abstracts
Journal: Diabetes
Diabetes 2020;69(Supplement_1):1830-P
Published: 01 June 2020
... in hepatic inflammatory marker expression and NAFLD activity score. Of note, when compared to FXR agonist or ACC (acetyl CoA carboxylase) inhibitor, HM15211 treatment was associated with greater efficacy improvement. To further confirm, CDHFD mice with an extended induction period (up to 16 wks) was used...
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Revised malonyl-<span class="search-highlight">CoA</span>/LC-<span class="search-highlight">CoA</span> model of insulin secretion. The malonyl-<span class="search-highlight">CoA</span>/LC-C...
Published: 01 April 2004
FIG. 8. Revised malonyl-CoA/LC-CoA model of insulin secretion. The malonyl-CoA/LC-CoA signaling pathway synergizes with other “classical” pathways that utilize Ca2+, PKC, and cAMP/protein kinase A signaling such that lipid signaling has a regulatory amplification role on insulin secretion to all fuel and nonfuel stimuli. Malonyl-CoA, derived from the anaplerosis pathway, modulates partitioning of exogenous FFAs via LC-CoA from fatty acid oxidation to lipid signaling involved in insulin vesicle exocytosis. AcCoAc, cytosolic acetyl-CoA; AcCoAm, mitochondrial acetyl-CoA; ACC, acetyl-CoA carboxylase; ARG, arginine; CCH, carbachol; FSK, forskolin; GLN, glutamine; LEU, leucine; βox, β-oxidation of fatty acids; PC, pyruvate carboxylase; PDH, pyruvate dehydrogenase. FIG. 8. Revised malonyl-CoA/LC-CoA model of insulin secretion. The malonyl-CoA/LC-CoA signaling pathway synergizes with other “classical” pathways that utilize Ca2+, PKC, and cAMP/protein kinase A signaling such that lipid signaling has a regulatory amplification role on insulin secretion to all fuel and nonfuel stimuli. Malonyl-CoA, derived from the anaplerosis pathway, modulates partitioning of exogenous FFAs via LC-CoA from fatty acid oxidation to lipid signaling involved in insulin vesicle exocytosis. AcCoAc, cytosolic acetyl-CoA; AcCoAm, mitochondrial acetyl-CoA; ACC, acetyl-CoA carboxylase; ARG, arginine; CCH, carbachol; FSK, forskolin; GLN, glutamine; LEU, leucine; βox, β-oxidation of fatty acids; PC, pyruvate carboxylase; PDH, pyruvate dehydrogenase. More
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Regulation of cellular fatty acid partitioning and metabolism by AMPK. <ita
Published: 01 December 2006
FIG. 2. Regulation of cellular fatty acid partitioning and metabolism by AMPK. A: AMPK neutral. By inhibiting CPT-1, malonyl-CoA, which is derived from glucose, diminishes the entrance of cytosolic FA-CoA into mitochondria where they are oxidized. This makes more cytosolic FA-CoA available for triglyceride (TG), diacylglycerol, and ceramide synthesis; lipid peroxidation; and possibly other events that lead to NKκB activation. B: AMPK activated: AMPK increases fatty acid oxidation acutely by phosphorylating and inhibiting ACC and activating MCD, leading to a decrease in malonyl-CoA. It also does this subacutely by effects on ACC, MCD, and CPT-1 abundance at the level of transcription. In addition, AMPK inhibits serine palmitoyltransferase, the first committed enzyme in the de novo pathway for ceramide synthesis and glycerophosphate acyltransferase, which plays a similar role in glycerolipid synthesis. The basis for the ability of AMPK to inhibit oxidant stress (ROS generation) and nuclear factor (NF)-κB activation (inflammation) is not known. Whether AMPK activation enhances or inhibits a process or an enzyme in this scheme is denoted by plus and minus signs, respectively (see full text for details). ACC, acetyl-CoA carboxylase; CPT1, carnitine palmitoyltransferase 1; DAG, diacylglycerol; FA CoA, cytosolic long-chain fatty acyl-CoA; FFA, free fatty acid; GPAT, glycerophosphate acyltransferase; MCD, malonyl-CoA decarboxylase; ROS, reactive O2 species. Adapted from Ruderman and Prentki ( 17 ). See text