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PHD3 (zeige EGLN3 ELISA Kits) loss in cancer enables metabolic reliance on fatty acid oxidation via deactivation of ACC2.
Inhibition of Acetyl-CoA Carboxylase 1 (ACC1 (zeige ACACA ELISA Kits)) 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 (zeige APOE ELISA Kits) 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 (zeige AGTR1 ELISA Kits) gene (rs5186) confers the risk of diabetic nephropathy in Asian Indian patients with T2DM.
A gene polymorphism in acetyl-coenzyme A carboxylase beta may be associated with the C-reactive protein (zeige CRP ELISA Kits) 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
The excess of ACCbeta might contribute to exacerbation of podocyte injury in the kidney of an animal model for diabetes mellitus, and the AMPK (zeige PRKAA1 ELISA Kits)/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 (zeige CD8A ELISA Kits)+ T cell responses.
AMPK (zeige PRKAA1 ELISA Kits)-dependent inactivation of ACC (zeige ACACA ELISA Kits) is not essential for the control of myocardial FAO and subsequent cardiac function during a variety of conditions involving AMPK (zeige PRKAA1 ELISA Kits)-independent and AMPK (zeige PRKAA1 ELISA Kits)-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 (zeige LEPR ELISA Kits) 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 (zeige INS ELISA Kits) sensitivity and leaner (zeige CACNA1A ELISA Kits) Acc2-/- mutant mice.
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