Identification and characterization of a novel bovine stearoyl-CoA desaturase isoform with homology to human SCD5.

Andrea J Lengi, Benjamin A Corl

Index: Lipids 42 , 499-508, (2007)

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Abstract

Stearoyl-CoA desaturase (SCD) is an enzyme responsible for the production of cis-9, trans-11 conjugated linoleic acid in ruminant fats, and for the synthesis of palmitoleoyl-CoA and oleoyl-CoA. 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 any of the described 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 the 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 five exons and four introns, and is highly expressed in the brain. In other tissues examined, mRNA expression of SCD5 was minimal. Furthermore, the expression levels of SCD5 between brain gray and white matter are not different. This is the first description of a homolog of human SCD5 in a non-primate species.