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Cloning and Expression of cDNA Encoding Bovine Liver Dihydrodiol Dehydrogenase 3, DD3

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Enzymology and Molecular Biology of Carbonyl Metabolism 6

Abstract

Dihydrodiol dehydrogenase (DDH) [EC 1.3.1.20] has been suggested to play an important physiological role in the metabolic detoxication of polycyclic aromatic hydrocarbons (PAHs) (Glatt et al., 1979). The pathways for metabolic activation and detoxication of a typical PAH, benzo[a]pyrene, are shown in Scheme 1. Environmental PAH is mainly activated through the action of liver P-450. The resulting 7,8-epoxide moiety is hydrolyzed by epoxide hydrolase in microsome. Then, the 7,8-dihydrodiol of PAH is further oxygenated to the 7,8-dihydrodiol-9,10-epoxide form by P-450 (Penning, 1993). This compound is assumed to be an ultimate carcinogen which binds covalently to DNA. Alternatively, DDH is reported as an important converting enzyme of the 7,8-dihydrodiol moiety to less active 7,8-dione (dicarbonyl). The dicarbonyl compound is further detoxicated with nonenzymatic ghlutathione-conjugation reaction (Penning, 1993).

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References

  • Bohren, K.M., Bullock, B., Wermuth, B. and Gabbay, K.H. (1989) The aldo-keto reductase superfamily. cDNA and deduced amino acid sequences of human aldehyde and aldose reductases. J.Biol.Chem. 264: 9547–9551.

    PubMed  CAS  Google Scholar 

  • Bolcsak, L.E. and Nerland, D.E. (1983) Purification of mouse liver benzene dihydrodiol dehydrogenases. J.Biol.Chem. 258: 7252–7255.

    PubMed  CAS  Google Scholar 

  • Cheng, K.C., White, P.C. and Qin, K.N. (1991) Molecular cloning and expression of rat liver 3α-hydroxysteroid dehydrogenase. Mol.Endcrinol. 5: 823–828.

    Article  CAS  Google Scholar 

  • 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 

  • Deyashiki, Y., Ogasawara, A., Nakayama, T., Nakanishi, M., Miyabe, Y., Sato, K., and Hara, A. (1994) Molecular cloning of two human liver 3α-hydroxysteroid/dihydrodiol dehydrogenase isozymes that are identical with chlordecone reductase and bile-acid binder. Biochem.J. 299: 545–552.

    PubMed  CAS  Google Scholar 

  • Glatt, H.R., Vogel, K., Bentley, P. and Oesch, F. (1979) Reduction of benzo(a)pyrene mutagenicity by dihydrodiol dehydrogenase. Nature 277: 319–320.

    Article  PubMed  CAS  Google Scholar 

  • Hara, A., Hasebe, K., Hayashibara, M., Matsuura, K., Nakayama, T. and Sawada, H. (1986) Dihydrodiol dehydrogenases in guinea pig liver. Biochem.Pharmacol. 35: 4005–4012.

    Article  PubMed  CAS  Google Scholar 

  • Hara, A., Nakayama, T., Harada, T., Kanazu, T., Shinoda, M., Deyashiki, Y., and Sawada, H. (1991) Distribution and characterization of dihydrodiol dehydrogenases in mammalian ocular tissues. Biochem.J. 275: 113–119.

    PubMed  CAS  Google Scholar 

  • Hoog, S.S., Pawlowski, J.E., Alzari, P.M., Penning, T.M. and Lewis, M. (1994) Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily. Proc.Natl.Acad.Sci.U.S.A. 91: 2517–2521.

    Article  PubMed  CAS  Google Scholar 

  • Hou, Y.T., Xia, W., Pawlowski, J.E. and Penning, T.M. (1994) Rat dihydrodiol dehydrogenase: complexity of gene structure and tissue-specific and sexually dimorphic gene expression. Cancer.Res. 54: 247–255.

    PubMed  CAS  Google Scholar 

  • Klein, J., Thomas, H., Post, K., WÅ¡rner, W. and Oesch, F. (1992) Dihydrodiol dehydrogenase activities of rabbit liver are associated with hydroxysteroid dehydrogenases and aldo-keto reductases. Eur.J.Biochem. 205: 1155–162.

    Article  PubMed  CAS  Google Scholar 

  • Kuchinke, K., Barski, O., Watanabe, K. and Hayaishi, O. (1992) A lung type prostagladin F synthase is expressed in bovine liver: cDNA sequence and expression in E.coli. Biochem.Biophys.Res.Commun. 183: 1238–1246.

    Article  PubMed  CAS  Google Scholar 

  • Lacy, W.R., Washenick, K.J., Cook, R.G., & Dunbar, B.S. (1993) Molecular cloning and expression of abundant rabbit ovarian protein with 20α-hydroxysteroid dehydrogenase activity. Mol.Endocr. 7: 58–66.

    Article  CAS  Google Scholar 

  • Matsuura, K., Hara, A., Nakayama, T., Nakagawa, M., Sawada, H. (1987) Purification and properties of two multiple forms of dihydrodiol dehydrogenase from guinea-pig testis. Biochim.Biophys.Acta. 912: 270–277.

