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Loss of Liver Cytochrome P-450 Caused by Chemicals

Damage to the Apoprotein and Degradation of the Heme Moiety
  • F. De Matteis
Chapter
Part of the Handbuch der experimentellen Pharmakologie / Handbook of Experimental Pharmacology book series (HEP, volume 44)

Abstract

The most common response of the liver to the administration of foreign chemicals is an increase in the concentration of its hemoproteins (especially that of cytochrome P-450); this is one aspect of the more general adaptive response, usually referred to as induction of the drug-metabolizing system, which has been dealt with by Bock and Remmer in Chapter 2. There are cases, however, in which a chemical causes a decrease rather than an increase in the concentration of the hemoproteins of the liver, and this may result from an inhibition of their formation, from an increase in the rate of their degradation, or, finally, from a combination of these two mechanisms. Compounds which are thought to act by inhibiting heme synthesis have been discussed by Tephly in Chapter 3. The purpose of this paper is to consider in detail the effects of those chemicals that increase the rate of degradation of heme and hemoproteins in the liver. In the discussion of these effects, one particular hemoprotein—cytochrome P-450—will figure prominently. This is partly because this hemoprotein has attracted a great deal of interest in the last few years, and it is also easy to measure, so it has been extensively studied in several laboratories; also, cytochrome P-450 is particularly liable to toxic damage by a number of chemicals, apparently much more liable than the other hemoproteins of the liver, including the other cytochrome of the endoplasmic reticulum, cytochrome b5. This is due to the properties peculiar to cytochrome P-450 of interaction with several classes of potentially toxic chemicals.

Keywords

Carbon Tetrachloride Liver Microsome Heme Oxygenase Green Pigment Carbon Disulphide 
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.

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References

  1. Abbritti, G., De Matteis, F.: Decreased levels of cytochrome P-450 and catalase in hepatic porphyria caused by substituted acetamides and barbiturates. Importance of the allyl group in the molecule of the active drugs. Chem. biol. Interact. 4, 281–286 (1971)Google Scholar
  2. Abbritti, G., De Matteis, F.: Effect of 3,5-diethoxycarbonyl-l,4-dihydrocollidine on degradation of liver haem. Enzyme 16, 196–202 (1973)PubMedGoogle Scholar
  3. Alme, B., Nystrom, E.: Preparation of lipophilic anion exchangers from chlorohydroxy-propylated sephadex and cellulose. J. Chromat. 59, 45–52 (1971)Google Scholar
  4. Bakken, A.F., Thaler, M.M., Schmid, R.: Metabolic regulation of heme catabolism and bilirubin production I. Hormonal control of hepatic heme oxygenase activity. J. clin Invest. 51, 530–536 (1972)PubMedGoogle Scholar
  5. Baron, J., Tephly, T.R.: The role of heme synthesis during the induction of hepatic microsomal cytochrome P-450 and drug metabolism produced by benzpyrene. Biochem. biophys. Res. Commun. 36, 526–532 (1969)PubMedGoogle Scholar
  6. Beloff-Chain, A., Serlupi-Crescenzi, G., Catanzaro, R., Venettacci, D., Balliano, M.: Influence of iron on oxidation of reduced nicotinamide-adenine-dinucleotide phosphate in rat-liver microsomes. Biochim. biophys. Acta (Amst.) 97, 416–421 (1965)Google Scholar
  7. Bissell, D.M., Guzelian, P.S., Hammaker, L.E., Schmid, R.: Stimulation of hepatic heme oxygenase and turnover of cytochrome P-450 may be related. Fed. Proc. 33, 1246 (1974)Google Scholar
