Molecular cloning of a novel type of rat cytoplasmic 17β- hydroxysteroid dehydrogenase distinct from the type 5 isozyme

Journal of Biochemistry

Volumn 139, Issue 6, 2006, Pages 1053-1063

  Ishikura, Shuhei ^a,d   Matsumoto, Kengo ^a   Sanai, Masaharu ^a   Horie, Kenji ^a   Matsunaga, Toshiyuki ^a   Tajima, Kazuo ^b   El Kabbani, Ossama ^c   Hara, Akira ^a  

^a GIFU PHARMACEUTICAL UNIVERSITY   (Japan)

^b HOKURIKU UNIVERSITY   (Japan)

^c MONASH UNIVERSITY   (Australia)

^d HOSPITAL FOR SICK CHILDREN   (Canada)

Author keywords

17 hydroxysteroid dehydrogenase; 20 hydroxysteroid dehydrogenase; 3 hydroxysteroid dehydrogenase; 9 hydroxyprostaglandin; Aldo keto reductase family; Xenobiotic ketone reductase

Indexed keywords

17BETA HYDROXYSTEROID; 20ALPHA HYDROXYSTEROID; 3ALPHA HYDROXYSTEROID; 3ALPHA HYDROXYSTEROID DEHYDROGENASE; 6 TERT BUTYL 2,3 EPOXY 5 CYCLOHEXENE 1,4 DIONE; 6 TERT BUTYL 2,3 EPOXY 5 CYCLOHEXENE 1,4 DIONE REDUCTASE 1; 6 TERT BUTYL 2,3 EPOXY 5 CYCLOHEXENE 1,4 DIONE REDUCTASE 2; 9 HYDROXYPROSTAGLANDIN; ALCOHOL; AMINO ACID; BENZENE DERIVATIVE; BENZENE DIHYDRODIOL; COMPLEMENTARY DNA; CYCLOHEXENE DERIVATIVE; DIETHYLSTILBESTROL; HEXESTROL; HYDROXYSTEROID; INDAN 1 OL; INDAN DERIVATIVE; ISATIN; ISOENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; PROSTAGLANDIN DERIVATIVE; RECOMBINANT ENZYME; STEROID; TESTOSTERONE 17BETA DEHYDROGENASE; TETRALOL; UNCLASSIFIED DRUG; XENOBIOTIC AGENT; ZEARALENONE;

AMINO ACID COMPOSITION; ANIMAL TISSUE; ARTICLE; CHROMATOGRAPHY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME SPECIFICITY; FEMALE; GASTROINTESTINAL TRACT; GENE EXPRESSION; KIDNEY; LIVER; LIVER CYTOSOL; MALE; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; OVARY; OXIDATION; PH; PROTEIN EXPRESSION; RAT; REDUCTION; SENSITIVITY AND SPECIFICITY; TISSUE DISTRIBUTION;

17-HYDROXYSTEROID DEHYDROGENASES; 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE (B-SPECIFIC); AMINO ACID SEQUENCE; ANIMALS; BLOTTING, WESTERN; CLONING, MOLECULAR; CYTOPLASM; FEMALE; HYDROGEN-ION CONCENTRATION; ISOENZYMES; KIDNEY; LIVER; MALE; MICE; MOLECULAR SEQUENCE DATA; OVARY; OXIDATION-REDUCTION; RATS; RATS, WISTAR; RECOMBINANT PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, MESSENGER; SEQUENCE HOMOLOGY, AMINO ACID; STOMACH; SUBSTRATE SPECIFICITY;

EID: 33746871473     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj109     Document Type: Article

References (46)

