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Expression of mRNAs for Dihydrodiol Dehydrogenase Isoforms in Human Tissues

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Enzymology and Molecular Biology of Carbonyl Metabolism 7

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 463))

Abstract

Dihydrodiol dehydrogenase (DD) [EC 1. 3. 1. 20] catalyzes the NADP+-linked oxidation of /trans-dihydrodiols of polycyclic aromatic hydrocarbons to corresponding catechols, and controls the formation of both their carcinogenic dihydrodiol epoxides (Oesch, et al.,, 1984) and cytotoxic o-quinones through autoxidation of the catechol metabolites (Flowers, et al.,., 1996). In addition, DD in mammalian liver is implicated in the metabolism of xenobiotic carbonyl compounds, steroids and prostaglandins because of its broad substrate specificity (Penning, et al.,, 1986; Hara, et al.,, 1986; Ohara, et al.,, 1994; 1995).

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References

  • Ciaccio, P. J. and Tew, K. D., 1994, cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase, Biochim. Biophys. Acta, 1186, 129–132.

    Article  PubMed  CAS  Google Scholar 

  • Dufort, I., Soucy, P., Labrie, F., and Luu-The, V., 1996, Molecular cloning of human type 3 3α-hydroxysteroid de-hydrogenase that differs from 20α-hydroxysteroid dehydrogenase by seven amino acids, Biochem. Biophys. Res. Commun., 228, 474–479.

    Article  PubMed  CAS  Google Scholar 

  • Flowers, L., Bleczinski, W. F., Burczynski, M. E., Harvey, R. G., and Penning, T. M., 1996, Disposition and biological activity of benzo[a]pyrene-7,8-dione. A genotoxic metabolite generated by dihydrodiol dehydrogenase, Biochemistry, 35, 13664–13672.

    Article  PubMed  CAS  Google Scholar 

  • Hara, A., Hasebe, K., Hayashibara, M, Matsuura, K., Nakayama, T. and Sawada, H., 1986, Dihydrodiol dehydro-genases in guinea pig liver, Biochem. Pharmacol., 35,4005–4012.

    Article  PubMed  CAS  Google Scholar 

  • Hara, A. Taniguchi, H., Nakayama, T., and Sawada, H., 1990, Purification and properties of multiple forms of dihydrodiol dehydrogenase from human liver, J. Biochem. (Tokyo), 108, 250–254.

    CAS  Google Scholar 

  • Hara, A., Matsuura, K., Tamada, Y, Sato, K., Miyabe, Y., Deyashiki, Y, and Ishida, N., 1996, Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductases of human colon cells, Biochem. J., 313, 373–376.

    PubMed  CAS  Google Scholar 

  • Iwasa, H., Hara, A., Kume, T., Yokoi, T., Kamataki, T., Inoue, K., Terada, K., Takagi, T., and Otsuka, M., 1997, Isolation and properties of human liver dihydrodiol dehydrogenase variant. The 117th Annual Meeting of the Pharmaceutical Society of Japan, Tokyo, Abstract, Part 3, p. 39.

    Google Scholar 

  • Jez, J. M., Flynn, T. G., and Penning, T. M., 1997, A new nomenclature for the aldo-keto reductase superfamily, Biochem. Pharmacol, 54, 639–647.

    Article  PubMed  CAS  Google Scholar 

  • Khanna, M., Qin, K.-N., Wang, R. W., and Cheng, K.-C., 1995, Substrate specificity, gene structure, and tissue distribution of multiple human 3α-hydroxysteroid dehydrogenases, J. Biol. Chem., 270, 20162–20168.

    Article  PubMed  CAS  Google Scholar 

  • Lacy, W. R., Washenik, R. G., and Dunbar, B. S., 1993, Molecular cloning and expression of an abundant rabbit ovarian protein with 20a-hydroxysteroid dehydrogenase activity, Mol. Endcrinol, 7, 58–66.

    Article  CAS  Google Scholar 

  • Lin, H.-K., Jez, J. M., Schlegel, B. R, Peehl, D. M., Pachter, J. A., and Penning, T. M., 1997, Expression and characterization of recombinant type 2 3α-hydroxysteroid dehydrogenase (HSD) from human prostate: Demonstration of bifunctional 3α/17β-HSD activity and cellular distribution, Mol. Endocrinol, 11, 1971–1984.

    Article  PubMed  CAS  Google Scholar 

  • Matsuura, K., Shiraishi, H., Hara, A., Sato, K., Deyashiki, Y., Niomiya, M., and Sakai, S., 1998, Identification of a principal mRNA species for human 3a-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity. J. Biochem. (Tokyo), in press.

