Molecular cloning of rat liver 3α-hydroxysteroid dehydrogenase and identification of structurally related proteins from rat lung and kidney
- PMID: 22217852
- DOI: 10.1016/0960-0760(92)90335-G
Molecular cloning of rat liver 3α-hydroxysteroid dehydrogenase and identification of structurally related proteins from rat lung and kidney
Abstract
3α-Hydroxysteroid dehydrogenase and related enzymes play important roles in the metabolism of endogenous compounds including androgens, corticosteroid, prostaglandins and bile acids, as well as drugs and xenobiotics such as benzo(a)pyrene. Complementary DNA clones encoding 3α-hydroxysteroid dehydrogenase were isolated from a rat liver cDNA lambda gt11 expression library using monoclonal antibodies as probes. A full-length cDNA clone of 1286 base pairs contained an open reading frame encoding a protein of 322 amino acids with an estimated M(w) of 37 kD. When expressed in E. coli, the encoded protein migrated to the same position on SDS-polycrylamide gels as the enzyme in rat liver cytosols. The protein expressed in bacteria was highly active in androsterone oxidation in the presence of NAD as cofactor and this activity was inhibited by indomethacin, a potent inhibitor of 3α-hydroxysteroid dehydrogenase. The predicted amino acid sequence of 3α-hydroxysteroid d dehydrogenase was related to sequences of several other aldo-keto reductases such as bovine prostaglandin F synthase, human chlordecone reductase, human aldose reductase, human aldehyde reductase and frog lens epsilon-crystallin, suggesting that these proteins belong to the same gene family. Recently, we have found that monoclonal antibodies against 3α-hydroxysteroid dehydrogenase also recognized multiple antigenically related proteins in rat lung, kidney and testis. Further screening of liver, lung and kidney cDNA libraries using these monoclonal antibodies as probes resulted in the isolation of additional five different cDNAs encoding proteins with high degree of structural homology to rat liver 3α-hydroxysteroid dehydrogenase.
Copyright © 1992. Published by Elsevier Ltd.
Similar articles
-
Molecular cloning and expression of rat liver 3 alpha-hydroxysteroid dehydrogenase.Mol Endocrinol. 1991 Jun;5(6):823-8. doi: 10.1210/mend-5-6-823. Mol Endocrinol. 1991. PMID: 1922097
-
Molecular cloning of a novel type of rat cytoplasmic 17beta-hydroxysteroid dehydrogenase distinct from the type 5 isozyme.J Biochem. 2006 Jun;139(6):1053-63. doi: 10.1093/jb/mvj109. J Biochem. 2006. PMID: 16788056
-
Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase.J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. doi: 10.1016/0960-0760(93)90308-j. J Steroid Biochem Mol Biol. 1993. PMID: 8274401
-
Multiplicity of mammalian reductases for xenobiotic carbonyl compounds.Drug Metab Pharmacokinet. 2006 Feb;21(1):1-18. doi: 10.2133/dmpk.21.1. Drug Metab Pharmacokinet. 2006. PMID: 16547389 Review.
-
Molecular cloning and functions of rat liver hydroxysteroid sulfotransferases catalysing covalent binding of carcinogenic polycyclic arylmethanols to DNA.Chem Biol Interact. 1994 Jun;92(1-3):87-105. doi: 10.1016/0009-2797(94)90056-6. Chem Biol Interact. 1994. PMID: 8033273 Review.
Cited by
-
A transaldolase : An enzyme implicated in crab steroidogenesis.Endocrine. 1996 Aug;5(1):23-32. doi: 10.1007/BF02738652. Endocrine. 1996. PMID: 21153090
-
Testosterone and progesterone metabolism in the central nervous system: cellular localization and mechanism of control of the enzymes involved.Cell Mol Neurobiol. 1996 Jun;16(3):271-82. doi: 10.1007/BF02088095. Cell Mol Neurobiol. 1996. PMID: 8818396 Free PMC article. Review.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases