PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21887335-1 2011 BACKGROUND: Acetyl Coenzyme A carboxylase beta (ACACB) is the rate-limiting enzyme in fatty acid oxidation, and continuous fatty acid oxidation in Acacb knock-out mice increases insulin sensitivity. Fatty Acids 86-96 acetyl-Coenzyme A carboxylase beta Mus musculus 12-46 21887335-1 2011 BACKGROUND: Acetyl Coenzyme A carboxylase beta (ACACB) is the rate-limiting enzyme in fatty acid oxidation, and continuous fatty acid oxidation in Acacb knock-out mice increases insulin sensitivity. Fatty Acids 86-96 acetyl-Coenzyme A carboxylase beta Mus musculus 48-53 18845612-1 2008 The activation of AMP-activated protein kinase (AMPK) and phosphorylation/inhibition of acetyl-CoA carboxylase 2 (ACC2) is believed to be the principal pathway regulating fatty acid oxidation. Fatty Acids 171-181 acetyl-Coenzyme A carboxylase beta Mus musculus 114-118 20074529-4 2010 Here, we have used either pharmacological (administration of the AMPK agonist 5(") aminoimidazole-4-carboxamide-riboside) or genetic means (mutation of the ACC2 gene in mice) to manipulate fatty acid oxidation to determine whether this is sufficient to promote leanness. Fatty Acids 189-199 acetyl-Coenzyme A carboxylase beta Mus musculus 156-160 19156225-6 2009 Of interest is the down-regulation of fatty acid metabolism-related molecules, including acetyl-CoA carboxylase (ACC)-1, ACC-2 and fatty acid synthase in the liver of KRAP(-/-) mice, which could in part account for the metabolic phenotype in KRAP(-/-) mice. Fatty Acids 38-48 acetyl-Coenzyme A carboxylase beta Mus musculus 121-126 18487439-1 2008 The cardiac-enriched isoform of acetyl-CoA carboxylase (ACC2) is a key regulator of mitochondrial fatty acid (FA) uptake via carnitine palmitoyltransferase 1 (CPT1). Fatty Acids 98-108 acetyl-Coenzyme A carboxylase beta Mus musculus 56-60 18826455-5 2008 Further support for the lipocentric hypothesis of the pathogenesis of insulin resistance was provided by knocking out the gene coding for ACC2 in mice; this led to greater fatty acid oxidation, reduced fat mass and, in consequence, greatly enhanced insulin sensitivity. Fatty Acids 172-182 acetyl-Coenzyme A carboxylase beta Mus musculus 138-142 16622296-4 2006 Acetyl-CoA carboxylase 1 (ACC1) and ACC2 regulate fatty acid synthesis and indirectly control fatty acid oxidation via a key product, malonyl CoA. Fatty Acids 50-60 acetyl-Coenzyme A carboxylase beta Mus musculus 36-40 18239600-5 2008 The treatment also resulted in the upregulation of the mRNA levels of acetyl-CoA carboxylase 2 (ACC2), a key regulatory enzyme for mitochondrial fatty-acid oxidation in muscle. Fatty Acids 145-155 acetyl-Coenzyme A carboxylase beta Mus musculus 96-100 16622296-4 2006 Acetyl-CoA carboxylase 1 (ACC1) and ACC2 regulate fatty acid synthesis and indirectly control fatty acid oxidation via a key product, malonyl CoA. Fatty Acids 94-104 acetyl-Coenzyme A carboxylase beta Mus musculus 36-40 15968460-2 2005 Mice deficient in ACC2 have continuous fatty acid oxidation and reduced body fat and body weight, validating this enzyme as a target for drug development against obesity, diabetes and other symptoms of the metabolic syndrome. Fatty Acids 39-49 acetyl-Coenzyme A carboxylase beta Mus musculus 18-22 16103361-1 2005 Acetyl-CoA carboxylases (ACC1 and ACC2) catalyze the carboxylation of acetyl-CoA to form malonyl-CoA, an intermediate metabolite that plays a pivotal role in the regulation of fatty acid metabolism. Fatty Acids 176-186 acetyl-Coenzyme A carboxylase beta Mus musculus 34-38 16103361-2 2005 We previously reported that ACC2 null mice are viable, and