  8. Bissell, D.M., Hammaker, L.E.: Cytochrome P-450 heme and the regulation of hepatic heme oxygenase activity. Arch. Biochem. Biophys. 176, 91–102 (1976)PubMedGoogle Scholar
  9. Bissell, D.M., Hammaker, L., Schmid, R.: Hemoglobin and erythrocyte catabolism in rat liver: The separate role of parenchymal and sinusoidal cells. Blood 40, 812–822 (1972)PubMedGoogle Scholar
  10. Bock, K.W., Frohling, W., Remmer, H.: Influence of fasting and hemin on microsomal cytochromes and enzymes. Biochem. Pharmacol. 22, 1557–1564 (1973)PubMedGoogle Scholar
  11. Bond, E.J., Butler, W.H., De Matteis, F., Barnes, J.M.: Effects of carbon disulphide on the liver of rats. Brit. J. industr. Med. 26, 335–337 (1969)PubMedGoogle Scholar
  12. Bond, E.J., De Matteis, F.: Biochemical changes in rat liver after administration of carbon disulphide, with particular reference to microsomal changes. Biochem. Pharmacol. 18, 2531–2549 (1969)PubMedGoogle Scholar
  13. Butler, T.C.: Reduction of carbon tetrachloride in vivo and reduction of carbon tetrachloride and chloroform in vitro by tissues and tissue constituents. J. Pharmac, exp. Ther. 134, 311–319 (1961)Google Scholar
  14. Cameron, G.R., Karunaratne, W.E.: Carbon tetrachloride in relation to liver regeneration. J. Path. Bact. 42, 1–21 (1936)Google Scholar
  15. Catignani, G.L., Neal, R.A.: Evidence for the formation of a protein bound hydrodisulfide resulting from the microsomal mixed function oxidase catalyzed desulfuration of carbon disulfide. Biochem. biophys. Res. Commun. 65, 629–636 (1975)PubMedGoogle Scholar
  16. Chvapil, M., Ryan, J.N., Elias, S.L., Peng, Y.M.: Protective effect of zinc on carbon tetrachloride-induced liver injury in rats. Exp. molec. Path. 19, 186–196 (1973)PubMedGoogle Scholar
  17. Dalvi, R.R., Hunter, A.L., Neal, R.A.: Toxicological implications of the mixed-function oxidase catalysed metabolism of carbon disulphide. Chem. biol. Interact. 10, 347–361 (1975)PubMedGoogle Scholar
  18. Dalvi, R.R., Poore, R.E., Neal, R.A.: Studies of the metabolism of carbon disulfide by rat-liver microsomes. Life Sci. 14, 1785–1796 (1974)PubMedGoogle Scholar
  19. Daly, J.: Enzymatic oxidation of carbon. In: Concepts in Biochemical Pharmacology, Part 2, Handbook of Experimental Pharmacology, Vol. 28. Brodie, B.B. and Gillette, J.R. (eds). Berlin–Heidelberg–New York: Springer 1971Google Scholar
  20. Davison, A.N.: The conversion of sehradan (OMPA) and parathion into inhibitors of Cholinesterase by mammalian liver. Biochem. J. 61, 203–209 (1955)PubMedGoogle Scholar
  21. De Matteis, F.: Rapid loss of cytochrome P-450 and heme caused in the liver microsomes by the porphyrogenic agent 2-allyl-2-isopropylacetamide. Febs Lett. 6, 343–345 (1970)PubMedGoogle Scholar
  22. De Matteis, F.: Loss of heme in rat liver caused by the porphyrogenic agent 2-allyl-2-isopropylacetamide. Biochem. J. 124 767–777 (1971a)PubMedGoogle Scholar
  23. De Matteis, F.: Contribution to the discussion of the paper by Pimstone, N.R. et al. S. Afr. J. Lab. clin. Med. 17, 173 (1971b)Google Scholar
  24. De Matteis, F.: Mechanisms of induction of hepatic porphyria by drugs. In: Proc. 5th Int. Congr. Pharmacology, San Francisco, 2, 89–99 (1972)Google Scholar
  25. De Matteis, F.: Drug-induced destruction of cytochrome P-450. Drug Metab. Dispos. 1, 267–272 (1973)PubMedGoogle Scholar
  26. De Matteis, F.: Covalent binding of sulfur to microsomes and loss of cytochrome P-450 during the oxidative desulfuration of several chemicals. Molec. Pharmacol. 10, 849–854 (1974)Google Scholar
  27. De Matteis, F.: Iron-dependent degradation of liver heme in vivo. In: Proceedings of the International Porphyrin Meeting, Freiburg, May 1–4, 1975. Basel: S. Karger 1976Google Scholar