for additional details. FIG. 2. Regulation of cellular fatty acid partitioning and metabolism by AMPK. A: AMPK neutral. By inhibiting CPT-1, malonyl-CoA, which is derived from glucose, diminishes the entrance of cytosolic FA-CoA into mitochondria where they are oxidized. This makes more cytosolic FA-CoA available for triglyceride (TG), diacylglycerol, and ceramide synthesis; lipid peroxidation; and possibly other events that lead to NKκB activation. B: AMPK activated: AMPK increases fatty acid oxidation acutely by phosphorylating and inhibiting ACC and activating MCD, leading to a decrease in malonyl-CoA. It also does this subacutely by effects on ACC, MCD, and CPT-1 abundance at the level of transcription. In addition, AMPK inhibits serine palmitoyltransferase, the first committed enzyme in the de novo pathway for ceramide synthesis and glycerophosphate acyltransferase, which plays a similar role in glycerolipid synthesis. The basis for the ability of AMPK to inhibit oxidant stress (ROS generation) and nuclear factor (NF)-κB activation (inflammation) is not known. Whether AMPK activation enhances or inhibits a process or an enzyme in this scheme is denoted by plus and minus signs, respectively (see full text for details). ACC, acetyl-CoA carboxylase; CPT1, carnitine palmitoyltransferase 1; DAG, diacylglycerol; FA CoA, cytosolic long-chain fatty acyl-CoA; FFA, free fatty acid; GPAT, glycerophosphate acyltransferase; MCD, malonyl-CoA decarboxylase; ROS, reactive O2 species. Adapted from Ruderman and Prentki (17). See text for additional details. More
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Liver lipid metabolism in the <em>ob/ob</em>-aP2-mal<sup>−/−</sup> ...
Published: 01 July 2006
FIG. 5. Liver lipid metabolism in the ob/ob-aP2-mal−/− mice. Total wet weight (A) and triglyceride content (B) of liver tissue. C: Portal concentration of free fatty acids. D: Hematoxylin-eosin staining of liver sections (×250). E: SCD1 expression in the liver tissue of ob/ob and ob/ob-AM−/− mice. F: Full-length (SREBP1) and nuclear SREBP1 (SREBP1-N) in the liver tissue of ob/ob and ob/ob-AM−/− mice. G and H: Relative liver mRNA expression in ob/ob-AM−/− mice compared with ob/ob controls. ACC, acetyl-CoA carboxylase; FAS, fatty acid synthase; SCD-1, stearoyl-CoA desaturase; ELOVL6, elongation of very-long- chain fatty acid-6; DGAT1, acyl-CoA:diacylglycerol acyltransferase 1; mGPAT, mitochondria glycerol-phosphate acyltransferase; HMGCoA, 3-hydroxy-3-methylglutaryl CoA. *P < 0.05. FIG. 5. Liver lipid metabolism in the ob/ob-aP2-mal−/− mice. Total wet weight (A) and triglyceride content (B) of liver tissue. C: Portal concentration of free fatty acids. D: Hematoxylin-eosin staining of liver sections (×250). E: SCD1 expression in the liver tissue of ob/ob and ob/ob-AM−/− mice. F: Full-length (SREBP1) and nuclear SREBP1 (SREBP1-N) in the liver tissue of ob/ob and ob/ob-AM−/− mice. G and H: Relative liver mRNA expression in ob/ob-AM−/− mice compared with ob/ob controls. ACC, acetyl-CoA carboxylase; FAS, fatty acid synthase; SCD-1, stearoyl-CoA desaturase; ELOVL6, elongation of very-long- chain fatty acid-6; DGAT1, acyl-CoA:diacylglycerol acyltransferase 1; mGPAT, mitochondria glycerol-phosphate acyltransferase; HMGCoA, 3-hydroxy-3-methylglutaryl CoA. *P < 0.05. More
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Overview of the role of the ATF/CREB family in the pathway involved in hepa...
Published: 15 February 2021
Figure 2 Overview of the role of the ATF/CREB family in the pathway involved in hepatic lipid metabolism. The ATF/CREB family members transduce various nutrient and energy signals into the nucleus and modulate hepatic lipid metabolism via regulating expression of key enzymes and regulators involve... More
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Impaired lipolysis in WAT of fasted <em>Ugcg</em>f/f//CamKCreERT2 m...