that ACC2 plays an important role in the regulation of fatty acid oxidation through the inhibition of carnitine palmitoyltransferase I, a mitochondrial component of the fatty-acyl shuttle system. Fatty Acids 114-124 acetyl-Coenzyme A carboxylase beta Mus musculus 64-68 16103361-9 2005 Our previous results of the ACC2 knockout mice and current studies of ACC1 knockout mice further confirm our hypotheses that malonyl-CoA exists in two independent pools, and that ACC1 and ACC2 have distinct roles in fatty acid metabolism. Fatty Acids 216-226 acetyl-Coenzyme A carboxylase beta Mus musculus 188-192 12440973-7 2002 Knockout mice, and other approaches, suggest that the malonyl-CoA produced by ACC-2 is exclusively involved in regulation of fatty acid oxidation, whereas that produced by ACC-1 is utilized in fatty acid synthesis. Fatty Acids 125-135 acetyl-Coenzyme A carboxylase beta Mus musculus 78-83 15677334-8 2005 These findings suggest that continuous 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. Fatty Acids 39-49 acetyl-Coenzyme A carboxylase beta Mus musculus 81-85 15677334-8 2005 These findings suggest that continuous 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. Fatty Acids 39-49 acetyl-Coenzyme A carboxylase beta Mus musculus 269-273 12842871-8 2003 CP-640186 also stimulated fatty acid oxidation in C2C12 cells (ACC2) and in rat epitrochlearis muscle strips with EC50s of 57 nm and 1.3 microm. Fatty Acids 26-36 acetyl-Coenzyme A carboxylase beta Mus musculus 63-67 12920182-1 2003 Malonyl-CoA, generated by acetyl-CoA carboxylases ACC1 and ACC2, is a key metabolite in the control of fatty acid synthesis and oxidation in response to dietary changes. Fatty Acids 103-113 acetyl-Coenzyme A carboxylase beta Mus musculus 59-63 12920182-2 2003 ACC2 is associated to the mitochondria, and Acc2-/- mice have a normal lifespan and higher fatty acid oxidation rate and accumulate less fat. Fatty Acids 91-101 acetyl-Coenzyme A carboxylase beta Mus musculus 44-48 12920182-4 2003 Fatty acid oxidation rates in the soleus muscle and in hepatocytes of Acc2-/- mice were significantly higher than those of WT cohorts and were not affected by the addition of insulin. Fatty Acids 0-10 acetyl-Coenzyme A carboxylase beta Mus musculus 70-74 12920182-8 2003 These results suggest that ACC2 plays an essential role in controlling fatty acid oxidation and is a potential target in therapy against obesity and related diseases. Fatty Acids 71-81 acetyl-Coenzyme A carboxylase beta Mus musculus 27-31 33989657-2 2021 Enhancing mitochondrial long-chain fatty acid uptake by Acetyl-CoA carboxylase 2 (ACC2) deletion increases FAO and prevents cardiac dysfunction during chronic stresses, but therapeutic efficacy of this approach has not been determined. Fatty Acids 35-45 acetyl-Coenzyme A carboxylase beta Mus musculus 56-80 11283375-2 2001 Here, we show that Acc2-/- mutant mice have a normal life span, a higher fatty acid oxidation rate, and lower amounts of fat. Fatty Acids 73-83 acetyl-Coenzyme A carboxylase beta Mus musculus 19-23 11283375-4 2001 The fatty acid oxidation rate in the soleus muscle of the Acc2-/- mice was 30% higher than that of wild-type mice and was not affected by addition of insulin; however, addition of insulin to the wild-type muscle reduced fatty acid oxidation by 45%. Fatty Acids 4-14 acetyl-Coenzyme A carboxylase beta Mus musculus 58-62 33989657-2 2021 Enhancing mitochondrial long-chain fatty acid uptake by Acetyl-CoA carboxylase 2 (ACC2) deletion increases FAO and prevents cardiac dysfunction during chronic stresses, but therapeutic efficacy of this approach has not been determined. Fatty