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Dhrs9  -  dehydrogenase/reductase (SDR family) member 9

Rattus norvegicus

Synonyms: 3-alpha hydroxysteroid dehydrogenase, 3-alpha-HSD, Dehydrogenase/reductase SDR family member 9, Short-chain dehydrogenase/reductase retSDR8
 
 
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Disease relevance of Dhrs9

 

High impact information on Dhrs9

 

Chemical compound and disease context of Dhrs9

  • We conclude, that detoxification enzymes like 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD) and delta4-3-ketosteroid-5beta-reductase (5beta-Red) might be replaced in hepatomas by tumor-associated proteins that are often present in the embryonal state, like the rARLPs or the Rak-c protein [10].
 

Biological context of Dhrs9

  • Members of the nuclear factor 1 transcription factor family regulate rat 3alpha-hydroxysteroid/dihydrodiol dehydrogenase (3alpha-HSD/DD AKR1C9) gene expression: a member of the aldo-keto reductase superfamily [11].
  • Measurement of the half-life of 3alpha-HSD/DD mRNA, with and without Dex treatment, indicated that the increase in steady state mRNA levels was not due to increased mRNA stability [12].
  • The Y55F and Y55S mutants displayed narrow substrate specificity and reduced select aromatic quinones and alpha-dicarbonyls. kcat versus pH profiles for steroid oxidoreduction catalyzed by wild-type 3alpha-HSD exhibited a single ionizable group with a pK= 7.0-7.5, which has been assigned to Tyr 55 [13].
  • Dissection of the physiological interconversion of 5alpha-DHT and 3alpha-diol by rat 3alpha-HSD via transient kinetics shows that the chemical step is rate-determining: effect of mutating cofactor and substrate-binding pocket residues on catalysis [14].
  • Rat liver 3 alpha-hydroxysteroid dehydrogenase (3 alpha-HSD) (EC 1.1.1.50) is an NAD(P)(+)-dependent oxidoreductase that is potently inhibited at its active site by non-steroidal anti-inflammatory drugs (NSAIDs) [15].
 

Anatomical context of Dhrs9

 

Associations of Dhrs9 with chemical compounds

 

Other interactions of Dhrs9

 