Published: 02 June 2015
Figure 2 Impaired lipolysis in WAT of fasted Ugcgf/f//CamKCreERT2 mice. A: Fasting overnight induces a release of FFA into the serum of Ugcgf/f control mice. However, fasting-induced FFA release is not significantly stimulated in Ugcgf/f//CamKCreERT2 mice. Refeeding (4 h) restrains FFA release in both groups (n = 7–10 [fed/fasted], n = 3 [refed]). B and C: IR levels are normal in WAT of Ugcgf/f//CamKCreERT2 mice (n = 7–9). D: Western blots of WAT from fasted Ugcgf/f//CamKCreERT2 mice demonstrate expression and phosphorylation status of enzymes involved in lipolysis and lipogenesis. E: The phosphorylations indicative for active HSL (Ser563 and Ser660) are significantly decreased in WAT of Ugcgf/f//CamKCreERT2 mice. The phosphorylation indicative for inactive HSL (Ser565), however, is not altered in fasted Ugcgf/f//CamKCreERT2 mice. Baseline HSL levels are not significantly changed (n = 4–5). F: Protein levels of ACC and FAS involved in lipogenesis are not significantly decreased in fasted Ugcgf/f//CamKCreERT2 mice (n = 4–5). *P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001. ACC, acetyl-CoA carboxylase; FAS, fatty acid synthase; n.s., not significant; P, phosphorylated. Mice were analyzed 6 weeks pi. Means ± SEM. Figure 2. Impaired lipolysis in WAT of fasted Ugcgf/f//CamKCreERT2 mice. A: Fasting overnight induces a release of FFA into the serum of Ugcgf/f control mice. However, fasting-induced FFA release is not significantly stimulated in Ugcgf/f//CamKCreERT2 mice. Refeeding (4 h) restrains FFA release in both groups (n = 7–10 [fed/fasted], n = 3 [refed]). B and C: IR levels are normal in WAT of Ugcgf/f//CamKCreERT2 mice (n = 7–9). D: Western blots of WAT from fasted Ugcgf/f//CamKCreERT2 mice demonstrate expression and phosphorylation status of enzymes involved in lipolysis and lipogenesis. E: The phosphorylations indicative for active HSL (Ser563 and Ser660) are significantly decreased in WAT of Ugcgf/f//CamKCreERT2 mice. The phosphorylation indicative for inactive HSL (Ser565), however, is not altered in fasted Ugcgf/f//CamKCreERT2 mice. Baseline HSL levels are not significantly changed (n = 4–5). F: Protein levels of ACC and FAS involved in lipogenesis are not significantly decreased in fasted Ugcgf/f//CamKCreERT2 mice (n = 4–5). *P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001. ACC, acetyl-CoA carboxylase; FAS, fatty acid synthase; n.s., not significant; P, phosphorylated. Mice were analyzed 6 weeks pi. Means ± SEM. More
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Gene expression profile in liver and skeletal muscle of wild-type and <ital
Published: 01 December 2006
FIG. 6. Gene expression profile in liver and skeletal muscle of wild-type and fld mice determined by real-time RT-PCR. Wild-type and fld mice were maintained on regular chow diet. Tissues were taken from these animals either after an 18-h fasting or after an 18-h fasting plus a 5-h refeeding (n = 4 for each genotype at each feeding status). Gene expression results are presented as means ± SEM and expressed as the percentage seen for the expression in wild-type mice tissues in the fasted state. Statistical differences (P < 0.05) were determined by two-way ANOVA, followed by Bonferroni posttests. Statistical differences determined by Bonferroni posttests of multiple comparison were shown between * and #. A: Gene expression of hepatic enzymes involved in gluconeogenesis and TCA cycle entry. All mRNA levels are statistically different for genotype (except for pyruvate kinase), feeding status (except for pyruvate carboxylase), and genotype/feeding interactions (except for PEPCK). B: Gene expression of hepatic fatty acid synthesis enzymes and muscle hexokinase II. All gene expressions were statistically different for genotype (except for ATP:citrate lyase and hexokinase II), feeding status, and genotype/feeding interactions. ACC, acetyl-CoA carboxylase; ACL, ATP:citrate lyase; FAS, fatty acid synthase; HKII, muscle hexokinase II; PC, pyruvate carboxylase; PK, pyruvate kinase; WT, wild type. FIG. 6. Gene expression profile in liver and skeletal muscle of wild-type and fld mice determined by real-time RT-PCR. Wild-type and fld mice were maintained on regular chow diet. Tissues were taken from these animals either after an 18-h fasting or after an 18-h fasting plus a 5-h refeeding (n = 4 for each genotype at each feeding status). Gene expression results are presented as means ± SEM and expressed as the percentage seen for the expression in wild-type mice tissues in the fasted state. Statistical differences (P < 0.05) were determined by two-way ANOVA, followed by Bonferroni posttests. Statistical differences determined by Bonferroni posttests of multiple comparison were shown between * and #. A: Gene expression of hepatic enzymes involved in gluconeogenesis and TCA cycle entry. All mRNA levels are statistically different for genotype (except for pyruvate kinase), feeding status (except for pyruvate carboxylase), and genotype/feeding interactions (except for PEPCK). B: Gene expression of hepatic fatty acid synthesis enzymes and muscle hexokinase II. All gene expressions were statistically different for genotype (except for ATP:citrate lyase and hexokinase II), feeding status, and genotype/feeding interactions. ACC, acetyl-CoA carboxylase; ACL, ATP:citrate lyase; FAS, fatty acid synthase; HKII, muscle hexokinase II; PC, pyruvate carboxylase; PK, pyruvate kinase; WT, wild type. More
Images
Fasting-induced lipolysis is impaired in weight-matched Ugcgf/f//CamKCreERT...
Published: 02 June 2015
Figure 3 Fasting-induced lipolysis is impaired in weight-matched Ugcgf/f//CamKCreERT2 mice 3–4 weeks pi. A: Parametrial WAT weight is significantly increased in Ugcgf/f//CamKCreERT2 mice (n = 6–13). B and C: WAT cells, as determined by hematoxylin-eosin staining, are also enlarged (n = 212–386 cells). D: Ugcgf/f//CamKCreERT2 mice lose less weight upon fasting (n = 6–13). E: A fasting-induced increase in serum FFA is observed in control mice, but not in Ugcgf/f//CamKCreERT2 mice (n = 5–8). F: Western blots of WAT from fasted Ugcgf/f//CamKCreERT2 mice demonstrate the expression and phosphorylation (P) status of enzymes involved in lipolysis and lipogenesis, as well as IR expression. G: IR expression in WAT is normal in Ugcgf/f//CamKCreERT2 mice. H: HSL phosphorylations indicative for active HSL (Ser563 and Ser660) are significantly decreased in Ugcgf/f//CamKCreERT2 mice, whereas HSL expression itself is unchanged (n = 6–8; n = 6 for Ser660). I: Expression levels of ACC and FAS involved in lipogenesis are not significantly changed (n = 6–8). ACC, acetyl-CoA carboxylase; FAS, fatty acid synthase; n.s., not significant. Mice were analyzed 3–4 weeks pi. Data are reported as the mean ± SEM. *P ≤ 0.05, **P ≤ 0.01. Figure 3. Fasting-induced lipolysis is impaired in weight-matched Ugcgf/f//CamKCreERT2 mice 3–4 weeks pi. A: Parametrial WAT weight is significantly increased in Ugcgf/f//CamKCreERT2 mice (n = 6–13). B and C: WAT cells, as determined by hematoxylin-eosin staining, are also enlarged (n = 212–386 cells). D: Ugcgf/f//CamKCreERT2 mice lose less weight upon fasting (n = 6–13). E: A fasting-induced increase in serum FFA is observed in control mice, but not in Ugcgf/f//CamKCreERT2 mice (n = 5–8). F: Western blots of WAT from fasted Ugcgf/f//CamKCreERT2 mice demonstrate the expression and phosphorylation (P) status of enzymes involved in lipolysis and lipogenesis, as well as IR expression. G: IR expression in WAT is normal in Ugcgf/f//CamKCreERT2 mice. H: HSL phosphorylations indicative for active HSL (Ser563 and Ser660) are significantly decreased in Ugcgf/f//CamKCreERT2 mice, whereas HSL expression itself is unchanged (n = 6–8; n = 6 for Ser660). I: Expression levels of ACC and FAS involved in lipogenesis are not significantly changed (n = 6–8). ACC, acetyl-CoA carboxylase; FAS, fatty acid synthase; n.s., not significant. Mice were analyzed 3–4 weeks pi. Data are reported as the mean ± SEM. *P ≤ 0.05, **P ≤ 0.01. More
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Interplay of metabolic effects of insulin and LXR. The green areas indicate...
