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Identification and characterization of a novel bovine stearoyl‐CoA desaturase isoform with homology to human SCD5
Author(s) -
Lengi Andrea,
A Benjamin
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a701-b
Subject(s) - gene isoform , stearoyl coa desaturase , biology , exon , biochemistry , oleic acid , amino acid , gene , peptide sequence , homology (biology) , conserved sequence , conjugated linoleic acid , intron , transmembrane domain , fatty acid , linoleic acid , fatty acid desaturase , enzyme , genetics , polyunsaturated fatty acid , gene expression
Stearoyl‐CoA desaturase (SCD) is an enzyme responsible for the production cis ‐9, trans ‐11 conjugated linoleic acid in ruminants, and for the synthesis of palmitoleic and oleic acids. To date, only one SCD isoform has been described in ruminant species, although multiple isoforms have been found in many other mammalian species. In this paper, we describe for the first time a second SCD isoform in cattle, which appears to be an ortholog of human SCD5 rather than a homolog of bovine SCD1 or the murine SCD isoforms. As described in other SCD proteins, the predicted amino acid sequence of bovine SCD5 includes four transmembrane domains and three conserved histidine motifs. The amino‐terminus of the predicted protein sequence of SCD5 lacks PEST sequences typically found in SCD1 homologs, which are thought to target proteins for rapid degradation. Similar to human SCD5 , the bovine SCD5 gene is organized into 5 exons and four introns, and is highly expressed in the brain indicating a possible role in the control of non‐lipogenic tissue fatty acid metabolism. This is the first description of a homolog of human SCD5 in a non‐primate species. Supported by the Virginia Agricultural Experiment Station.