1. Bachur, N.R. (1976) Cytoplasmic aldo-keto reductases: A class of drug metabolizing enzymes. Science 193, 595-597
2. Felsted, R.L. and Bachur, N.R. (1980) Mammalian carbonyl reductases. Drug Metab. Rev. 11, 1-60
3. Maser, E. (1995) Xenobiotic carbonyl reduction and physiological steroid oxidoreduction. The pluripotency of several hydroxysteroid dehydrogenases. Biochem. Pharmacol. 49, 421-440
4. Oppermann, U.C. and Maser, E. (2000) Molecular and structural aspects of xenobiotic carbonyl metabolizing enzymes. Role of reductases and dehydrogenases in xenobiotic phase I reactions. Toxicology 144, 71-81
5. Tajima, K., Hashizaki, M., Yamamoto, K., Narimatsu, S., and Mizutani, T. (1999) Purification and some properties of two enzymes from rat liver cytosol that catalyze carbonyl reduction of 6-tert-butyl-2,3-epoxy-5-cyclohexene-1,4- dione, a metabolite of 3-tert-butyl-4-hydroxyanisole. Arch. Biochem. Biophys. 361, 207-214
6. Hyndman, D., Bauman, D.R., Heredia, V.V., and Penning, T.M. (2003) The aldo-keto reductase superfamily homepage. Chem. Biol. Interact. 143-144, 621-631
7. Labrie, F., Luu-The, V., Lin, S.-X., Simard, J., Labrie, C., El-Alfy, M., Pelletier, G., and Belanger, A. (2000) Intracrinology: role of the family of 17β-hydroxysteroid dehydrogenases in human physiology and diseases. J. Mol. Endocrinol. 25, 1-16
8. Peltoketo, H., Luu-The, V., Simard, J., and Adamisk, J. (1999) 17β-hydroxysteroid dehydrogenase (HSD)/17-ketosteroid reductase (KSR) family; nomenclature and main characteristics of the 17HSD/KSR enzymes. J. Mol. Endocrinol. 23, 1-11
9. Adamisk, J. and Jakob, F.J. (2001) A guide to 17β-hydroxysteroid dehydrogenases. Mol. Cell. Endocrinol. 171, 1-4
10. 2 11-ketoreductase activity. J. Biochem. 124, 940-946
11. Penning, T.M., Burczynski, M.E., Jez, J.M., Hung, C.-F., Lin, H.-K., Ma, H., Moode, M., Palackal, N., and Patnam, K. (2000) Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveal roles in the inactivation and formation of male and female sex hormones. Biochem. J. 351, 67-77
12. Suzuki-Yamamoto, T., Nishizawa, M., Fukui, M., Okuda-Ashitaka, E., Nakajima, T., Ito, S., and Watanabe, K. (1999) cDNA cloning, expression and characterization of human prostaglandin F synthase. FEBS Lett. 462, 335-340
13. Deyashiki, Y., Ohshima, K., Nakanishi, M., Sato, K., Matsuura, K., and Kara, A. (1995) Molecular cloning and characterization of mouse estradiol 17β-dehydrogenase (A-specific), a member of the aldo-keto reductase family. J. Biol. Chem. 270, 10461-10467
14. Sawada, H., Hara, A., Nakayama, T., Nakagawa, M., Inoue, Y., Hasebe, K., and Zhang, Y.-P. (1988) Mouse liver dihydrodiol dehyrogenases. Identity of the predominant and a minor form with 17β-hydroxysteroid dehydrogenase and aldehyde reductase. Biochem. Pharmacol. 37, 453-458
15. Sato, K., Inazu, A., Yamaguchi, S., Nakayama, T., Deyashiki, Y., Sawada, H., and Hara, A. (1993) Monkey 3-deoxyglucosone reductase: Tissue distribution, purification of three forms of the kidney enzyme that are identical with dihydrodiol dehydrogenase, aldehyde reductase and aldose reductase. Arch. Biochem. Biophys. 307, 286-294
16. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual (2nd ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
17. Nakanishi, M., Deyashiki, Y., Ohshima, K., and Hara, A. (1995) Cloning, expression and tissue distribution of mouse tetrameric carbonyl reductase. Identity with an adipocyte 27-kDa protein. Eur. J. Biochem. 228, 381-387
18. Ishikura, S., Usami, N., Nakajima, S., Kameyama, A., Shiraichi, H., Carbone, V., El-Kabbani, O., and Hara, A. (2004) Characterization of two isoforms of mouse 3(17)α-hydroxysteroid dehydrogenases of the aldo-keto reductase family. Biol. Pharm. Bull. 27, 1939-1945
19. Pawlowski, J.E. and Penning, T.M. (1994) Overexpression and mutagenesis of the cDNA for rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase. Role of cysteins and tyrosine in catalysis. J. Biol. Chem. 269, 13502-13510
20. Platt, K.L. and Oesch, F. (1977) An improved synthesis of trans-5,6-dihydroxy-1,3-cyclohexadiene (trans-1,2-dihydroxy-1,2-dihydrobenzene). Synthesis 7, 449-450
21. Monder, C. and Furfine, C.S. (1989) 21-Hydroxysteroid dehydrogenase of liver and adrenal. Method Enzymol. 15, 667-675
22. Tajima, K., Hashizaki, M., Yamamoto, K., and Mizutani, T. (1992) Metabolism of 3-tert-butyl-4-hydroxyanisole by horse-radish peroxidase and hydrogen peroxide. Drug. Metab. Dispos. 20, 816-20
