Advertisement

Physiological and Pathophysiological Alterations in Rat Hepatic Cytochrome P-450+

  • John B. Schenkman
  • Kenneth E. Thummel
  • Leonard V. Favreau
Part of the NATO ASI Series Advanced Science Institutes Series book series (NSSA, volume 202)

Abstract

Cytochrome P-450 is a large family of related enzymes comprising a number of sub-families. The different cytochrome P-450 enzymes are present in just about every phylum examined for them. They are found in prokaryotes [1], unicellular eukaryotes [2], plants [3], fowl [4], insects [5], fish [6], invertebrates [7], and mammals [8]. While the prokaryotic enzyme, e.g., P-450CAM, is a soluble hemoprotein, that of higher organisms is membrane- bound. In mammals it is located in the mitochondrial inner membrane as well as in the endoplasmic reticulum membranes. In the mammal, different forms of cytochrome P-450 are involved in such diverse reactions as steroid hormone synthesis, at several steps, and the processing of compounds of exogenous origin as well as of endogenous origin for excretion from the body. The enzymes involved in the elimination of compounds are located in the endoplasmic reticulum of most organs and tissues in the body. The very large number of such forms found suggests roles for these other than just broad, overlapping spectra of chemical detoxication.

Keywords

Growth Hormone Liver Microsome Growth Hormone Secretion Liver Microsomal Cytochrome Aniline Hydroxylase Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    I.C. Gunsalus, Z. Physioi. Chem., 349, 1610 (1968).Google Scholar
  2. 2.
    A. Lindenmayer and L. Smith, Biochim. Biophys. Acta, 93, 445 (1964).PubMedCrossRefGoogle Scholar
  3. 3.
    D.W. Russell, J. Biol. Chem., 246, 3870 (1971).PubMedGoogle Scholar
  4. 4.
    A. Poland and A. Kappas, Mol. Pharmacol., 7, 697 (1971)PubMedGoogle Scholar
  5. 5.
    J.W. Ray, Biochem Pharmacol., 16, 99 (1967).CrossRefGoogle Scholar
  6. 6.
    J.J. Stegeman, R.L. Binder and A. Orren, Biochem Pharmacol., 28, 3431 (1979).PubMedCrossRefGoogle Scholar
  7. 7.
    L.C. Quattrochi and R.F. Lee, Comp. Biochem. Physiol., 79C, 171 (1984).Google Scholar
  8. 8.
    T. Omura and R. Sato, J. Biol. Chem., 237, PC1375 (1962).Google Scholar
  9. 9.
    L.H. Botelho, D.E. Ryan and W. Levin, J. Biol. Chem., 254, 5635 (1979).PubMedGoogle Scholar
  10. 10.
    I. Jansson, J. Mole and J.B. Schenkman, J. Biol. Chem., 260, 7084 (1985).PubMedGoogle Scholar
  11. 11.
    K.E. Thummel, L.V. Favreau, J. Mole and J.B. Schenkman, Arch. Biochem. Biophys., 266, 319 (1988).PubMedCrossRefGoogle Scholar
  12. 12.
    K.-C. Cheng and J.B. Schenkman, J. Biol. Chem., 257, 2378 (1982).PubMedGoogle Scholar
  13. 13.
    J.B. Schenkman, L.V. Favreau and I. Jansson in Biological Reactive Intermediates (J.J. Kocsis, D.J. Jollow, C.M. Witmer, J.O. Nelson and R. Snyder, eds.) Vol III, Plenum, N.Y. (1986) pp. 107–117.Google Scholar
  14. 14.
    L.V. Favreau, D.M. Malchoff, J.E. Mole and J.B. Schenkman, J. Biol. Chem., 262, 14319 (1987).PubMedGoogle Scholar
  15. 15.
    L.V. Favreau and J.B. Schenkman, Diabetes, 37, 577 (1988).PubMedCrossRefGoogle Scholar
  16. 16.
    R. Axen, J. Porath and S. Ernback, Nature 214, 1302 (1967).PubMedCrossRefGoogle Scholar
  17. 17.
    L.V. Favreau and J.B. Schenkman, Biochem. Biophys. Res. Commun., 142, 623 (1987).PubMedCrossRefGoogle Scholar
  18. 18.
    H. Towbin, T. Staehelin and J. Gordon, Proc. Natl. Acad. Sci. USA, 76, 4350 (1979).PubMedCrossRefGoogle Scholar
