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Results suggest that the genomes uncoupled 1 (GUN1) and genomes uncoupled 5 (GUN5)-involved plastid-to-nucleus retrograde communication played a role in regulating acetyl-CoA carboxylase 2 (ACC2).
Results identified ACC2 amino acid mutations affecting specific inhibition of the isozyme by compound CD-017-0191. They form two clusters separated by 60-90 A: one located in the vicinity of the BC active site and the other one in the vicinity of the ACC1 phosphorylation sites in the central domain, suggesting a contribution of the interface of two ACC dimers in the polymer to the inhibitor binding site.
Targeted analysis of DNA methylation array revealed the mesenchymal stem cells in infants born to obese mothers had hypermethylation in genes regulating Fatty Acid Oxidation (PRKAG2, ACC2, CPT1A, SDHC) and corresponding lower mRNA content of these genes. Moreover, mesenchymal stem cells methylation was positively correlated with infant adiposity.
ACC2 gene (ACACB) expression was decreased by 25% in HCC tissue compared to non-cancerous liver tissue.
of ACCs decreased polyunsaturated fatty acid (PUFA) concentrations in liver due to reduced malonyl-CoA, which is required for elongation of essential fatty acids.
PHD3 loss in cancer enables metabolic reliance on fatty acid oxidation via deactivation of ACC2.
Inhibition of Acetyl-CoA Carboxylase 1 (ACC1) and 2 (ACC2) Reduces Proliferation and De Novo Lipogenesis of EGFRvIII Human Glioblastoma Cells
Cetuximab-mediated activation of AMPK and subsequent phosphorylation and inhibition of ACC is followed by a compensatory increase in total ACC, which rewires cancer metabolism from glycolysis-dependent to lipogenesis-dependent.
A significant association exists of ACACB gene polymorphism and diabetic nephropathy among Caucasian patients with diabetes.
Our meta-analysis supports that the apolipoprotein E epsilon2 allele and acetyl-CoA carboxylase beta rs2268388 C>T might act as promotion factors of nephropathy in type 2 diabetes.
The knockdown of ACC2 reduced palmitic acid -induced autophagy and thus protects the cells from palmitic acid - induced lipotoxicity with attenuated lipid accumulation and rescued cell viability.
These data support a role for ACACB in obesity and potential roles for altered lipid metabolism in susceptibility to diabetic nephropathy.
TT genotypes of ACACB gene (rs2268388) and CC genotype of AGTR1 gene (rs5186) confers the risk of diabetic nephropathy in Asian Indian patients with T2DM.
Its involvement in the development of diabetic nephropathy is explained by the promotion of the so-called micro-inflammation associated with the diabetic state.
A gene polymorphism in acetyl-coenzyme A carboxylase beta may be associated with the C-reactive protein level in a prediabetic and diabetic population.
In conclusion, common polymorphisms of ACACB gene are associated with obesity and, independently, with type 2 diabetes in postmenopausal women
Common variants within the ACACB locus appear to regulate adipose gene expression
Structure-guided inhibitor design for human acetyl-coenzyme A carboxylase by interspecies active site conversion.
The acetyl-coenzyme A carboxylase beta (ACACB) gene is associated with nephropathy in Chinese patients with type 2 diabetes.
Acetyl-CoA carboxylase beta (ACC2) plays a key role in fatty acid synthesis and oxidation pathways.
The -368 C/T single-nucleotide polymorphism in ACACB P-II binds HepG2 nuclear proteins that affect promoter activity in an allele-specific fashion.
Using mice with Ser(79)Ala/Ser(212)Ala knock-in mutations (ACC DKI) the authors find that inhibition of ACC phosphorylation leads to reduced appetite in response to fasting or cold exposure.
AMPK-ACC signaling is coupled to the control of thrombosis by specifically modulating thromboxane and granule release in response to collagen.
Findings suggest that ACC2 deletion leads to intramyocellular lipid reduction without suppressing glucose use via an elevation in acetyl-CoA metabolism even under high-fat diet conditions and offer new mechanistic insight into the therapeutic potential of ACC2 inhibition on insulin resistance.
Lipogenesis is dispensable for liver tumorigenesis in mice treated with diethylnitrosamine, and ACC enzymes have an important role in redox regulation and cell survival.
The excess of ACCbeta might contribute to exacerbation of podocyte injury in the kidney of an animal model for diabetes mellitus, and the AMPK/ACCbeta pathway may be a novel therapeutic target for the prevention of diabetes-related podocyte injury.
These results suggest that ACC2 is dispensable for CD8+ T cell responses.
AMPK-dependent inactivation of ACC is not essential for the control of myocardial FAO and subsequent cardiac function during a variety of conditions involving AMPK-independent and AMPK-dependent metabolic adaptations.
Data show that acetyl CoA carboxylase 2 ACC2 deletion led to a significant reduction in cardiac malonyl CoA levels.
Inhibition of acetyl-CoA carboxylase 2 enhances skeletal muscle fatty acid oxidation and improves whole-body glucose homeostasis in db/db mice.
the ACC2 deletion protects against fatty liver, despite increased de novo lipogenesis and a diet that induces obesity, fatty liver, and diabetes.
Acc2 does not have a major role in regulating body weight, fat mass, or food intake
ACC2 plays an essential role in controlling fatty acid oxidation and is a potential target in therapy against obesity and related diseases.
Fatty acid oxidation in the adipocytes of Acc2-/- mutant mice, combined with a higher level of glucose oxidation and a higher rate of lipolysis, are major factors leading to efficient maintenance of insulin sensitivity and leaner Acc2-/- mutant mice.
Acc2(-/-) mice were protected from fat-induced peripheral and hepatic insulin resistance.
Report reduced heart size and increased myocardial fuel substrate oxidation in ACC2 mutant mice.
Data suggest that the ability of SREBP-1a to activate hepatic ACC2 to a greater extent than SREBP-1c must relate to more efficient recruitment of transcriptional coactivators to the more potent SREBP-1a activation domain.
Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. ACC-beta is thought to control fatty acid oxidation by means of the ability of malonyl-CoA to inhibit carnitine-palmitoyl-CoA transferase I, the rate-limiting step in fatty acid uptake and oxidation by mitochondria. ACC-beta may be involved in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. There is evidence for the presence of two ACC-beta isoforms.
, acetyl-CoA carboxylase 2
, acetyl-Coenzyme A carboxylase beta
, acetyl-Coenzyme A carboxylase 2