PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
1992 | 39 | 4 |

Tytuł artykułu

Effect of mesitylene on ethanol metabolism in rat liver microsomes

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Increased catalase activity was observed in the liver microsomal fraction of ethanol-treated rats (10% v/v aqueous ethanol solution per os for 5 weeks). In contrast, cytochrome P-450 concentration and specific activity of NADPH-cytochrome c reductase remained at the same level as in the liver of control rate (drinking water). The ratio of microsomal H202-generation to catalase activity was lower In the "ethanol" group than in the control one. This phenomenon seems to be related to the increased contribution of the "peroxidatic" reaction (increased rate of ethanot oxidation). Administration of mesitylene (1,3,5-trimethylbenzene) by gastric tube for 3 days (5 mmoles per kg daily) increased cytochrome P-450 concentration» specific activity of NADPH-cytochrome c reductase and ethanol metabolism.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

39

Numer

4

Opis fizyczny

p.335-343

Twórcy

  • Medical Academy, Debinki 1, 80-211 Gdansk, Poland
autor

Bibliografia

  • 1. Thompson, R. P. H. (1986) Measuring the damage-ethanol and the liver. Gut, 27,751 -755.
  • 2. Lieber, C. S. & De Carli, L. M. (1968) Ethanol oxidation by hepatic microsomes: Adaptive increase after ethanol feeding. Science, 162,917 - 918.
  • 3. Lieber, C. S. & De Carli, L. M. (1970) Hepatic microsomal ethanol-oxidizing system. In vitro characteristics and adaptive properties in vivo. J. Biol Chem245,2505 - 2512.
  • 4. Roach, M. K., Reese, W. N. & Creaven, P. J. (1969) Ethanol oxidation in the microsomal fraction of rat liver. Biockem. Biophys. Res. Commun., 36,596 - 602.
  • 5. Vatsis, K. P. & Schulman, M. P. (1973) Absence of ethanol metabolism in "acatalatic" hepatic microsomes that oxidize drugs. Biochem. Biophys. Res. Commun52,588 - 594.
  • 6. Vatsis, K. P. & Schulman, M. P. (1977) Pathways of ethanol oxidation in hepatic microsomes of acatalasemic (csb) mice; in Advances in Experimental Medicine and Biology. Alcohol intoxication and withdrawal - Ilia. Biological aspects of ethanol (Gross, M. M., ed.) Vol. 85 A, pp. 303 - 317, Plenum Press, New York and London.
  • 7. Peters, T. J. (1982) Ethanol metabolism. Br. Med. Bull., 38,17 - 20.
  • 8. Ohnishi, K. & Lieber, C. S. (1977) Reccmstitution of the microsomal ethanol oxidizing system. Qualitative and quantitative changes of cytochrome P-450 after chronic ethanol consumption. J. Biol Chem., 252,7124-7137.
  • 9. Nebert, D. W., Nelson, D. R., Coon, M. J., Estabrook, R. W., Feyeneisen, R., Fujii- Kuriyama, Y., Gonzalez, F. J., Guengeiich, F. P., Gunsalus, I. C., Johnson, E. F., Lopa*, J. C., Sato, R., Waterman, M. R. & Waxman, D. J. (1991) The P-450 superfamily: Update on new sequences, gene mapping, and recommended nomenclature. DNA and Cell Biology, 10,1 -14.
  • 10. Koop, D. R., Morgan* E. T., Tarr, G. E. & Coon, M. J. (1982) Purification and characterization of a unique isozyme of cytochrome P-450 from liver microsomes of ethanol-treated rabbits. 7. Biol Chem., 257,8472 - 8480.
  • 11. Morgan, E, T„ Koop, D. R. & Coon, M. J. (1982) Catalytic activity of cytochrome P-450 isozyme 3a isolated from liver microsomes of ethanol-treated rabbits. Oxidation of alcohols. J, Biol Chem., 257,13951 - 13957.
  • 12. Koop, D. R., Crump, B. L„ Nordblom, G. D. & Coon, M. J. (1985) Immunochemical evidence for induction of the alcohol-oxidizing cytochrome P-450 of rabbit liver micro­somes by diverse agents: ethanol, imidazole, trichloroethylene, acetone, pyrazole and isoniazid. Proc. Natl Acad. Sci. U.S.A., 82,4065 - 4069.
  • 13. Thomas, P. E., Bandiera, S„ Maines, S, L„ Ryan, D. E. & Levin, W. (1987) Regulation of cytochrome P-450j, a high-affinity W-nitrosodimethylamine demethylase, in rat hepatic microsomes. Biochemistry, 26,2280 - 2289.
  • 14. Keilin, D. & Hartree, E. F. (1945) Properties of catalase. Catalysis of coupled oxidation of alcohols. Biochem. J., 39,293 - 301.
  • 15. Chance, B., Sies, H. & Boveris, A. (1979) Hydroperoxide metabolism in mammalian organs. Physiol Rev., 59,527 - 605.