  19. 19.
    D.J. Waxman, G.A. Dannan and F.P. Guengerich, Biochemistry, 24, 4409 (1985).PubMedCrossRefGoogle Scholar
  20. 20.
    P.E. Thomas, L.M. Reik, D.E. Ryan and W. Levin, J. Biol. Chem., 258, 4590 (1983).PubMedGoogle Scholar
  21. 21.
    I. Johansson, G. Ekström, B. Scholte, D. Puzycki, H. Jornvall and M. Ingelman-Sundberg, Biochemistry, 27, 1925 (1988).PubMedCrossRefGoogle Scholar
  22. 22.
    Y. Funae, and S. Imaoka, Biochim. Biophys. Acta, 926, 349 (1987).PubMedCrossRefGoogle Scholar
  23. 23.
    S. Imaoka, Y. Terano and Y. Funae, Biochim. Biophys. Acta, 916, 358 (1987).PubMedCrossRefGoogle Scholar
  24. 24.
    D.J. Waxman, D.P. Lapenson, S.S. Park, C. Attisano and H.V. Gelboin, Mol. Pharmacol., 32, 615 (1987).PubMedGoogle Scholar
  25. 25.
    W. Levin, P.E. Thomas, D.E. Ryan and A.W. Wood, Arch. Biochem. Biophys., 258, 630 (1987).PubMedCrossRefGoogle Scholar
  26. 26.
    K. Nagata, T. Matsunaga, J. Gillette, H.V. Gelboin and F.J. Gonzalez, J. Biol. Chem., 262, 2787 (1987).PubMedGoogle Scholar
  27. 27.
    K. Maeda, T. Kamataki, T. Nagai and R. Kato, Biochem. Pharmacol., 33, 509 (1984).PubMedCrossRefGoogle Scholar
  28. 28.
    C. MacGeoch, E.T., Morgan, and J.A. Gustafsson, Endocrinol., 117, 2085 (1985).CrossRefGoogle Scholar
  29. 29.
    E.T. Morgan, C. MacGeoch and J.A. Gustafsson, J. Biol. Chem., 260, 11895 (1985).PubMedGoogle Scholar
  30. 30.
    D.J. Waxman, J. Biol. Chem., 259, 15481 (1984).PubMedGoogle Scholar
  31. 31.
    S. Bandiera, D.E. Ryan, W. Levin and P.E. Thomas, Arch. Biochem. Biophys., 248, 658 (1986).PubMedCrossRefGoogle Scholar
  32. 32.
    D.J. Waxman, G.A. LeBlanc, J.J. Morrissey, J. Staunton and D.P. Lapenson, J. Biol. Chem., 263, 11396 (1988).PubMedGoogle Scholar
  33. 33.
    P.E. Thomas, S. Bandiera, S.L. Maines, D.E. Ryan and W. Levin, Biochemistry, 26, 2280 (1987).PubMedCrossRefGoogle Scholar
  34. 34.
    J.B. Schenkman, K.E. Thummel and L.V. Favreau, in Cytochrome P-450: Biochemistry and Biophysics pp. 851–854 (I. Schuster, ed), Taylor & Francis Pub., 1989.Google Scholar
  35. 35.
    R.C. Dixon, L.G. Hart and J.R. Fouts, U. Pharmacol. Exp. Ther., 133, 7 (1961).Google Scholar
  36. 36.
    M.R. Past and D.E. Cook, Biochem, Pharmacol., 31, 3329 (1982).CrossRefGoogle Scholar
  37. 37.
    J.P. Casazza, M.E. Felver and R.L. Veech, 3. Biol. Chem., 259, 231 (1984).Google Scholar
  38. 38.
    D.E. Ryan, D.R. Koop, P.E. Thomas, M.J. Coon and W. Levin, Arch. Biochem Biophys., 246, 633 (1986).PubMedCrossRefGoogle Scholar
  39. 39.
    D.R. Koop and J.P. Casazza, J. Biol. Chem., 260, 13607 (1985).PubMedGoogle Scholar
  40. 40.
    F.T. Murray, J. Orth, G. Gunsalus, J. Weisz, J.B. Li., L.S. Jefferson, N.A. Musto and C.W. Bardin, Internat. J. Androl., 4, 265 (1981).CrossRefGoogle Scholar
  41. 41.
    B.A. Merrick, M.H. Davies, D.E. Cook, T.L. Holcslaw and R.C. Schnell, Pharmacology, 30, 129, (1985).PubMedCrossRefGoogle Scholar
  42. 42.
    P. Greenspan and J. Baron, Biochem, Pharmacol, 30, 678 (1981).CrossRefGoogle Scholar
  43. 43.
    S. Eden, Endocrinology, 105, 555 (1979).PubMedCrossRefGoogle Scholar
  44. 44.
    P. Walker, J.H. Dussault, G. Alvarado-Urbina and A. Dupont, Endocrinology, 101, 782 (1977).PubMedCrossRefGoogle Scholar
  45. 45.
    S.R. Ojeda and H.E. Jameson, Endocrinology, 100, 881 (1977).PubMedCrossRefGoogle Scholar
  46. 46.
    T. Kamataki, M. Shimada, K. Maeda and R. Kato, Biochem. Biophys. Res. Comm. 130, 1247 (1985).PubMedCrossRefGoogle Scholar