Published: 01 February 2004
FIG. 1. Interplay of metabolic effects of insulin and LXR. The green areas indicate LXR target genes, blue arrows indicate activating effect, and the red arrow indicates inhibitory effects. Activation of LXR leads to increased glucose uptake in muscle and adipose tissue via the GLUT transporters. ... More
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CD36 is involved in OPG-regulated hepatic steatosis. <em>A</em> and...
Published: 10 July 2019
Figure 5 CD36 is involved in OPG-regulated hepatic steatosis. A and B: L02 cells were treated with BSA or FFAs after transfection with Adv-GFP, Adv-OPG, Adv-control, or Adv-shOPG. A and B: The protein levels of lipogenic genes (A) and CD36 (B). ACC, acetyl-CoA carboxylase; FAS, fatty acid synthase. C: CD36 protein levels in the livers of WT or OPG−/− mice fed the SD or HFD for 12 weeks. D and E: MPHs from CD36 −/− mice were treated with BSA or FFAs after treatment with OPG-Fc. Oil Red O staining (D) and TG contents (E). Data are presented as the mean ± SD. *P < 0.01 vs. Adv-GFP, Adv-control, or SD-WT. #P < 0.01 vs. Adv-control or HFD-WT. F: Deletion analysis of the mouse CD36 gene promoter. L02 cells were transfected with OPG overexpression vector, together with a series of truncated CD36 promoter-driven luciferase (Luc) reporters. Luciferase activity was measured 48 h after the transfection and expressed in relative luciferase units. G: Site-directed mutagenesis analysis. L02 cells were cotransfected with OPG expression plasmids and luciferase reporter plasmids containing WT and PPRE or pregnane X receptor response element (PXRE) binding site mutant CD36 promoters, and luciferase reporter assays were performed. The data are expressed as the mean ± SD. *P < 0.01 vs. GFP. Figure 5. CD36 is involved in OPG-regulated hepatic steatosis. A and B: L02 cells were treated with BSA or FFAs after transfection with Adv-GFP, Adv-OPG, Adv-control, or Adv-shOPG. A and B: The protein levels of lipogenic genes (A) and CD36 (B). ACC, acetyl-CoA carboxylase; FAS, fatty acid synthase. C: CD36 protein levels in the livers of WT or OPG−/− mice fed the SD or HFD for 12 weeks. D and E: MPHs from CD36 −/− mice were treated with BSA or FFAs after treatment with OPG-Fc. Oil Red O staining (D) and TG contents (E). Data are presented as the mean ± SD. *P < 0.01 vs. Adv-GFP, Adv-control, or SD-WT. #P < 0.01 vs. Adv-control or HFD-WT. F: Deletion analysis of the mouse CD36 gene promoter. L02 cells were transfected with OPG overexpression vector, together with a series of truncated CD36 promoter-driven luciferase (Luc) reporters. Luciferase activity was measured 48 h after the transfection and expressed in relative luciferase units. G: Site-directed mutagenesis analysis. L02 cells were cotransfected with OPG expression plasmids and luciferase reporter plasmids containing WT and PPRE or pregnane X receptor response element (PXRE) binding site mutant CD36 promoters, and luciferase reporter assays were performed. The data are expressed as the mean ± SD. *P < 0.01 vs. GFP. More
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Hepatic <em>Igf-1</em> transgene does not resolve hepatic lipid met...