Acids 35-45 acetyl-Coenzyme A carboxylase beta Mus musculus 82-86 32592696-6 2020 ACC2 deletion had a significant impact on the global transcriptome including downregulation of the peroxisome proliferator-activated receptors (PPARs) signaling and fatty acid degradation pathways. Fatty Acids 165-175 acetyl-Coenzyme A carboxylase beta Mus musculus 0-4 32592696-7 2020 Increasing fatty acids by HFD feeding normalized expression of fatty acid degradation genes in ACC2 deficient mouse hearts to the same level as the control mice. Fatty Acids 11-22 acetyl-Coenzyme A carboxylase beta Mus musculus 95-99 32592696-7 2020 Increasing fatty acids by HFD feeding normalized expression of fatty acid degradation genes in ACC2 deficient mouse hearts to the same level as the control mice. Fatty Acids 11-21 acetyl-Coenzyme A carboxylase beta Mus musculus 95-99 27693463-3 2016 In mice with a germline cardiac-specific deletion of acetyl CoA carboxylase 2 (ACC2), systolic dysfunction induced by pressure-overload was prevented by maintaining cardiac fatty acid oxidation (FAO). Fatty Acids 173-183 acetyl-Coenzyme A carboxylase beta Mus musculus 53-77 32256446-12 2020 Of particular interest was the finding that room temperature housing reduced, whereas propranolol increased, expression of the gene for acetyl-CoA carboxylase (Acacb), the rate-limiting step for fatty acid synthesis and a key regulator of beta-oxidation. Fatty Acids 195-205 acetyl-Coenzyme A carboxylase beta Mus musculus 136-158 32256446-12 2020 Of particular interest was the finding that room temperature housing reduced, whereas propranolol increased, expression of the gene for acetyl-CoA carboxylase (Acacb), the rate-limiting step for fatty acid synthesis and a key regulator of beta-oxidation. Fatty Acids 195-205 acetyl-Coenzyme A carboxylase beta Mus musculus 160-165 29684438-6 2018 Moreover, increased rigidity of the actin cytoskeleton in mice on HFD induced mRNA expression of Acc1, Acc2, Fasn, and Lipe, key genes involved in fatty acid metabolism in the liver. Fatty Acids 147-157 acetyl-Coenzyme A carboxylase beta Mus musculus 103-107 32663458-5 2020 ACC2 hydroxylation occurs in conditions of high energy and represses fatty acid oxidation. Fatty Acids 69-79 acetyl-Coenzyme A carboxylase beta Mus musculus 0-4 29433631-2 2018 AMPK inhibits fatty acid synthesis and promotes fatty acid oxidation by phosphorylation of acetyl-CoA carboxylase (ACC) 1 at Ser79 and ACC2 at Ser212. Fatty Acids 48-58 acetyl-Coenzyme A carboxylase beta Mus musculus 135-139 29175182-6 2018 N-3 PUFA-deficient diet increased hepatic lipid droplets accumulation and expression of genes promoting fatty acid synthesis: Acaca, Acacb, and Scd1. Fatty Acids 104-114 acetyl-Coenzyme A carboxylase beta Mus musculus 133-138 29175182-7 2018 DE further increased the plasma leptin and the expression of fatty acid synthesis-related genes: Acacb, Fasn, and Scd1. Fatty Acids 61-71 acetyl-Coenzyme A carboxylase beta Mus musculus 97-102 27693463-3 2016 In mice with a germline cardiac-specific deletion of acetyl CoA carboxylase 2 (ACC2), systolic dysfunction induced by pressure-overload was prevented by maintaining cardiac fatty acid oxidation (FAO). Fatty Acids 173-183 acetyl-Coenzyme A carboxylase beta Mus musculus 79-83 26156967-2 2015 An important regulator of fatty acid oxidation is acetyl-CoA carboxylase (ACC), which exists as two isoforms (ACC1 and ACC2) with ACC2 predominating in skeletal muscle. Fatty Acids 26-36 acetyl-Coenzyme A carboxylase beta Mus musculus 119-123 27643638-4 2016 We describe the ability of ND-646-an allosteric inhibitor of the ACC enzymes ACC1 and ACC2 that prevents ACC