  47. 47.
    R. Kato, Y. Yamazoe, M. Shimada, N. Murayama and T. Kamataki, J. Biochem., 100, 895 (1986).PubMedGoogle Scholar
  48. 48.
    C. MacGoech, E.T. Morgan, J. Halpert and J.-A. Gustafsson, J. Biol. Chem., 259, 15433 (1984).Google Scholar
  49. 49.
    Y. Yamazoe, M. Shimada, N. Murayama, S. Kawano and R. Kato, J. Biochem., 100, 1095 (1986).PubMedGoogle Scholar
  50. 50.
    R. Kato and J.R. Gillette, J. Pharmacol. Exp. Ther., 150, 285 (1965).PubMedGoogle Scholar
  51. 51.
    L.A. Reinke, H. Rosenberg and S.J. Stohs, Res. Comm. Chem. Pathol. Pharmacol., 19, 445 (1978).Google Scholar
  52. 52.
    G.S. Tannenbaum, Endocrinology, 108, 76 (1981).PubMedCrossRefGoogle Scholar
  53. 53.
    Y. Yamazoe, M. Shimada, N. Murayama and R. Kato, J. Biol. Chem., 262, 7423 (1987).PubMedGoogle Scholar
  54. 54.
    G.S. Tannenbaum, O. Rostad and D. Brazeau, Endocrinology, 104, 1733 (1979).PubMedCrossRefGoogle Scholar
  55. 55.
    P. Hahn and O. Koldovsky, in Utilization of Nutrients during postnatal development. Pergamon Press, Oxford, 1966.Google Scholar
  56. 56.
    J. Hong, J. Pan, F.J. Gonzalez, H.V. Gelboin and C.S. Yang, Biochem. Biophys. Res. Commun., 142, 1077 (1987).PubMedCrossRefGoogle Scholar
  57. 57.
    K.W. Miller and C.S. Yang, Arch. Biochem. Biophys., 229, 483 (1984).PubMedCrossRefGoogle Scholar
  58. 58.
    P.S. Schein, K.G.M.M. Alberti and D.H. Williamson, Endocrinology, 9 827 (1971).CrossRefGoogle Scholar
  59. 59.
    K. Kosugi, V. Chandramouli, K. Kumaran, W.C. Schumann and B.R. Landau J. Biol. Chem., 261, 13179 (1986).PubMedGoogle Scholar
  60. 60.
    O.E. Owen, V.E. Trapp, CL. Skutches, M.A. Mozzoli, R.D. Hoeldtke, G. Boden and G.A. Reichard, Jr., Diabetes, 31, 242 (1982).PubMedCrossRefGoogle Scholar
  61. 61.
    Y.Y. Tu, R. Peng, Z.-F. Chang and C.S. Yang. Biol. Interact., 44, 247, (1983).CrossRefGoogle Scholar
  62. 62.
    D.R. Koop, B.L. Crump, G.D. Nordblom and M.J. Coon, Proc. Natl. Acad. Sci. USA, 82, 4065 (1985).PubMedCrossRefGoogle Scholar
  63. 63.
    C.J. Patten, S.M. Ning, A.Y.H. Lu and C.S. Yang, Arch. Biochem. Biophys., 251, 629 (1986).PubMedCrossRefGoogle Scholar
  64. 64.
    A. Lefevre, H. Adler and C.S. Lieber, J. Clin, Invest., 49, 1775 (1970).CrossRefGoogle Scholar
  65. 65.
    J.M. Argiles, Trends in Biological Sciences, 11, 61 (1986).CrossRefGoogle Scholar
  66. 66.
    K. Kosugi, R.F. Scofield, V. Chandramouli, K. Kumaran, W.C. Schumann and B.R. Landau. J. Biol. Chem. 261, 3952 (1986)PubMedGoogle Scholar
  67. 67.
    Schenkman, J.B., Favreau, L.V., Jansson, I. and Mole, J.E. in Drug Metabolism from Molecules to Man, pp. 1–13, D. J. Benford, J.W. Bridges and G. G. Gibson, eds., Taylor and Francis, London, 1986.Google Scholar
  68. 68.
    D.J. Waxman, Biochem. Pharmacol., 37, 71 (1988).PubMedCrossRefGoogle Scholar
  69. 69.
    A.W. Wood, D.E. Ryan, P.E. Thomas and W. Levin, J. Biol. Chem., 258 8839 (1983).PubMedGoogle Scholar
  70. 70.
    J. Capdevila, N. Chacos, J. Werringloer, R.A. Prough and R.W. Estabrook, Proc. Natl. Acad. Sci. USA, 78, 5362 (1985).CrossRefGoogle Scholar
  71. 71.
    D. Kupfer, I. Jansson, L.V. Favreau, A.D. Theoharides and J.B. Schenkman, Arch. Biochem. Biophys., 261, 186 (1988).PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • John B. Schenkman
    • 1
  • Kenneth E. Thummel
    • 1
  • Leonard V. Favreau
    • 1
  1. 1.Department of PharmacologyUniversity of Connecticut Health CenterFarmingtonUSA

Personalised recommendations