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A Novel Short-Chain Alcohol Dehydrogenase from Rats with Retinol Dehydrogenase Activity, Cyclically Expressed in Uterine Epithelium¹

^a Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232

Retinoic acid is necessary for the maintenance of many lining epithelia of the body, such as the epithelium of the luminal surface of the uterus. Administration of estrogen to prepubertal rats induces in these epithelial cells the ability to synthesize retinoic acid from retinol, coincident with the appearance of cellular retinoic acid-binding protein, type two, which is normally present in these cells only at estrus in the mature, cycling animal. Here, we report the isolation, from a cDNA library prepared from uterine mRNA collected at the estrous stage and from a rat mammary adenocarcinoma cell line, of a cDNA that encodes a novel retinol dehydrogenase. A member of the short-chain alcohol dehydrogenase family, the encoded enzyme was capable of metabolizing retinol to retinal when expressed in cells after transfection of its cDNA. When cotransfected with the cDNA of human aldehyde 6, a known retinaldehyde dehydrogenase, the transfected cells synthesized retinoic acid from retinol. Immunohistochemical analysis revealed that the protein was present in the uterine lining epithelium of the mature animal only at estrus, coincident with the presence of cellular retinol-binding protein and cellular retinoic acid-binding protein, type two. Consequently, this novel short-chain alcohol dehydrogenase is an excellent candidate for the retinol dehydrogenase that catalyzes the first step in retinoic acid biosynthesis that occurs in uterine epithelial cells.

¹ Supported in part by grants DK32642 and HD25206. B.R. was supported by USPHS training grant HD 07043. Core facilities used were from the Clinical Nutrition Research Unit (protein and immunology core), the Diabetes Center (oligo synthesis), and the Vanderbilt-Ingram Cancer Center (DNA sequencing), supported by NIH grants DK 26657, DK 20593, and CA 68485, respectively. The sequence described in this paper has been submitted to GenBank with accession number AF337953.

² Correspondence: David E. Ong, Department of Biochemistry, Vanderbilt University School of Medicine, 610 MRB, 23rd Ave. at Pierce, Nashville, TN 37232-0146. FAX: 615 343 7347; david.e.ong{at}vanderbilt.edu

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