  28. De Matteis, F., Gibbs, A.H.: The effect of cobaltous chloride on liver heme metabolism in the rat. Evidence for inhibition of heme synthesis and for increased heme degradation. Ann. clin. Res. 8, Suppl. 17, 193–197 (1976)PubMedGoogle Scholar
  29. De Matteis, F., Seawright, A.A.S.: Oxidative metabolism of carbon disulphide by the rat. Effect of treatments which modify the liver toxicity of carbon disulphide. Chem. biol. Interact. 7, 375–388 (1973)PubMedGoogle Scholar
  30. De Matteis, F., Sparks, R.G.: Iron-dependent loss of liver cytochrome P-450 heme in vivo and in vitro. Febs Lett. 29,141–144 (1973)PubMedGoogle Scholar
  31. De Matteis, F., Unseld, A.: Increased liver heme degradation caused by foreign chemicals. A comparison of the effects of 2-allyl-2-isopropylacetamide and cobaltous chloride. Biochem. Soc. Trans. 4, 205–209 (1976)PubMedGoogle Scholar
  32. De Toranzo, E.G.D., Diaz Gomez, M.I., Castro, J.A.: Mechanism of in vivo carbon tetrachloride-induced liver microsomal cytochrome P-450 destruction. Biochem. biophys. Res. Commun. 64, 823–828 (1975)PubMedGoogle Scholar
  33. Doedens, D.J.: Metabolic fate of the porphyrogenic drug allylisopropylacetamide. Diss. Abstr. Part B Sci. Eng. 32, 2901 (1971)Google Scholar
  34. Ellin, A., Orrenius, S.: Hydroperoxide-supported cytochrome P-450-linked fatty acid hydroxylation in liver microsomes. Febs Lett. 50, 378–381 (1975)PubMedGoogle Scholar
  35. Falk, J.E.: Porphyrins and metalloporphyrins. BBA Libr. Vol. 2, p. 232. Amsterdam: Elsevier 1964Google Scholar
  36. Fong, K., McKay, P.B., Poyer, J.L., Keele, B.B., Misra, H.: Evidence that peroxidation of lysosomal membranes is initiated by hydroxyl free radicals produced during flavin enzyme activity. J. biol. Chem. 248, 7792–7797 (1973)PubMedGoogle Scholar
  37. Foreman, R.L., Maynert, E.W.: A tetrahydrofuropyrimidine as a metabolite of secobarbital. Pharmacologist 12, 255 (1970)Google Scholar
  38. Fowler, J.S.L.: Carbon tetrachloride metabolism in the rabbit. Brit. J. Pharmacol. 37, 733–737 (1969)Google Scholar
  39. Freundt, K.J., Dreher, W.: Inhibition of drug metabolism by small concentrations of carbon disulphide. Naunym-Schmiedebergs Arch. Pharmakol. exp. Path. 263, 208–209 (1969)Google Scholar
  40. Garner, R.C., McLean, A.E.M.: Increased susceptibility to carbon tetrachloride poisoning in the rat after pretreatment with oral phenobarbitone. Biochem. Pharmacol. 18, 645–650 (1969)PubMedGoogle Scholar
  41. Greene, F.E., Stripp, B., Gillette, J.R.: The effect of carbon tetrachloride on heme components and ethylmorphine metabolism in rat liver microsomes. Biochem. Pharmacol. 18, 1531–1533 (1969)PubMedGoogle Scholar
  42. Hadley, W.M., Miya, R.S., Bousquet, W.F.: Cadmium inhibition of hepatic drug metabolism in the rat. Toxicol, appl. Pharmacol. 28, 284–291 (1974)Google Scholar
  43. Hafeman, D.F., Hoekstra, W.F.: Protection by vitamin E and selenium against lipid peroxidation in vivo as measured by ethane evolution. Fed. Prod. 34, 939 (1975)Google Scholar
  44. Harvey, D.J., Glazener, L., Stratton, C., Johnson, D.B., Mill, R.M., Horning, E.C., Horning, M.G.: Detection of epoxides of allyl-substituted barbiturates in rat urine. Res. Commun. chem. Path. Pharmacol. 4, 247–260 (1972)Google Scholar
  45. Haurowitz, F., Groh, M., Gansinger, G.: Mechanism and kinetics of the hemin-catalyzed oxidation of linoleate in the oil-water interface. J. biol. Chem. 248, 3810–3818 (1973).PubMedGoogle Scholar
  46. Högberg, J.: Iron induced lipid peroxidation in rat liver. A study on mechanisms and consequences. Dissertation, Karolińska Institutet, Stockholm 1975Google Scholar
  47. Högberg, J., Bergstrand, A., Jakobsson, S.V.: Lipid peroxidation of rat-liver microsomes. Its effect on the microsomal membrane and some membrane-bound microsomal enzymes. Europ. J. Biochem. 37, 51–59 (1973)PubMedGoogle Scholar
  48. Högberg, J., Orrenius, S., Larson, R.E.: Lipid peroxidation in isolated hepatocytes. Europ. J. Biochem. 50, 595–602 (1975)PubMedGoogle Scholar
  49. Hrycay, E.G., Gustafsson, J., Ingelman-Sundberg, M., Ernster, L.: Sodium periodate, sodium chlorite, and organic hydroperoxides as hydroxylating agents in hepatic microsomal steroid hydroxylation reactions catalyzed by cytochrome P-450. Febs Lett. 56, 161–165 (1975)PubMedGoogle Scholar
  50. Hrycay, E.G., O’Brien, P.J.: Cytochrome P-450 as a microsomal peroxide utilizing a lipid peroxide substrate. Arch. Biochem. Biophys. 147, 14–27 (1971)PubMedGoogle Scholar
  51. Hunter, A., Neal, R.A.: Response of the hepatic mixed function oxidase system to thionosulfur-containing compounds. Pharmacologist 16, 239 (1974)Google Scholar
  52. Hupka, A.L., Karler, R.: Biotransformation of ethylmorphine and heme by isolated parenchymal and reticuloendothelial cells of rat liver. J. reticuloendoth. Soc. 14, 225–241 (1973)Google Scholar
  53. Ivanetich, K.M., Marsh, J.A., Bradshaw, J.J., Kaminsky, L.S.: Fluroxene (2,2,2-trifluoro-ethyl vinyl ether) mediated destruction of cytochrome P-450 in vitro. Biochem. Pharmacol. 24, 1933–1936 (1975)PubMedGoogle Scholar
  54. Jackson, A.H., Jackson, J.R.: Unpublished work quoted by Jackson, A.H. Heme catabolism. In: Iron in Biochemistry and Medicine. Jacobs, A., Worwood, M. (eds.), pp. 145–182. London — New York: Academic Press 1974Google Scholar
  55. Jaeger, R.J., Conolly, R.B., Murphy, S.D.: Diurnal variations of hepatic glutathione concentration and its correlation with 1,1-dichloroethylene inhalation toxicity in rats. Res. Commun, ehem. Path. Pharmacol. 6, 465–471 (1973)Google Scholar
  56. Jose, P.J., Slater, T.F., Sawyer, B.C.: The effects of starvation on rat liver microsomal inosine concentrations, reduced nicotinamide-adenine dinucleotide-linked lipid-peroxidation system and other microsomal enzymes. Biochem. Soc. Trans. 1, 939–941 (1973)Google Scholar
  57. Kadlubar, F.F., Morton, K.C., Ziegler, D.M.: Microsomal-catalyzed hydroperoxide-dependent C-oxidation of amines. Biochem. biophys. Res. Commun. 54, 1255–1261 (1973)PubMedGoogle Scholar
  58. Kamataki, T., Kitagawa, H.: Effects of lipid peroxidation on activities of drug-metabolizing enzymes in liver microsomes of rats. Biochem. Pharmacol. 22, 3199–3207 (1973)PubMedGoogle Scholar
  59. Kokatnur, M.G., Bergan, J.G., Draper, H.H.: Observations on the decomposition of hemin by fatty acid hydroperoxides. Proc. Soc. exp. Biol. (N.Y.) 123, 314–317 (1966)Google Scholar
  60. Landaw, S.A., Callahan, E.W. Jr., Schmid, R.: Catabolism of heme in vivo: comparison of the simultaneous production of bilirubin and carbon monoxide. J. clin. Invest. 49, 914–925 (1970)PubMedGoogle Scholar
  61. Lemberg, R., Falk, J.E.: Comparison of heme a, the dichroic heme of heart muscle, and of porphyrin a with compounds of known structure. Biochem. J. 49, 674–683 (1951)PubMedGoogle Scholar
  62. Levin, W., Jacobson, M., Kuntzman, R.: Incorporation of radioactive δ-aminolevulinic acid into microsomal cytochrome P-450. Selective breakdown of the hemoprotein by allylisopropylacetamide and carbon tetrachloride. Arch. Biochem. Biophys. 148, 262–269 (1972a)PubMedGoogle Scholar
  63. Levin, W., Jacobson, M., Sernatinger, E., Kuntzman, R.: Breakdown of cytochrome P-450 heme by secobarbital and other allyl-containing barbiturates. Drug. Metab. Dispos. 1, 275–284 (1973a)PubMedGoogle Scholar
  64. Levin, W., Kuntzman, R.: Biphasic decrease of radioactive hemoprotein from liver microsomal CO-binding particles. Effect of 3-methylcholanthrene. J. biol. Chem. 244, 3671–3676 (1969)PubMedGoogle Scholar