subunit dimerization-to suppress fatty acid synthesis in vitro and in vivo. Fatty Acids 142-152 acetyl-Coenzyme A carboxylase beta Mus musculus 86-90 26668208-1 2016 An important regulator of fatty acid oxidation (FAO) is the allosteric inhibition of CPT-1 by malonyl-CoA produced by the enzyme acetyl-CoA carboxylase 2 (ACC2). Fatty Acids 26-36 acetyl-Coenzyme A carboxylase beta Mus musculus 129-153 26668208-1 2016 An important regulator of fatty acid oxidation (FAO) is the allosteric inhibition of CPT-1 by malonyl-CoA produced by the enzyme acetyl-CoA carboxylase 2 (ACC2). Fatty Acids 26-36 acetyl-Coenzyme A carboxylase beta Mus musculus 155-159 26043180-2 2015 PRKA stimulates FAO by phosphorylating and inactivating acetyl CoA carboxylase (ACAC; formerly ACC), leading to decreased malonyl CoA levels and augmenting fatty-acid transport into mitochondria. Fatty Acids 156-166 acetyl-Coenzyme A carboxylase beta Mus musculus 80-84 26156967-5 2015 In resting muscle the activation of AMPK with AICAR leads to increased phosphorylation of ACC (S79 on ACC1 and S221 on ACC2), which reduces ACC activity and malonyl-CoA; effects associated with increased fatty acid oxidation. Fatty Acids 204-214 acetyl-Coenzyme A carboxylase beta Mus musculus 119-123 26156967-8 2015 We find that surprisingly, ACC2-KI mice had normal exercise capacity and whole-body fatty acid oxidation during treadmill running despite elevated muscle ACC2 activity and malonyl-CoA. Fatty Acids 84-94 acetyl-Coenzyme A carboxylase beta Mus musculus 27-31 26156967-2 2015 An important regulator of fatty acid oxidation is acetyl-CoA carboxylase (ACC), which exists as two isoforms (ACC1 and ACC2) with ACC2 predominating in skeletal muscle. Fatty Acids 26-36 acetyl-Coenzyme A carboxylase beta Mus musculus 130-134 24913514-3 2014 Phosphorylation of acetyl-CoA carboxylase 2 (ACC2) at S221 (S212 in mice) by AMPK reduces ACC activity and malonyl-CoA content but the importance of the AMPK-ACC2-malonyl-CoA pathway in controlling fatty acid metabolism and insulin sensitivity is not understood; therefore, we characterised Acc2 S212A knock-in (ACC2 KI) mice. Fatty Acids 198-208 acetyl-Coenzyme A carboxylase beta Mus musculus 45-49 24913514-5 2014 RESULTS: ACC2 KI mice were resistant to increases in skeletal muscle fatty acid oxidation elicited by AICAR. Fatty Acids 69-79 acetyl-Coenzyme A carboxylase beta Mus musculus 9-13 24913514-0 2014 AMPK phosphorylation of ACC2 is required for skeletal muscle fatty acid oxidation and insulin sensitivity in mice. Fatty Acids 61-71 acetyl-Coenzyme A carboxylase beta Mus musculus 24-28 22532389-0 2012 Inhibition of acetyl-CoA carboxylase 2 enhances skeletal muscle fatty acid oxidation and improves whole-body glucose homeostasis in db/db mice. Fatty Acids 64-74 acetyl-Coenzyme A carboxylase beta Mus musculus 14-38 22532389-2 2012 Acetyl-CoA carboxylase 2 (ACC2) is a key regulatory enzyme controlling skeletal muscle mitochondrial fatty acid oxidation; inhibition of ACC2 results in enhanced oxidation of lipids. Fatty Acids 101-111 acetyl-Coenzyme A carboxylase beta Mus musculus 0-24 22532389-2 2012 Acetyl-CoA carboxylase 2 (ACC2) is a key regulatory enzyme controlling skeletal muscle mitochondrial fatty acid oxidation; inhibition of ACC2 results in enhanced oxidation of lipids. Fatty Acids 101-111 acetyl-Coenzyme A carboxylase beta Mus musculus 26-30 22532389-2 2012 Acetyl-CoA carboxylase 2 (ACC2) is a key regulatory enzyme controlling skeletal muscle mitochondrial fatty acid oxidation; inhibition of ACC2 results in enhanced oxidation of lipids. Fatty Acids 101-111 acetyl-Coenzyme A carboxylase beta Mus musculus 137-141