Published: 27 September 2016
Figure 5 Hepatic Igf-1 transgene does not resolve hepatic lipid metabolism in Li-GHRKO mice. A and B: Liver gene expression of key players in lipid metabolism was determined by real-time PCR (n = 8/genotype). C: SCD-1 index determined by the ratio of hepatic stearic and oleic acid concentrations determined by GC/MS. D: Hepatic gene expression of key players in glycolysis (GLUT2, glucokinase [GCK], and liver pyruvate kinase [PKLr]) and gluconeogenesis (PC, PCK1, and glucose 6 phosphatase [G6PC]). Liver RNA extracted from 16- to 24-week-old male mice and processed for real-time PCR assay. E: Hepatic glycogen content assayed in livers of 16-week-old male mice. Data presented as mean ± SEM. N indicates sample size. Significance accepted at P < 0.05: control vs. Li-GHRKO (a), control vs. Li-GHRKO-HIT (b), Li-GHRKO vs. Li-GHRKO-HIT (d), Li-GHRKO vs. HIT (e), and Li-GHRKO-HIT vs. HIT (f). ACC, acetyl-CoA carboxylase; Fas2, FA synthase 2; Fatp, FA transport protein; LDLR, LDL receptor; PGC1α, peroxisome proliferator–activated receptor-γ coactivator 1α; PPARγ, peroxisome proliferator–activated receptor γ; SREBP1c, sterol regulatory element–binding protein 1c. Figure 5. Hepatic Igf-1 transgene does not resolve hepatic lipid metabolism in Li-GHRKO mice. A and B: Liver gene expression of key players in lipid metabolism was determined by real-time PCR (n = 8/genotype). C: SCD-1 index determined by the ratio of hepatic stearic and oleic acid concentrations determined by GC/MS. D: Hepatic gene expression of key players in glycolysis (GLUT2, glucokinase [GCK], and liver pyruvate kinase [PKLr]) and gluconeogenesis (PC, PCK1, and glucose 6 phosphatase [G6PC]). Liver RNA extracted from 16- to 24-week-old male mice and processed for real-time PCR assay. E: Hepatic glycogen content assayed in livers of 16-week-old male mice. Data presented as mean ± SEM. N indicates sample size. Significance accepted at P < 0.05: control vs. Li-GHRKO (a), control vs. Li-GHRKO-HIT (b), Li-GHRKO vs. Li-GHRKO-HIT (d), Li-GHRKO vs. HIT (e), and Li-GHRKO-HIT vs. HIT (f). ACC, acetyl-CoA carboxylase; Fas2, FA synthase 2; Fatp, FA transport protein; LDLR, LDL receptor; PGC1α, peroxisome proliferator–activated receptor-γ coactivator 1α; PPARγ, peroxisome proliferator–activated receptor γ; SREBP1c, sterol regulatory element–binding protein 1c. More
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HFD-fed CEPT1-MKO mice are protected from diet-induced skeletal muscle insu...
Published: 28 October 2015
Figure 3 HFD-fed CEPT1-MKO mice are protected from diet-induced skeletal muscle insulin resistance. A: Body weight. n = 7/experimental group. B: Body composition by MRI. n = 9/experimental group. C: Oxygen consumption. n = 5/experimental group. D: Respiratory quotient. n = 5–6/experimental group. E: Glucose tolerance testing (GTT). Area under the curve (AUC) quantification is provided as an insert. n = 10/experimental group. F: Insulin tolerance testing (ITT). Area under the curve quantification is provided as an insert. n = 6–7/experimental group. GJ: Hyperinsulinemic-euglycemic clamp studies. n = 4/experimental group. G: Glucose infusion rate (GIR). H: Glucose disposal rate (GDR). I: IS-GDR. J: HGP suppression. KN: Studies of isolated soleus muscles. n = 6/experimental group. K: 2DG uptake in basal and insulin-stimulated soleus. L: Δ2DG uptake was calculated by subtracting values of 2DG uptake in basal muscles from values of 2DG uptake in insulin-stimulated muscles. M and N: Western blot quantification of incubated soleus muscles under basal or insulin-stimulated conditions. Data are means ± SEM. *P < 0.05. †P < 0.05 vs. control (Ctrl). ACC, acetyl-CoA carboxylase; Ins, insulin; p, phosphorylated; RQ, respiratory quotient. Figure 3. HFD-fed CEPT1-MKO mice are protected from diet-induced skeletal muscle insulin resistance. A: Body weight. n = 7/experimental group. B: Body composition by MRI. n = 9/experimental group. C: Oxygen consumption. n = 5/experimental group. D: Respiratory quotient. n = 5–6/experimental group. E: Glucose tolerance testing (GTT). Area under the curve (AUC) quantification is provided as an insert. n = 10/experimental group. F: Insulin tolerance testing (ITT). Area under the curve quantification is provided as an insert. n = 6–7/experimental group. G–J: Hyperinsulinemic-euglycemic clamp studies. n = 4/experimental group. G: Glucose infusion rate (GIR). H: Glucose disposal rate (GDR). I: IS-GDR. J: HGP suppression. K–N: Studies of isolated soleus muscles. n = 6/experimental group. K: 2DG uptake in basal and insulin-stimulated soleus. L: Δ2DG uptake was calculated by subtracting values of 2DG uptake in basal muscles from values of 2DG uptake in insulin-stimulated muscles. M and N: Western blot quantification of incubated soleus muscles under basal or insulin-stimulated conditions. Data are means ± SEM. *P < 0.05. †P < 0.05 vs. control (Ctrl). ACC, acetyl-CoA carboxylase; Ins, insulin; p, phosphorylated; RQ, respiratory quotient. More
Journal Articles
Journal: Diabetes
Diabetes 1997;46(3):393–400
Published: 01 March 1997
... of metabolic enzymes implicated in the regulation of insulin secretion, in particular acetyl-CoA carboxylase (ACC). This enzyme catalyzes the formation of malonyl-CoA, a key regulator of fatty acid oxidation. Using the β-cell line INS-1 as a model, the results show that the polyunsaturated fatty acid linoleate...