  65. Levin, W., Lu, A.Y.H., Jacobson, M., Kuntzman, R., Poyer, J.L., McCay, P.B.: Lipid peroxidation and the degradation of cytochrome P-450 heme. Arch. Biochem. Biophys. 158, 842–852 (1973b)PubMedGoogle Scholar
  66. Levin, W., Sernatinger, E., Jacobson, M., Kuntzman, R.: Destruction of cytochrome P-450 by secobarbital and other barbiturates containing allyl groups. Science 176, 1341–1343 (1972b)PubMedGoogle Scholar
  67. Little, C., O’Brien, P.J.: An intracellular GSH-peroxidase with a lipid peroxide substrate. Biochem. biophys. Res. Commun. 31, 145–150 (1968)PubMedGoogle Scholar
  68. Lucier, G.W., Matthews, H.B., Brubaker, P.E., Klein, R., McDaniel, O.S.: Effects of methylmercury in microsomal mixed-function oxidase components of rodents. Molec. Pharmacol. 9, 237–246 (1973)Google Scholar
  69. Magos, L., Butler, W.H.: Effect of phenobarbitone and starvation on hepatotoxicity in rats exposed to carbon disulphide vapour. Brit. J. industr. Med. 29, 95–98 (1972)PubMedGoogle Scholar
  70. Maines, M.D., Anders, M.W., Muller-Eberhard, U.: Studies on heme transfer from microsomal hemoproteins to heme-binding plasma proteins. Molec. Pharmacol. 10, 204–213 (1974)Google Scholar
  71. Maines, M.D., Kappas, A.: Cobalt induction of hepatic heme oxygenase; with evidence that cytochrome P-450 is not essential for this enzyme activity. Proc. nat. Acad. Sci. (Wash.) 71, 4293–4297 (1974)Google Scholar
  72. Maines, M.D., Kappas, A.: Regulation of hepatic heme metabolism by metals. International Porphyrin Meeting, Freiburg, May 1–4 1975. Abstracts page 9 (1975a)Google Scholar
  73. Maines, M.D., Kappas, A.: Cobalt stimulation of heme degradation in the liver. Dissociation of microsomal oxidation of heme from cytochrome P-450. J. biol. Chem. 250, 4171–4177 (1975b)PubMedGoogle Scholar
  74. Maines, M.D., Kappas, A.: Studies on the mechanism of induction of heme oxygenase by cobalt and other metal ions. Biochem. J. 154, 125–131 (1976)PubMedGoogle Scholar
  75. McCay, P.B., Pfeifer, P.M., Stipe, W.H.: Vitamin E protection of membrane lipids during electron transport functions. Ann. N.Y. Acad. Sci. 203, 62–73 (1972)PubMedGoogle Scholar
  76. McDonagh, A.F., Pospisil, R., Meyer, U.A.: Degradation of hepatic heme to porphyrins and oxophlorins in rats treated with 2-allyl-2-isopropylacetamide. Biochem. Soc. Trans. 4, 297–298 (1976)PubMedGoogle Scholar
  77. McLean, A.E.M.: Effect of hexane and carbon tetrachloride on microsomal cytochrome (P-450). Biochem. Pharmacol. 16, 2030–2033 (1967)PubMedGoogle Scholar
  78. McLean, A.E.M., McLean, E.K.: The effect of diet and l,l,l-trichloro-2,2-bis-(p-chlorophenyl)-ethane (DDT) on microsomal hydroxylating enzymes and on sensitivity of rats to carbon tetrachloride poisoning. Biochem. J. 100, 564–571 (1966)PubMedGoogle Scholar
  79. Meyer, U.A., Marver, H.S.: Chemically induced porphyria. Increased microsomal heme turn-over after treatment with allylisopropylacetamide. Science 171, 64–66 (1971)PubMedGoogle Scholar
  80. Murakami, K., Mason, H.S.: An electron spin resonance study of microsomal Fex. J. biol. Chem. 2421, 1102–1110 (1967)Google Scholar
  81. Nakamura, M., Yasukochi, Y., Minakami, S.: Effect of cobalt on heme biosynthesis in rat liver and spleen. J. Biochem. (Tokyo) 78, 373–380 (1975)Google Scholar
  82. Nakatsugawa, T., Dahm, P.A.: Microsomal metabolism of parathion. Biochem. Pharmacol. 16, 25–38 (1967)Google Scholar
  83. Nakatsugawa, T., Tolman, N.M., Dahm, P.A.: Degradation and activation of parathion analogues by microsomal enzymes. Biochem. Pharmacol. 17, 1517–1528 (1968).PubMedGoogle Scholar
  84. Neal, R.A.: Studies on the metabolism of diethyl-4-nitrophenylphosphorothionate (parathion) in vitro. Biochem. J. 103, 183–191 (1967)PubMedGoogle Scholar