    Article  PubMed  CAS  Google Scholar 

  • Mizoguchi, T., Nanjo, H., Umemura, T., Nishinaka, T., Iwata, C., Imanishi, T., Tanaka, T., Terada, T. and Nishihara, T. (1992) A novel dihydrodiol dehydrogenase in bovine liver cytosol: purification and characterization of multiple forms of dihydrodiol dehydrogenase. J.Biochem.(Tokyo) 112: 523–529.

    CAS  Google Scholar 

  • Nakagawa, M., Harada, T., Hara, A., Nakayama, T. and Sawada, H. (1989) Purification and properties of multiple forms of dihydrodiol dehydrogenase from monkey liver. Chem.Pharm.Bull. 37: 2852–2854.

    Article  PubMed  CAS  Google Scholar 

  • Nanjo, H. Adachi, H., Aketa, M., Mizoguchi, T., Nishihara, T. and Terada, T. (1995) Role of cysteine in the alteration of bovine liver dihydrodiol dehydrogenase 3 activity. Biochem.J. 310: 101–107.

    PubMed  CAS  Google Scholar 

  • Nanjo, H., Terada, T. Umemura, T. Nishinaka, T. Mizoguchi, T. and Nihishihara, T. (1992) Characterization of bovine liver cytosolic 3α-hydroxysteroid dehydrogenase and its aldo-keto reductase activity. Int.J.Biochem. 24:815–820.

    Article  PubMed  CAS  Google Scholar 

  • Pawlowski, J., Huizinga, M. and Penning, T.M. (1991) Cloning and sequncing of the cDNA for rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase. J.Biol.Chem. 266: 8820–8825.

    PubMed  CAS  Google Scholar 

  • Penning, T.M. (1993) Dihydrodiol dehydrogenase and its role in polycyclic aromatic hydrocarbon metabolism. Chem.Biol.Interact. 89: 1–34.

    Article  PubMed  CAS  Google Scholar 

  • Penning, T.M. and Sharp, R.B. (1990) Characterization of dihydrodiol dehydrogenase in human liver and lung. Carcinogenesis 11: 1203–1208.

    Article  PubMed  CAS  Google Scholar 

  • Qin, K.N., Khanna, M. and Cheng, K.C. (1994) Structure of a gene coding for human dihydrodiol dehydrogenase/bile acid-binding protein. Gene 149: 357–361.

    Article  PubMed  CAS  Google Scholar 

  • Rondeau, J.M., Téte-Favier, F., Podjarny, A., Reymann, J.M., Barth, P., Biellmann, J.F. and Moras, D. (1992) Novel NADPH-binding domain revealed by the crystal structure of aldose reductase. Nature 355: 469–72.

    Article  PubMed  CAS  Google Scholar 

  • Sato, S. (1993) Aldose reductase the major protein associated with naphthalene dihydrodiol dehydrogenase activity in rat lens. Invest.Ophthalmol. Vis.Sci. 34: 3172–3178.

    PubMed  CAS  Google Scholar 

  • Stolz, A., Rahimi-Kiani, M., Ameis, D., Chan, E., Ronk, M., and Shively, J.E. (1991) Molecular structure of rat hepatic 3α-hydroxysteroid dehydrogenase. A member of the oxidereductase gene family. J.Biol. Chem. 266: 15253–15257.

    PubMed  CAS  Google Scholar 

  • Terada, T., Kohno, T., Samejima, T., Hosomi, S., Mizoguchi, T. and Uehara, K. (1985) Purification and properties of beef liver aldehyde reductase catalyzing the reduction of D-erythrose 4-phosphate. J.Biochem. (Tokyo) 97: 79–87.

    PubMed  CAS  Google Scholar 

  • Terada, T., Niwase, N., Koyama, I., Imamura, M., Shinagawa, K., Toya, H. and Mizoguchi, T. (1993) Purification and characterization of carbonyl reductase from bovine liver cytosol and microsome. The cytosolic enzyme has a novel 3α/17β-hydroxysteroid dehydrogenase activity. Int.J.Biochem. 25: 12331239.

    Google Scholar 

  • Vogel, K., Bentley, P., Platt, K.L. and Oesch, F. (1980) Rat liver cytoplasmic dihydrodiol dehydrogenase. Purification to apparent homogeneity and properties. J.Biol.Chem. 255: 9621–9625.

    PubMed  CAS  Google Scholar 

  • Watanabe, K., Fujii, Y., Nakayama, K., Ohkubo, H., Kuramitsu, S., Kagamiyama, H., Nakanishi, S. and Hayaishi, O. (1988) Structural similarity of bovine lung prostaglandin F synthase to lens e-crystallin of European common frog. Proc.Natl.Acad.Sci.U.S.A. 85: 11–15.

    Article  PubMed  CAS  Google Scholar 

  • Wilson, D.K., Bohren, K.M., Gabbay, K.H. and Quiocho, F.A. (1992) An unlikely sugar substrate site in the 1.65 Ã… structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257: 81–84.

    Article  PubMed  CAS  Google Scholar 

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© 1996 Springer Science+Business Media New York

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Terada, T. et al. (1996). Cloning and Expression of cDNA Encoding Bovine Liver Dihydrodiol Dehydrogenase 3, DD3. In: Weiner, H., Lindahl, R., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 6. Advances in Experimental Medicine and Biology, vol 414. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5871-2_62

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  • DOI: https://doi.org/10.1007/978-1-4615-5871-2_62

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7692-7

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