Meeting Abstracts
Journal: Diabetes
Diabetes 2000;49(8):1295–1300
Published: 01 August 2000
...D Dean; J R Daugaard; M E Young; A Saha; D Vavvas; S Asp; B Kiens; K H Kim; L Witters; E A Richter; N Ruderman Studies in rats suggest that increases in fatty acid oxidation in skeletal muscle during exercise are related to the phosphorylation and inhibition of acetyl-CoA carboxylase (ACC...
Journal Articles
Journal: Diabetes
Diabetes 1996;45(2):190–198
Published: 01 February 1996
...- and long-term regulation of acetyl-CoA carboxylase (ACC) and fatty acid synthase (FAS) in the β-cell. These enzymes catalyze the formation of malonyl-CoA and its usage for de novo fatty acid biogenesis. ACC mRNA, protein, and enzymatic activity are present at appreciable levels in rat pancreatic islets...
Meeting Abstracts
Journal: Diabetes
Diabetes 1998;47(12):1904–1908
Published: 01 December 1998
... via the circulation. Here we examine the capacity of ZDF islets to synthesize fatty acids de novo. Compared with age-matched wild-type (+/+) control islets, acetyl CoA carboxylase (ACC) mRNA was fivefold and sixfold higher and fatty acid synthetase (FAS) was fourfold and sevenfold higher...
Journal Articles
Journal: Diabetes
Diabetes 2001;50(7):1580–1587
Published: 01 July 2001
...Anjaneyulu Kowluru; Hai-Qing Chen; Lisa M. Modrick; Claudio Stefanelli Acetyl-CoA carboxylase (ACC) catalyzes the formation of malonyl-CoA, a precursor in the biosynthesis of long-chain fatty acids, which have been implicated in physiological insulin secretion. The catalytic function of ACC...
Journal Articles
Journal: Diabetes
Diabetes 2005;54(12):3484–3489
Published: 01 December 2005
... responses among genotypes. In Tg-Prkag3225Q mice, acetyl-CoA carboxylase (ACC) phosphorylation was increased and triglyceride content was reduced after exercise, suggesting that this mutation promotes greater reliance on lipid oxidation. In contrast, ACC phosphorylation and triglyceride...
Meeting Abstracts
Journal: Diabetes
Diabetes 2000;49(8):1281–1287
Published: 01 August 2000
... group (low muscle glycogen content [LG]). In perfused fast-twitch muscles, contractions induced significant increases in AMPK activity and glucose transport and decreases in acetyl-CoA carboxylase (ACC) activity in both HG and LG groups. Contraction-induced glucose transport was nearly 2-fold (P...
Journal Articles
Journal: Diabetes
Diabetes 2002;51(5):1548–1555
Published: 01 May 2002
.... Because acetyl-CoA carboxylase (ACC) is the rate-limiting enzyme for liver fatty acid biosynthesis and a key regulator of muscle fatty acid oxidation, we examined whether ACC plays a role in the accumulation of intracellular TG. We also determined the potential role of 5′-AMP-activated protein kinase...