    Google Scholar 

  • Miura, R., Shiota, K., Noda, K., Yagi, S., Ogawa, T., and Takahashi, M., 1994, Molecular cloning of cDNA for rat ovarian 20α-hydroxysteroid dehydrogenase (HSD1), Biochem. J., 299, 561–567.

    PubMed  CAS  Google Scholar 

  • Miyabe, Y, Matsuura, K., Nakayama, T., Ohya, I., and Hara, A., 1997, A sensitive fluorometric assay for dihy-drodiol dehydrogenase, Yakugaku Zasshi, 117, 167–177.

    PubMed  CAS  Google Scholar 

  • Nagase, T., Miyajima, N., Tanaka, A., Sazuka, T., Seki, N., Sato, S., Tabata, S., Ishikawa, K., Kawarabayashi, Y, Kotani, H., and Nomura, N., 1995, Prediction of the coding sequences of unidentified genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1, DNA Res., 2, 37–43.

    Article  PubMed  CAS  Google Scholar 

  • Oesch, F., Glatt, H. R., Vogel, K., Seidel, A., Petrovic, P., and Platt, K. L., 1984, Dihydrodiol dehydrogenase: Anew level of control by both sequestration of proximate and inactivation of ultimate carcinogens. In Greim, H., Jung, R., Kramer, M., Marquardt, H., and Oesch, F. (Eds. ), Biochemical Basis of Carcinogenesis, Raven Press, New York, pp. 23–31.

    Google Scholar 

  • Ohara, H., Nakayama, T., Deyashiki, Y, Hara, A., Miyabe, Y, and Tukada, F., 1994, Reduction of prostaglandin D2 to 9α, 11 β-prostaglandin F2 by a human liver 3a-hydroxy-steroid/dihydrodiol dehydrogenase isozyme, Biochim. Biophys. Acta,1215, 59–65.

    Article  PubMed  CAS  Google Scholar 

  • Ohara, H., Miyabe, Y, Deyashiki, Y, Matsura, K., and Hara, A., 1995, Reduction of drug ketones by dihydrodiol dehydrogenases, carbonyl reductase and aldehyde reductase of human liver, Biochem. Pharmacol., 50, 221–227.

    Article  PubMed  CAS  Google Scholar 

  • Penning, T. M., Smithgall, T. E., Askonas, L. J., and Sharp, R. B., 1986, Rat liver 3 α-hydroxy steroid dehydrogenase, Steroids, 47,221–247.

    Article  PubMed  CAS  Google Scholar 

  • Qin, K.-N., New, M. I., and Cheng, K.-C, 1993, Molecular cloning of Multiple cDNAs encoding human enzymes structurally related to 3α-hydroxysteroid dehydrogenase, J. Steroid Biochem. Molec. Biol, 46, 673–679.

    Article  PubMed  CAS  Google Scholar 

  • Shiraishi, H., Ishiküra, S., Matsuura, K., Deyashiki, Y, Niomiya, M., Sakai, S., and Hara, A., 1998, Sequence of human dihydrodiol dehydrogenase isoform (AKR1C2) cDNA and tissue distribution of its mRNA. Biochem. J., in press.

    Google Scholar 

  • Stolz, A., Hammond., L., Lou, H., Takikawa, H., Ronk, M., and Shively, J. E., 1993, cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family, J. Biol. Chem., 268, 10448–10457.

    PubMed  CAS  Google Scholar 

  • Tamaoki, B. and Shikita, M., 1966, Biosynthesis of steroids in testicular tissue in vitro. In Pincus, G., Nakao, T. and Tait, J. F. (Eds. ), Steroid Dynamics, Academic Press, New York, pp. 493–530.

    Google Scholar 

  • Winters, C. J., Molowa, D. T., and Guzelian, P. S., 1990, Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase, Biochemistry, 29, 1080–1087.

    Article  PubMed  CAS  Google Scholar 

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Shiraishi, H., Matsuura, K., Kume, T., Hara, A. (1999). Expression of mRNAs for Dihydrodiol Dehydrogenase Isoforms in Human Tissues. In: Weiner, H., Maser, E., Crabb, D.W., Lindahl, R. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 7. Advances in Experimental Medicine and Biology, vol 463. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4735-8_68

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  • DOI: https://doi.org/10.1007/978-1-4615-4735-8_68

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7146-5

  • Online ISBN: 978-1-4615-4735-8

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