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Volume 272, Number 52, Issue of December 26, 1997
pp. 33125-33131
(Received for publication, November 14, 1996, and in revised form, September 4, 1997)
From the Department of Biochemistry, School of Medicine and
Biomedical Sciences, State University of New York at Buffalo,
Buffalo, New York 14214
We report a mouse cDNA that encodes a
317-amino acid short-chain dehydrogenase which recognizes as substrates
9-cis-retinol, 11-cis-retinol,
5
cDNA Cloning and Characterization of a
cis-Retinol/3
-Hydroxysterol Short-chain
Dehydrogenase
-androstan-3,17
-diol, and 5-androstan-3-ol-17-one. This
cis-retinol/androgen dehydrogenase (CRAD) shares closest amino acid similarity with mouse retinol dehydrogenase isozymes types 1 and 2 (86 and 91%, respectively). Recombinant CRAD uses NAD+ as its preferred cofactor and exhibits cooperative
kinetics for cis-retinoids, but Michaelis-Menten kinetics
for 3-hydroxysterols. Unlike recombinant retinol dehydrogenase
isozymes, recombinant CRAD was inhibited by 4-methylpyrazole, was not
stimulated by ethanol, and did not require phosphatidylcholine for
optimal activity. CRAD mRNA was expressed intensely in kidney and
liver, in contrast to retinol dehydrogenase isozymes, which show strong
mRNA expression only in liver. CRAD mRNA expression was
widespread (relative abundance): kidney (100) > liver (92) > small
intestine (9) = heart (9) > retinal pigment epithelium and sclera
(4.5) > brain (2) > retina and vitreous (1.6) > spleen (0.7) > testis (0.6) > lung (0.4). CRAD may catalyze the first step in an
enzymatic pathway from 9-cis-retinol to generate the
retinoid X receptor ligand 9-cis-retinoic acid and/or may
regenerate dihydrotestosterone from its catabolite 5-androstan-3,17-diol. These data also illustrate the
multifunctional nature of short-chain dehydrogenases and provide a
potential mechanism for androgen-retinoid interactions.
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