  85. Nilsson, R., Orrenius, S., Ernster, L.: The TPNH-dependent oxidation of luminol catalyzed by rat liver microsomes. Biochem. biophys. Res. Commun. 17, 303–309 (1964)Google Scholar
  86. Nishibayashi, H., Omura, T., Sato, R., Estabrook, R.W.: Comments on the absorption spectra of hemoprotein P-450. In: Structure and Function of Cytochromes. Okunuki, K., Kamon, M.D., Sekuzu, I. (eds.), pp. 658–665. Baltimore — Manchester: University Park Press 1968Google Scholar
  87. O’Brien, R.D.: Activation of thionophosphates by liver microsomes. Nature (Lond.) 183, 121–122 (1959)Google Scholar
  88. O’Brien, R.D.: Desulfuration. In: Proc. 1st Intern. Pharmacol. Meeting, Stockholm, 6, 111–119 (1961)Google Scholar
  89. O’Carra, P., Colleran, E.: Heme catabolism and coupled oxidation of hemoproteins. Febs Lett. 5, 295–298 (1969)Google Scholar
  90. Orrenius, S., Dallner, G., Ernster, L.: Inhibition of the TPNH-linked lipid peroxidation of liver microsomes by drugs undergoing oxidative demethylation. Biochem. biophys. Res. Commun. 14, 329–334 (1964)PubMedGoogle Scholar
  91. Pederson, T.C., Aust, S.D.: Relationship between reduced nicotinamide adenine dinucleotide phosphate-dependent lipid peroxidation and drug hydroxylation in rat liver microsomes. Biochem. Pharmacol. 23, 2467–2469 (1974)PubMedGoogle Scholar
  92. Pederson, T.C., Aust, S.D.: The mechanism of liver microsomal lipid peroxidation. Biochim. biophys. Acta (Amst.) 385, 232–241 (1975)Google Scholar
  93. Pederson, T.C., Buege, J.A., Aust, S.D.: Microsomal electron transport. The role of reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase in liver microsomal lipid peroxidation. J. biol. Chem. 248, 7134–7141 (1973)PubMedGoogle Scholar
  94. Penning, W., Scoppa, P.: Breakdown of cytochrome P-450 in acute lead poisoning. IUPHAR Satellite Symposium on Active Intermediates: Formation, Toxicity and Inactivation, Turku, Finland, July 26–27, 1975, Abstracts p. 41Google Scholar
  95. Pimstone, N.R., Engel, P., Tenhunen, R., Seitz, P.T., Marver, H.S., Schmid, R.: Further studies of microsomal heme oxygenase: mechanism for stimulation of enzyme activity and cellular localization. S. Afr. J. Lab. clin. Med. 17, 169–173 (1971)Google Scholar
  96. Poore, R.E., Neal, R.A.: Evidence for extrahepatic metabolism of parathion. Toxicol, appl. Pharmacol. 23, 759–768 (1972)Google Scholar
  97. Ptashne, K.A., Wolcott, R.M., Neal, R.A.: Oxygen-18 studies on the chemical mechanisms of the mixed function oxidase catalysed desulfuration and dearylation reactions of parathion. J. Pharmacol, exp. Ther. 179, 380–385 (1971)Google Scholar
  98. Radtke, H.E., Coon, M.J.: Role of cytochrome P-450 in lipid peroxidation and peroxide-dependent drug hydroxy lation. Fed. Proc. 33, 588 (1974)Google Scholar
  99. Rahimtula, A.D., O’Brien, P.J.: Hydroperoxide dependent O-dealkylation reactions catalyzed by liver microsomal cytochrome P-450. Biochem. biophys. Res. Commun. 62, 268–275 (1975)PubMedGoogle Scholar
  100. Recknagel, R.O.: Carbon tetrachloride hepatotoxicity. Pharmacol. Rev. 19, 145–208 (1967)PubMedGoogle Scholar
  101. Recknagel, R.O., Glende, E.A. Jr., Hruszkewycz, A.M.: New data supporting an obligatory role for lipid peroxidation in carbon tetrachloride induced loss of aminopyrine demethylase, cytochrome P-450 and glucose-6-phosphatase. IUPHAR Satellite Symposium on Active Intermediates: Formation, Toxicity and Inactivation, Turku, Finland, July 26–27, 1975, Abstracts, P. 26Google Scholar
  102. Recknagel, R.O., Lombardi, B.: Studies of biochemical changes in subcellular particles of rat liver and their relationship to a new hypothesis regarding the pathogenesis of carbon tetrachloride fat accumulation. J. biol. Chem. 236, 564–569 (1961)PubMedGoogle Scholar