Analytical, diagnostic and therapeutic context of Dhrs9

References

  1. Characterization of dihydrodiol dehydrogenase in rat H-4IIe hepatoma cells. Buller, A.L., Sharp, R.B., Penning, T.M. Cancer Res. (1989) [Pubmed]
  2. Effects of testosterone mediated or modulated by pituitary factors. De Moor, P., Adam-Heylen, M., Van Baelen, H., Verhoeven, G. J. Endocrinol. (1975) [Pubmed]
  3. Effect of whole and fractionated dietary alfalfa meal on zearalenone toxicosis and metabolism in rats and swine. Stangroom, K.E., Smith, T.K. Can. J. Physiol. Pharmacol. (1984) [Pubmed]
  4. Pathogenesis of diabetic neuropathy--do hyperglycemia and aldose reductase inhibitors affect neuroactive steroid formation in the rat sciatic nerves? Colciago, A., Negri-Cesi, P., Celotti, F. Exp. Clin. Endocrinol. Diabetes (2002) [Pubmed]
  5. Time-studies of the changes in the sex-dependent activities of enzymes of hepatic steroid metabolism in the rat during oestrogen administration. Lax, E.R., Kreuzfelder, E., Schriefers, H. Hoppe-Seyler's Z. Physiol. Chem. (1979) [Pubmed]
  6. Cyclical oxidation-reduction of the C3 position on bile acids catalyzed by rat hepatic 3 alpha-hydroxysteroid dehydrogenase. I. Studies with the purified enzyme, isolated rat hepatocytes, and inhibition by indomethacin. Takikawa, H., Stolz, A., Kaplowitz, N. J. Clin. Invest. (1987) [Pubmed]
  7. Cyclical oxidation-reduction of the C3 position on bile acids catalyzed by 3 alpha-hydroxysteroid dehydrogenase. II. Studies in the prograde and retrograde single-pass, perfused rat liver and inhibition by indomethacin. Takikawa, H., Ookhtens, M., Stolz, A., Kaplowitz, N. J. Clin. Invest. (1987) [Pubmed]
  8. Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes. Griffin, L.D., Mellon, S.H. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  9. Conversion of mammalian 3alpha-hydroxysteroid dehydrogenase to 20alpha-hydroxysteroid dehydrogenase using loop chimeras: changing specificity from androgens to progestins. Ma, H., Penning, T.M. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  10. Proteome analysis of rat hepatomas: carcinogen-dependent tumor-associated protein variants. Zeindl-Eberhart, E., Klugbauer, S., Dimitrijevic, N., Jungblut, P.R., Lamer, S., Rabes, H.M. Electrophoresis (2001) [Pubmed]
  11. Members of the nuclear factor 1 transcription factor family regulate rat 3alpha-hydroxysteroid/dihydrodiol dehydrogenase (3alpha-HSD/DD AKR1C9) gene expression: a member of the aldo-keto reductase superfamily. Hung, C.F., Penning, T.M. Mol. Endocrinol. (1999) [Pubmed]
  12. Dexamethasone regulation of the rat 3alpha-hydroxysteroid/dihydrodiol dehydrogenase gene. Hou, Y.T., Lin, H.K., Penning, T.M. Mol. Pharmacol. (1998) [Pubmed]
  13. Retention of NADPH-linked quinone reductase activity in an aldo-keto reductase following mutation of the catalytic tyrosine. Schlegel, B.P., Ratnam, K., Penning, T.M. Biochemistry (1998) [Pubmed]
  14. Dissection of the physiological interconversion of 5alpha-DHT and 3alpha-diol by rat 3alpha-HSD via transient kinetics shows that the chemical step is rate-determining: effect of mutating cofactor and substrate-binding pocket residues on catalysis. Heredia, V.V., Penning, T.M. Biochemistry (2004) [Pubmed]
  15. The kinetic mechanism catalysed by homogeneous rat liver 3 alpha-hydroxysteroid dehydrogenase. Evidence for binary and ternary dead-end complexes containing non-steroidal anti-inflammatory drugs. Askonas, L.J., Ricigliano, J.W., Penning, T.M. Biochem. J. (1991) [Pubmed]
  16. Inhibition of a major NAD(P)-linked oxidoreductase from rat liver cytosol by steroidal and nonsteroidal anti-inflammatory agents and by prostaglandins. Penning, T.M., Talalay, P. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  17. Identification of the oxidative 3alpha-hydroxysteroid dehydrogenase activity of rat Leydig cells as type II retinol dehydrogenase. Hardy, D.O., Ge, R.S., Catterall, J.F., Hou, Y.T., Penning, T.M., Hardy, M.P. Endocrinology (2000) [Pubmed]
  18. Subcellular distribution of 3 alpha-hydroxysteroid dehydrogenase and antiestrogen action on androgen-metabolizing enzymes in rat pituitary gland. Ghraf, R., Schneider, K., Kirchhoff, J., Hiemke, C. J. Neurochem. (1982) [Pubmed]
  19. Steroid metabolism in normal mammary gland and in the dimethylbenzanthracene-induced mammary tumor of rats. Mori, M., Tominaga, T., Tamaoki, B.I. Endocrinology (1978) [Pubmed]
  20. Models for development of nonreceptor methods for distinguishing androgen-sensitive and -insensitive prostatic tumors. Isaacs, J.T., Isaacs, W.B., Coffey, D.S. Cancer Res. (1979) [Pubmed]
  21. Indomethacin-sensitive 3 alpha-hydroxysteroid dehydrogenase in rat tissues. Smithgall, T.E., Penning, T.M. Biochem. Pharmacol. (1985) [Pubmed]
  22. Steroid metabolism and steroid receptors in dimethylbenz(a)anthracene-induced rat mammary tumors. Eechaute, W., de Thibault de Boesinghe, L., Lacroix, E. Cancer Res. (1983) [Pubmed]
  23. Evidence for a granulosa cell site of dihydrostestosterone metabolism in the adult rat ovary. Jarrell, J., Belbeck, L. Biol. Reprod. (1985) [Pubmed]
  24. Inhibition of pyridine-nucleotide-dependent enzymes by pyrazoles. Synthesis and enzymology of a novel A-ring pyrazole steroid. Holt, D.A., Levy, M.A., Brandt, M., Metcalf, B.W. Steroids (1986) [Pubmed]
  25. Effects of unilateral orchidectomy on rat epididymal delta 4-5 alpha-reductase and 3 alpha-hydroxysteroid dehydrogenase. Robaire, B. Can. J. Physiol. Pharmacol. (1979) [Pubmed]
  26. Impaired reductive regeneration of ascorbic acid in the Goto-Kakizaki diabetic rat. Kashiba, M., Oka, J., Ichikawa, R., Kageyama, A., Inayama, T., Kageyama, H., Ishikawa, T., Nishikimi, M., Inoue, M., Inoue, S. Biochem. J. (2000) [Pubmed]
  27. 3alpha-hydroxysteroid dehydrogenase messenger RNA transcription in the immature rat ovary in response to an ovulatory dose of gonadotropin. Espey, L.L., Yoshioka, S., Ujioka, T., Fujii, S., Richards, J.S. Biol. Reprod. (2001) [Pubmed]
  28. Opposing changes in 3alpha-hydroxysteroid dehydrogenase oxidative and reductive activities in rat leydig cells during pubertal development. Ge, R.S., Hardy, D.O., Catterall, J.F., Hardy, M.P. Biol. Reprod. (1999) [Pubmed]
 
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