title: Identification of a second human acetyl-CoA carboxylase gene.
abstract: Acetyl-CoA carboxylase (ACC), an important enzyme in fatty acid biosynthesis and a regulator of fatty acid oxidation, is present in at least two isoenzymic forms in rat and human tissues. Previous work has established the existence of a 265,000 Da enzyme in both the rat and human (RACC265; HACC265) and a higher-molecular-mass species (275,000-280,000 Da) in the same species (RACC280; HACC275). An HACC265 gene has previously been localized to chromosome 17. 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. The gene encoding this isoenzymic form of ACC has been localized to the long arm of human chromosome 12. Thus, ACC is represented in a multigene family in both rodents and humans. The newly discovered human gene and its rat homologue appear to be under different regulatory control to the HACC265 gene, as judged by tissue-specific expression in vivo and by independent modulation in cultured cells in vitro.
authors.affiliation: Department of Medicine, Dartmouth Medical School, Hanover NH 03755, USA.
authors.forename: J
authors.initials: J
authors.lastname: Widmer
authors.forename: K S
authors.initials: KS
authors.lastname: Fassihi
authors.forename: S C
authors.initials: SC
authors.lastname: Schlichter
authors.forename: K S
authors.initials: KS
authors.lastname: Wheeler
authors.forename: B E
authors.initials: BE
authors.lastname: Crute
authors.forename: N
authors.initials: N
authors.lastname: King
authors.forename: N
authors.initials: N
authors.lastname: Nutile-McMenemy
authors.forename: W W
authors.initials: WW
authors.lastname: Noll
authors.forename: S
authors.initials: S
authors.lastname: Daniel
authors.forename: J
authors.initials: J
authors.lastname: Ha
authors.forename: K H
authors.initials: KH
authors.lastname: Kim
authors.forename: L A
authors.initials: LA
authors.lastname: Witters
mesh_terms: D000103:Acetyl-CoA Carboxylase / Q000096:biosynthesis* / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002454:Cell Differentiation; D002460:Cell Line; D002874:Chromosome Mapping; D002881:Chromosomes, Human, Pair 12; D002886:Chromosomes, Human, Pair 17; D002995:Clofibric Acid / Q000031:analogs & derivatives / Q000494:pharmacology; D006224:Cricetinae; D004790:Enzyme Induction / Q000187:drug effects; D058607:Fibric Acids; D005947:Glucose / Q000494:pharmacology; D006801:Humans; D007527:Isoenzymes / Q000096:biosynthesis / Q000235:genetics*; D008114:Liver Neoplasms, Experimental; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000096:biosynthesis; D051381:Rats; D017386:Sequence Homology, Amino Acid; D014158:Transcription, Genetic
chemical_list: D058607:Fibric Acids; D007527:Isoenzymes; D012333:RNA, Messenger; D002995:Clofibric Acid; D000103:Acetyl-CoA Carboxylase; C019304:ciprofibrate; D005947:Glucose