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Xenobiotica
the fate of foreign compounds in biological systems
Volume 32, 2002 - Issue 11
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Research Article

Comparison of rat and human cytochrome P450 (CYP) sources of N-alkylprotoporphyrin IX. Formation after interaction with porphyrinogenic xenobiotics: studies with cDNA-expressed single CYP enzymes

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Pages 997-1006 | Published online: 22 Sep 2008

References

  • BORNHEIM, L. M., UNDERWOOD, M. C., CALDERA, P., BETTIE, A. E., TRAGER, W. F., WRIGHTON, S. A. and CORREIA, M. A., 1987, Inactivation of multiple hepatic cytochrome P-450 isozymes in rats by allylisopropylacetamide: mechanistic implications. Molecular Pharmacology, 32, 299–308.
  • DE MATTEIS, F., GIBBS, A. H., Cam-um, L. and FRANCIS, J., 1980, Substrate-dependent irreversible inactivation of cytochrome P-450: conversion of its haem moiety into modified porphyrins. Ciba Foundation Symposium, 76, 119–139.
  • DE MATTEIS, F. and MARKS, G. S., 1996, Cytochrome P450 and its interactions with the heme biosynthetic pathway. Canadian Journal of Physiology and Pharmacology, 74, 1–8.
  • LAVIGNE, J. A., NAKATSU, K. and MARKS, G. S., 2002, Identification of human hepatic Cytochrome P450 sources of N-alkylprotoporphyrin IX after interaction with porphyrinogenic xenobiotics. Drug Metabolism and Disposition 30, 788–794.
  • MARKS, G. S., MCCLUSKEY, S. A., MACKIE, J. E., RIDDICK, D. S. and JAMES, C. A., 1988, Disruption of hepatic heme biosynthesis after interaction of xenobiotics with cytochrome P-450. FASEB Journal, 2, 2774–2783.
  • MCNAMEE, J. P. and MARKS, G. S., 1996, Cytochrome P4503A is the major source of N-vinyl-protoporphyrin IX formation after administration of 3- [2-(24-methylsydnone to untreated and dexamethasone- pretreated rats. Drug Metabolism and Disposition, 24, 872–878.
  • ORTIZ DE MONTELLANO, P. R. and CORREIA, M. A., 1996, Inhibition of cytochrome P450 enzymes. In P. R. Ortiz de Montellano (ed.), Cytochrome P450: Structure, Mechanism, and Biochemistry (New York: Plenum), pp. 305–364.
  • ORTIZ DE MONTELLANO, P. R. and GRAB, L. A., 1986, Inactivation of cytochrome P450 during catalytic oxidation of a 3-[(arylthio)ethyl]sydnone: N-vinyl heme formation via insertion into the Fe-N Bond. Journal of the American Chemical Society, 108, 5584–5589.
  • ORTIZ DE MONTELLANO, P. R. and Mico, B. A., 1981, Destruction of cytochrome P-450 by allylisopropylacetamide is a suicidal process. Archives in Biochemistry and Biophysics, 206, 43–50.
  • RIDDICK, D. S., PARK, S. S., GELBOIN, H. V. and MARKS, G. S., 1990, Effects of 4-alkyl analogues of 3,5-diethoxycarbony1-1,4-dihydro-2,4,6-trimethylpyridine on hepatic cytochrome P-450 heme, apoproteins, and catalytic activities following in vivo administration to rats. Molecular Pharmacology, 37, 130–136.
  • RODRIGUES, A. D., 1999, Integrated cytochrome P450 reaction phenotyping: attempting to bridge the gap between cDNA-expressed cytochromes P450 and native human liver microsomes. Biochemical Pharmacology, 57, 465–480.
  • SUTHERLAND, E. P., MARKS, G. S., GRAB, L. A. and ORTIZ DE MONTELLANO P. R, 1986, Porphyrinogenic activity and ferrochelatase-inhibitory activity of sydnones in chick embryo liver cells. FEBS Letters, 197, 17–20.
  • TEPHLY, T. R., Gums, A. H. and DE MATTEIS, F., 1979, Studies on the mechanism of experimental porphyria produced by 3,5- diethoxycarbonyl-1,4- dihydrocollidine. Role of a porphyrin-like inhibitor of protohaem ferro-lyase. Biochemical Journal, 180, 241–244.
  • WONG, S. G., Kosus, S. M., MCNAMEE, J. P. and MARKS, G. S., 1998, Gender differences in N-alkyl protoporphyrin IX production in rats after the administration of porphyrinogenic xenobiotics. Drug Metabolism and Disposition, 26, 739–744.
  • WONG, S. G., LIN, E. H. and MARKS, G. S., 1999, Cytochrome CYP sources of N-alkylprotoporphyrin IX after administration of porphyrinogenic xenobiotics to rats. Drug Metabolism and Disposition, 27, 960–965.

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