23. Tajima, K., Hashizaki, M., Yamamoto, K., and Mizutani, T., (1994) Carbonyl reduction of 6-tert-butyl-2,3-epoxy-1,4-benzoquinone, a metabolite of 3-tert-butyl-4-hydroxyanisole, by rat liver microsomes and cytosol. Drug Metab. Dispos. 22, 815-818
24. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
25. Qin, K.-N. and Cheng, K.-C. (1994) Structure and tissue-specific expression of the aldo-keto reductase superfamily. Biochemistry 33, 3223-3228
26. Jez, J.M., Bennett, M.J., Schlegel, B.P., Lewis, M., and Penning, T.M. (1997) Comparative anatomy of the aldo-keto reductase superfamily. Biochem. J. 326, 625-636
27. Couture, J.-F., Legrand, P., Cantin, L., Luu-The, V., Labrie, F., and Breton, R. (2003) Human 20α-hydroxysteroid dehydrogenase: Crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids. J. Mol. Biol. 331, 593-604
28. + and ursodeoxycholate. Biochemistry 40, 10161-10168
29. + bound to 3α-hydroxysteroid/ dihydrodiol dehydrogenase. Structure 5, 799-812
30. Tanaka, N., Nonaka, T., Nakamura, N.T., and Hara, A. (2001) SDR: structure, mechanism of action, and substrate recognition. Cur. Org. Chem. 5, 89-111
31. Ishikura, S., Horie, K., Sanai, M., Matsumoto, K., and Hara, A. (2005) Enzymatic properties of a member (AKR1C19) of the aldo-keto reductase family. Biol. Pharm. Bull. 28, 1075-1078
32. Deyashiki, Y., Takatsuji, T., and Hara, A. (2003) Molecular cloning and characterization of dihydrodiol dehydrogenase from the mouse. In Aldo-Keto Reductases and Toxicant Metabolism (Penning, T.M. and Petrash, J.M., eds.) pp. 101-114, ACS, Washington
33. Yamano, S., Ito, K., Ogata, S., and Toki, T. (1997) Purification, characterization and partial primary structure of morphine 6-dehydrogenase from rabbit liver cytosol. Arch. Biochem. Biophys. 341, 81-89
34. Todaka, T., Yamano, S., and Toki, T. (2000) Purification and characterization of NAD-dependent morphine 6-dehydrogenase from hamster liver cytosol, a new member of the aldo-keto reductase superfamily. Arch. Biochem. Biophys. 374, 189-197
35. Veech, R.L., Eggleston, L.V., and Krebs, H.A. (1969) The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver. Biochem. J. 115, 609-619
36. Mustonen, M., Poutanen, M., Chotteau-Lelievre, A., de Launoit, Y., Isomaa, V., Vainio, S., Vihko, R., and Vihko, P. (1997) Ontogeny of 17β-hydroxysteroid dehydrogenase type 2 mRNA expression in the developing mouse placenta and fetus. Mol. Cell Endocrinol. 134, 33-40
37. Mustonen, M.V., Poutanen, M.H., Kellokumpu, S., de Launoit, Y., Isomaa, V.V., Vihko, R.K., and Vihko, P.T. (1998) Mouse 17β-hydroxysteroid dehydrogenase type 2 mRNA is predominantly expressed in hepatocytes and in surface epithelial cells of the gastrointestinal and urinary tracts. J. Mol. Endocrinol. 20, 67-74
38. Oduwole, O.O., Isomaa, V.V., Nokelainen, P.A., Stenback, F., and Vihko, P.T. (2002) Downregulation of estrogen-metabolizing 17β-hydroxysteroid dehydrogenase type 2 expression correlates inversely with Ki67 proliferation marker in colon-cancer development. Int. J. Cancer 97, 1-6
39. Oduwole, O.O., Makinen, J.M., Isomaa, V., Karttunen, T.J., and Vihko, P.T. (2003) Sex steroid metabolism in human gastric mucosa: 17β- hydroxysteroid dehydrogenase type 2 in normal, inflamed and neoplastic gastric tissues. Anticancer Res. 23, 3889-3898
40. Kaplan, L., Lee, S.C., and Levine, L. (1975) Partial purification and some properties of human erythrocyte prostaglandin 9-ketoreductase and 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. 167, 287-293
41. 2 9-reductase from corpus luteum of pseudopregnant rabbit is a member of the aldo-keto reductase superfamily featuring 20α-hydroxysteroid dehydrogenase. Eur. J. Biochem. 234, 264-270
42. Schieber, A., Frank, R.W., and Ghisla, S. (1992) Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney. Identity with human carbonyl reductase. Eur. J. Biochem. 206, 491-502
43. Tai, H.H. and Yuan, B. (1982) Purification and assay of 9-hydroxyprostaglandin dehydrogenase from rat kidney. Methods Enzymol. 86, 113-117
44. Takenoshita, R. and Toki, S. (1985) Purification and properties of rat liver 3-hydroxyhexobarbital dehydrogenase. J. Pharmacobio-Dyn. 8, 159
45. Penning, T.M., Burczynski, M.E., Hung, C.-F., McCoull, K.D., Palackal, N.T., and Tsuruda, L.S. (1999) Dihydrodiol dehydrogenases and polycyclic aromatic hydrocarbon activation: Generation of reactive and redox active o-quinones. Chem. Res. Toxicol. 12, 1-18
46. Bradlow, H.L. and Monder, C. (1979) Steroid carboxylic acids. In Steroid Biochemistry Vol. 1 (Hobkik, R., ed.) pp. 29-82, Boca Raton, CRC Press