Identification of a second human acetyl-CoA carboxylase gene

Author:

WIDMER Jane1,FASSIHI Katherine S.1,SCHLICHTER Susannah C.1,WHEELER Kate S.1,CRUTE Barbara E.1,KING Nicole1,NUTILE-McMENEMY Nancy1,NOLL Walter W.1,DANIEL Samira2,HA Joohun2,KIM Ki-Han2,WITTERS Lee A.1

Affiliation:

1. Departments of Medicine, Biochemistry and Pathology, Dartmouth Medical School, Hanover, NH 03755, U.S.A.

2. Department of Biochemistry, Purdue University, West Lafayette, IN 47907, U.S.A.

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 265000 Da enzyme in both the rat and human (RACC265; HACC265) and a higher-molecular-mass species (275000–280000 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.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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