  • 16. Deisseroth, A. & Dounce, A. L. (1970) Catalase: Physical and chemical properties, mechanism of catalysis and physiological role. Physiol Rev., 50, 319 - 375.
  • 17. Percy, M. E. (1984) Catalase: an old enzyme with a new role? Can. J. Biochem. Cell Biol., 62, 1006 -1014.
  • 18. Oshino, N., Oshino, R. & Chance, B. (1973) The characteristics of the peroxidatic reaction of catalase in ethanol oxidation. Biochem. J131,555 - 567.
  • 19. Pyykkft, K. (1980) Effects of methylbenzenes on microsomal enzymes in rat liver, kidney and lung. Biochim. Biophys. Acta633,1-9.
  • 20. Teschke, R., Hasumura, Y. & Lieber, C. S. (1976) Hepatic ethanol metabolism: Respective roles of alcohol dehydrogenase, the microsomal ethanol-oxidizing system, and catalase. Arch. Biochem. Biophys175,635 - 643.
  • 21. Gupta, N. K. & Robinson, W. G. (1966) Coupled oxidation reduction activity of liver alcohol dehydrogenase. Biochim. Biophys. Acta, 118,431 - 434.
  • 22. Omura, T. & Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes. J. Biol Chem., 239,2370 - 2378.
  • 23. Johnson, R. K., Mazel, P., Donahue, J. D. & Jondorf, W. R. (1971) Factors involved in the inhibition of drug metabolism by (-)-emetine. Biochem. Pharmacol, 20,955 - 966.
  • 24. Philips, A. H. & Langdon, R. G. (1962) Hepatic triphosphopyridine nucleotide- cytochrome c reductase: isolation, characterization and kinetic studies. J. Biol Chem., 237,2652 - 2660.
  • 25. Nash, T. (1953) The colorimetric estimation of formaldehyde by means of the Hantzsch reaction. Biochem. J., 55,416 - 421.
  • 26. Wills, E. D. (1969) Lipid peroxide formation in microsomes. Relationship of hydroxylation to lipid peroxide formation. Biochem. J113, 333 - 341.
  • 27. Beers, R. F. & Sizer, J. W. (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol Chem., 195,133 - 140.
  • 28. Cederbaum, A. J., Dicker, E., Rubin, E. & Cohen, G. (1979) Effect of thiourea on microsomal oxidation of alcohols and associated microsomal functions. Biochemistry, 18, 1187-1191.
  • 29. Layne, E. (1957) Spectrophotometric and turbidimetric methods for measuring proteins; in Methods in Enzymology. (Colowick, S. P. & Kaplan, N. O., eds.) Vol 3, pp. 450 -451.
  • 30. Howell, S. R.t Christian, J. E. & Isom, G. E. (1986) The hepatotoxic potential of combined toluene-chronic ethanol exposure. Arch. Toxicol., 59,45 - 50.
  • 31. Jansson, I. & Schenkman, J. B. (1973) Evidence against participation of cytochrome 1)5 in the hepatic microsomal mixed-function oxidase reaction. Mol. Pharmacol., 9,840 - 845.
  • 32. Levin, W., Ryan, D., West, S. & Lu, A. Y. H. (1974) Preparation of partially purified, lipid-depleted cytochrome P-450 and reduced nicotinamide adenine dinucleotide phos- phate-cytochrome c reductase from rat liver microsomes. J. Biol. Chem., 249,1747-1754.
  • 33. Van der Hoeven, T. A., Haugen, D. A. & Coon, M. J. (1974) Cytochrome P-450 purified to apparent homogeneity from phenobarbital-induced rabbit liver microsomes: catalytic activity and other properties. Biochem. Biophys. Res. Commun60, 569 - 575.
  • 34. Koop, D. R. & Coon, M. J. (1984) Purification of liver microsomal cytochrome P-450 isozymes 3a and 6 from imidazole treated rabbits. Evidence for the identity of isozyme 3a with the form obtained by ethanol treatment. Mol Pharmacol., 25,494 - 501.
  • 35. Cohen, B. S. & Estabrook, R. W. (1971) Microsomal electron transport reactions. I. Interaction of reduced triphosphopyridine nucleotide during the oxidative demethylation of aminopyrine and cytochrome bs reduction. Arch. Biochem. Biophys., 143,37 - 45.
  • 36. Correia, M. A. & Mannedng, G. J. (1973) Reduced diphosphopyridine nucleotide synergism of the reduced triphosphopyridine nucleotide-dependent mixed-function oxidase system of hepatic microsomes. I. Effects of activation and inhibition of the fatty acyl coenzyme A desaturation system. Mol. Pharmacol., 9,455 - 469.
  • 37. Hildebrandt, A. & Estabrook, R. W. (1971) Evidence for the participation of cytochrome bs in hepatic microsomal mixed-function oxidation reactions. Arch. Biochem. Biophys143,66 - 79.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-177824e7-fb4b-4ef9-a8c3-816823671c00
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.