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Gene Review

ACACB  -  acetyl-CoA carboxylase beta

Homo sapiens

Synonyms: ACC-beta, ACC2, ACCB, Acetyl-CoA carboxylase 2, HACC275
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Disease relevance of ACACB

  • A fragment of ACC-beta cDNA was expressed in Escherichia coli and antibodies against the peptide were generated to establish that the cDNA sequence that we cloned is that for ACC-beta [1].
  • Employing quantitative real-time PCR, we determined that expression of mitochondrial acetyl-CoA carboxylase 2 (ACC2) was increased by 50% with obesity (P < 0.05) [2].
  • These findings indicate that LKB1 plays a crucial role in regulating AMPKalpha2 activation and acetyl-CoA carboxylase-2 phosphorylation and also regulating cellular energy levels in response to ischemia [3].
  • Increases (P < 0.05) in AMPK activity, AMPKalpha Thr(172) phosphorylation, ACCbeta Ser(221) phosphorylation, free AMP content, and glucose clearance were more influenced by the absolute than by the relative exercise intensity, being greatest in 73% Normoxia with no difference between 51% Normoxia and 72% Hypoxia [4].
  • 2. Based on the study of human tissue and human-derived breast cancer cell lines by enzyme isolation and protein blotting techniques, we have now identified two human isoforms of M(r) 265,000 (HACC 265) and 275,000 (HACC 275), each of which is homologous to one of the rat isozymes [5].

High impact information on ACACB

  • Consistent with the in vivo response, adenovirus-directed expression of PGC-1alpha in C2C12 muscle cells provoked the phosphorylation/inactivation and reduced expression of acetyl-CoA carboxylase 2, causing a reduction of the malonyl-CoA concentration [6].
  • These analyses demonstrated that ACC1 is a cytosolic protein and that ACC2 was associated with the mitochondria, a finding that was confirmed further by the immunocolocalization of a known human mitochondria-specific protein and the carnitine palmitoyltransferase 1 [7].
  • The association of ACC2 with the mitochondria is consistent with the hypothesis that ACC2 is involved in the regulation of mitochondrial fatty acid oxidation through the inhibition of carnitine palmitoyltransferase 1 by its product malonyl-CoA [7].
  • The predicted amino acid sequence of ACC2 contains an additional 136 aa relative to ACC1, 114 of which constitute the unique N-terminal sequence of ACC2 [7].
  • The sequence of amino acid residues 1-20 of ACC2 is highly hydrophobic, suggesting that it is a leader sequence that targets ACC2 for insertion into membranes [7].

Biological context of ACACB

  • Assignment of acetyl-CoA carboxylase-beta (ACACB) to human chromosome band 12q24.1 by in situ hybridization [8].
  • In this study we report the complete amino acid sequence and unique features of an isoform of ACC with a molecular mass of 275 kDa (ACC-beta), which is primarily expressed in heart and skeletal muscles [1].
  • Human ACC-beta cDNA has an open reading frame of 7,343 bases, encoding a protein of 2,458 amino acids, with a calculated molecular mass of 276,638 Da [1].
  • In this study, we revealed that ACCbeta expression in liver is markedly stimulated by food intake at the transcriptional level [9].
  • In the present study, we report cloning of a partial-length human cDNA sequence which appears to correspond to HACC275 and its rat homologue, RACC280, as judged by mRNA tissue distribution and cell-specific regulation of mRNA/protein expression [10].

Anatomical context of ACACB


Associations of ACACB with chemical compounds


Regulatory relationships of ACACB

  • Moreover, transient expression of Myf6 induced significant activation on the ACCbeta promoter or an artificial promoter harboring this novel cis-element [19].
  • USF1-induced ACCbeta promoter responsiveness was markedly attenuated when co-transfecting cardiomyocytes with a -93/+65 or -38/+65 promoter deletion construct (lacking E-boxes 1-3) [12].

Other interactions of ACACB


Analytical, diagnostic and therapeutic context of ACACB


  1. Cloning of human acetyl-CoA carboxylase-beta and its unique features. Ha, J., Lee, J.K., Kim, K.S., Witters, L.A., Kim, K.H. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  2. Expression of genes regulating Malonyl-CoA in human skeletal muscle. Pender, C., Trentadue, A.R., Pories, W.J., Dohm, G.L., Houmard, J.A., Youngren, J.F. J. Cell. Biochem. (2006) [Pubmed]
  3. Deficiency of LKB1 in heart prevents ischemia-mediated activation of AMPK{alpha}2 but not AMPK{alpha}1. Sakamoto, K., Zarrinpashneh, E., Budas, G.R., Pouleur, A.C., Dutta, A., Prescott, A.R., Vanoverschelde, J.L., Ashworth, A., Jovanovic, A., Alessi, D.R., Bertrand, L. Am. J. Physiol. Endocrinol. Metab. (2006) [Pubmed]
  4. Effect of exercise intensity and hypoxia on skeletal muscle AMPK signaling and substrate metabolism in humans. Wadley, G.D., Lee-Young, R.S., Canny, B.J., Wasuntarawat, C., Chen, Z.P., Hargreaves, M., Kemp, B.E., McConell, G.K. Am. J. Physiol. Endocrinol. Metab. (2006) [Pubmed]
  5. Identification of human acetyl-CoA carboxylase isozymes in tissue and in breast cancer cells. Witters, L.A., Widmer, J., King, A.N., Fassihi, K., Kuhajda, F. Int. J. Biochem. (1994) [Pubmed]
  6. Hypothalamic malonyl-CoA triggers mitochondrial biogenesis and oxidative gene expression in skeletal muscle: Role of PGC-1{alpha}. Cha, S.H., Rodgers, J.T., Puigserver, P., Chohnan, S., Lane, M.D. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  7. The subcellular localization of acetyl-CoA carboxylase 2. Abu-Elheiga, L., Brinkley, W.R., Zhong, L., Chirala, S.S., Woldegiorgis, G., Wakil, S.J. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  8. Assignment of acetyl-CoA carboxylase-beta (ACACB) to human chromosome band 12q24.1 by in situ hybridization. Ullrich, C.K., Widmer, J., Park, J.P., Mohandas, T.K., Witters, L.A. Cytogenet. Cell Genet. (1997) [Pubmed]
  9. Acetyl-CoA carboxylase beta gene is regulated by sterol regulatory element-binding protein-1 in liver. Oh, S.Y., Park, S.K., Kim, J.W., Ahn, Y.H., Park, S.W., Kim, K.S. J. Biol. Chem. (2003) [Pubmed]
  10. Identification of a second human acetyl-CoA carboxylase gene. Widmer, J., Fassihi, K.S., Schlichter, S.C., Wheeler, K.S., Crute, B.E., King, N., Nutile-McMenemy, N., Noll, W.W., Daniel, S., Ha, J., Kim, K.H., Witters, L.A. Biochem. J. (1996) [Pubmed]
  11. Impaired activation of AMP-kinase and fatty acid oxidation by globular adiponectin in cultured human skeletal muscle of obese type 2 diabetics. Chen, M.B., McAinch, A.J., Macaulay, S.L., Castelli, L.A., O'brien, P.E., Dixon, J.B., Cameron-Smith, D., Kemp, B.E., Steinberg, G.R. J. Clin. Endocrinol. Metab. (2005) [Pubmed]
  12. Upstream stimulatory factor 1 transactivates the human gene promoter of the cardiac isoform of acetyl-CoA carboxylase. Makaula, S., Adam, T., Essop, M.F. Arch. Biochem. Biophys. (2006) [Pubmed]
