J. Lipid Res.
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A more recent version of this article appeared on March 1, 2003

Papers In Press, published online ahead of print December 1, 2002
J. Lipid Res., doi:10.1194/jlr.M200399-JLR200
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Submitted on October 9, 2002
Revised on November 19, 2002
Accepted on November 19, 2002

A cluster of eight hydroxysteroid dehydrogenase genes belonging to the Aldo-keto reductase supergene family on mouse chromosome 13

Laurent Vergnes, Jack Phan, Andrew Stolz, and Karen Reue

Medicine/VAGLAHS, UCLA, Los Angeles, CA 90073

Corresponding Author: Reuek{at}ucla.edu

A subclass of Hydroxysteroid Dehydrogenases (HSD) are NADP(H)-dependent oxidoreductases that belong to the Aldo-Keto Reductase (AKR) superfamily. They are involved in pre-receptor or intracrine steroid modulation, able to activate and inactivate potent steroid hormones and also act as bile acid-binding proteins. The HSD protein family members characterized thus far in human and rat have a high degree of protein sequence similarity but exhibit distinct substrate specificities. Here we report the identification of nine murine AKR genes in a cluster on chromosome 13 by a combination of molecular cloning and in silico analysis of this region. These include four previously isolated mouse HSD genes (Akr1c18, Akr1c6, Akr1c12, Akr1c13), the more distantly related Akr1e1, and four novel HSD genes. These genes exhibit highly conserved exon/intron organization and protein sequence predictions indicate 75% amino acid similarity. The previously identified AKR protein active site residues (Asp-50, Tyr-55, Lys-84, His-117) are invariant among all nine proteins, but differences are observed in regions that have been implicated in determining substrate specificity. Differences are also observed in tissue expression patterns, with expression of some genes restricted to specific tissues (i.e., liver or kidney and spleen) and others expressed at high levels in multiple tissues. Finally, we detected a novel alternative mRNA splice form for Akr1c12 that results in production of a truncated protein, suggesting that mRNA processing may be a previously unrecognized mechanism to modulate HSD enzyme activity. Our findings dramatically expand the repertoire of AKR genes and identify unrecognized family members with potential roles in the regulation of steroid metabolism.


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