  103. Reiner, O., Athanassopoulos, S., Hellmer, K.H., Murray, R.E., Uehleke, H.: Bidlung von Chloroform aus Tetrachlorkohlenstoff in Lebermikrosomen, Lipidperoxidation und Zerstörung von Cytochrom P-450. Arch. Toxikol. 29, 219–233 (1972)PubMedGoogle Scholar
  104. Reiner, O., Uehleke, H.: Bindung von Tetrachlorkohlenstoff an reduziertes mikrosomales Cytochrom P-450 und an Häm. Hoppe-Seylers Z. physiol. Chem. 352, 1048–1052 (1971)PubMedGoogle Scholar
  105. Riely, CA., Cohen, G., Lieberman, M.: Ethane evolution: A new index of lipid peroxidation. Science 183, 208–210 (1974)PubMedGoogle Scholar
  106. Ross, W.E., Simrell, C., Oppelt, W.W.: Sex-dependent effects of cyclic AMP on the hepatic mixed function oxidase system. Res. Commun, chem. Path. Pharmacol. 5, 319–332 (1973)Google Scholar
  107. Rothwell, J.D., Lacroix, S., Sweeney, G.D.: Evidence against a regulatory role for heme oxygenase in hepatic synthesis. Biochim. biophys. Acta (Amst.) 304, 871–874 (1973)Google Scholar
  108. Rotruck, J.T., Pope, A.L., Ganther, H.E., Swanson, A.B., Hafeman, D.G., Hoekstra, W.G.: Selenium biochemical role as a component of glutathione peroxidase. Science 179, 588–590 (1973)PubMedGoogle Scholar
  109. Sasame, H.A., Castro, J.A., Gillette, J.R.: Studies on the destruction of liver microsomal cytochrome P-450 by carbon tetrachloride administration. Biochem. Pharmacol. 17, 1759–1768 (1968)PubMedGoogle Scholar
  110. Schacter, B.A., Marver, H.S., Meyer, U.A.: Hemoprotein catabolism during stimulation of microsomal lipid peroxidation. Biochim. biophys, Acta (Amst.) 279, 221–227 (1972)Google Scholar
  111. Schacter, B.A., Marver, H.S., Meyer, U.A.: Heme and hemoprotein catabolism during stimulation of microsomal lipid peroxidation. Drug Metab. Dispos. 1, 286–290 (1973)PubMedGoogle Scholar
  112. Schacter, B.A., Waterman, M.R.: Activity of various metalloporphyrin protein complexes with microsomal heme oxygenase. Life Sci. 14, 47–53 (1974)PubMedGoogle Scholar
  113. Schmid, R., McDonagh, A.F.: The enzymatic formation of bilirubin. Ann. N.Y. Acad. Sci. 244, 533–552 (1975)PubMedGoogle Scholar
  114. Schwartz, S., Ikeda, K.: Studies of porphyrin synthesis and interconversion, with special reference to certain green porphyrins in animals with experimental hepatic porphyria. In: Ciba Found, Symp.: Porphyrin Biosynthesis and Metabolism. Wolstenholme, G.E.W. (ed.), pp. 209–226. London: J. and A. Churchill Ltd. 1955Google Scholar
  115. Scoppa, P., Roumengous, M., Penning, W.: Hepatic drug-metabolizing activity in lead-poisoned rats. Experientia (Basel) 29, 970–972 (1973)Google Scholar
  116. Scott, M.L., Noguchi, T., Combs, G.F. Jr.: New Evidence concerning mechanisms of action of vitamin E and selenium. Vitam. Horm. 32, 429–444 (1974)Google Scholar
  117. Seawright, A.A., Hrdlicka, J., De Matteis, F.: The hepatotoxicity of 0,0-diethyl, O-phenyl phosphorothionate (SV1) for the rat. Brit. J. exp. Path. 57, 16–22 (1976)PubMedGoogle Scholar
  118. Seawright, A.A., McLean, A.E.M.: The effect of diet on carbon tetrachloride metabolism. Biochem. J. 105, 1055–1060 (1967)PubMedGoogle Scholar
  119. Shah, H.C., Carlson, G.P.: Alteration by phenobarbital and 3-methylcholanthrene of functional and structural changes in rat liver due to carbon tetrachloride inhalation. J. Pharmacol. exp. Ther. 193, 281–292 (1975)PubMedGoogle Scholar
  120. Slater, T.F.: Free Radical Mechanisms in Tissue Injury. London: Pion Ltd. 1972Google Scholar
  121. Slater, T.F., Sawyer, B.C.: The stimulatory effects of carbon tetrachloride on peroxidative reactions in rat liver fractions in vitro. Interaction sites in the endoplasmic reticulum. Biochem. J. 123, 815–821 (1971)PubMedGoogle Scholar