  13. Roles of acetyl-CoA carboxylase beta in muscle cell differentiation and in mitochondrial fatty acid oxidation. Lee, J.K., Kim, K.H. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  14. Expression, purification, and characterization of human and rat acetyl cfenzyme A carboxylase (ACC) isozymes. Cheng, D., Chu, C.H., Chen, L., Feder, J.N., Mintier, G.A., Wu, Y., Cook, J.W., Harpel, M.R., Locke, G.A., An, Y., Tamura, J.K. Protein Expr. Purif. (2007) [Pubmed]
  15. Decreased muscle acetyl-coenzyme A carboxylase 2 mRNA and insulin resistance in formerly obese subjects. Rosa, G., Manco, M., Vega, N., Greco, A.V., Castagneto, M., Vidal, H., Mingrone, G. Obes. Res. (2003) [Pubmed]
  16. Metformin increases AMP-activated protein kinase activity in skeletal muscle of subjects with type 2 diabetes. Musi, N., Hirshman, M.F., Nygren, J., Svanfeldt, M., Bavenholm, P., Rooyackers, O., Zhou, G., Williamson, J.M., Ljunqvist, O., Efendic, S., Moller, D.E., Thorell, A., Goodyear, L.J. Diabetes (2002) [Pubmed]
  17. AMP-activated protein kinase is not down-regulated in human skeletal muscle of obese females. Steinberg, G.R., Smith, A.C., Van Denderen, B.J., Chen, Z., Murthy, S., Campbell, D.J., Heigenhauser, G.J., Dyck, D.J., Kemp, B.E. J. Clin. Endocrinol. Metab. (2004) [Pubmed]
  18. Role of 5'AMP-activated protein kinase in glycogen synthase activity and glucose utilization: insights from patients with McArdle's disease. Nielsen, J.N., Wojtaszewski, J.F., Haller, R.G., Hardie, D.G., Kemp, B.E., Richter, E.A., Vissing, J. J. Physiol. (Lond.) (2002) [Pubmed]
  19. Cloning of human acetyl-CoA carboxylase beta promoter and its regulation by muscle regulatory factors. Lee, J.J., Moon, Y.A., Ha, J.H., Yoon, D.J., Ahn, Y.H., Kim, K.S. J. Biol. Chem. (2001) [Pubmed]
  20. Evaluation of fatty acid metabolism-related gene expression in nonalcoholic fatty liver disease. Nakamuta, M., Kohjima, M., Morizono, S., Kotoh, K., Yoshimoto, T., Miyagi, I., Enjoji, M. Int. J. Mol. Med. (2005) [Pubmed]
  21. Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise. Wojtaszewski, J.F., Mourtzakis, M., Hillig, T., Saltin, B., Pilegaard, H. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  22. The effect of a 3-month low-intensity endurance training program on fat oxidation and acetyl-CoA carboxylase-2 expression. Schrauwen, P., van Aggel-Leijssen, D.P., Hul, G., Wagenmakers, A.J., Vidal, H., Saris, W.H., van Baak, M.A. Diabetes (2002) [Pubmed]
  23. Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms. Abu-Elheiga, L., Almarza-Ortega, D.B., Baldini, A., Wakil, S.J. J. Biol. Chem. (1997) [Pubmed]
  24. Predominant {alpha}2/{beta}2/{gamma}3 AMPK activation during exercise in human skeletal muscle. Birk, J.B., Wojtaszewski, J.F. J. Physiol. (Lond.) (2006) [Pubmed]
  25. Progressive increase in human skeletal muscle AMPKalpha2 activity and ACC phosphorylation during exercise. Stephens, T.J., Chen, Z.P., Canny, B.J., Michell, B.J., Kemp, B.E., McConell, G.K. Am. J. Physiol. Endocrinol. Metab. (2002) [Pubmed]
  26. Lifestyle changes and lipid metabolism gene expression and protein content in skeletal muscle of subjects with impaired glucose tolerance. Mensink, M., Blaak, E.E., Vidal, H., De Bruin, T.W., Glatz, J.F., Saris, W.H. Diabetologia (2003) [Pubmed]
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