  122. Smuckler, E.A., Arrenius, E., Hultin, T.: Alterations in microsomal electron transport, oxidative N-demethylation and azo-dye cleavage in carbon tetrachloride and dimethylnitrosamine-induced liver injury. Biochem. J. 103, 55–64 (1967)PubMedGoogle Scholar
  123. Stern, J.O., Peisach, J.: A model compound study of the CO-adduct of cytochrome P-450. J. biol. Chem. 249, 7495–7498 (1974)PubMedGoogle Scholar
  124. Tappel, A.L.: Unsaturated lipid oxidation catalyzed by hematin compounds. J. biol. Chem. 217, 721–733 (1955)PubMedGoogle Scholar
  125. Tappel, A.L.: Vitamin E and free radical peroxidation of lipids. Ann. N.Y. Acad. Sci. 203, 12–28 (1972)PubMedGoogle Scholar
  126. Tateishi, N., Higashi, T., Shinya, S., Naruse, A., Sakamoto, Y.: Studies on the regulation of glutathione level in rat liver. J. Biochem. 75, 93–103 (1974)PubMedGoogle Scholar
  127. Tephly, T.R., Hibbeln, P.: The effect of cobalt chloride administration on the synthesis of hepatic microsomal cytochrome P-450. Biochem. biophys. Res. Commun. 42, 589–595 (1971)PubMedGoogle Scholar
  128. Tephly, T.R., Webb, C., Trussler, P., Kniffen, F., Hasegawa, E., Piper, W.: The regulation of heme synthesis related to drug metabolism. Drug Metab. Dispos. 1, 259–265 (1973)PubMedGoogle Scholar
  129. Uehleke, H., Hellmer, K.H., Tabarelli, S.: Binding of 14C-carbon tetrachloride to microsomal proteins in vitro and formation of CHC13 by reduced liver microsomes. Xenobiotica 3, 1–11 (1973)PubMedGoogle Scholar
  130. Unseld, A., De Matteis, F.: Isolation and partial characterisation of green pigments produced in rat liver by 2-allyl-2-isopropylacetamide. In: Proceedings of the International Porphyrin Meeting, Freiburg, May 1–4, 1975. Basel: S. Karger 1976Google Scholar
  131. Vainio, H.: Defective drug metabolism in rat liver in endotoxin shock. Ann. Med. exp. Biol. Finn. 51, 65–68 (1973)Google Scholar
  132. Wada, O., Yano, Y., Urata, G., Nakao, K.: Behaviour of hepatic microsomal cytochromes after treatment of mice with drugs known to disturb porphyrin metabolism in liver. Biochem. Pharmacol. 17, 595–603 (1968).PubMedGoogle Scholar
  133. Waterfield, M.D., Del Favero, A., Gray, C.H.: Effect of l,4-dihydro-3,5-dicarbethoxycollidine on hepatic microsomal heme, cytochrome b5 and cytochrome P-450 in rabbits and mice. Biochim, biophys. Acta (Amst.) 184, 470–473 (1969)Google Scholar
  134. Weiner, M., Buterbaugh, G.G., Blake, D.A.: Inhibition of hepatic drug metabolism by cyclic 3′,5′-adenosine monophosphate. Res. Commun, chem. Path. Pharmacol. 3, 249–263 (1972)Google Scholar
  135. Williams, R.T.: Detoxication Mechanisms, 2nd, ed., p. 181. London: Chapman and Hall Limited 1959Google Scholar
  136. Wills, E.D.: Lipid peroxide formation in microsomes. The role of non-heme iron. Biochem. J. 113, 325–332 (1969a)PubMedGoogle Scholar
  137. Wills, E.D.: Lipid peroxide formation in microsomes. Relationship of hydroxylation to lipid peroxide formation. Biochem. J. 113, 333–341 (1969b)PubMedGoogle Scholar
  138. Wills, E.D.: Effects of iron overload on lipid peroxide formation and oxidative demethylation by the liver endoplasmic reticulum. Biochem. Pharmacol. 21, 239–247 (1972)PubMedGoogle Scholar
  139. Yoshida, T., Takahashi, S., Kikuchi, G.: Partial purification and reconstitution of the heme oxygenase system from pig spleen microsomes. J. Biochem. 75, 1187–1191 (1974)PubMedGoogle Scholar
  140. Yu, C. A., Gunsalus, I.C.: Cytochrome P-450 cam. IL Interconversion with P-420. J. biol. Chem. 249, 102–106 (1974)PubMedGoogle Scholar

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© Springer-Verlag Berlin Heidelberg 1978

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  • F. De Matteis

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