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The Regulation of Cytochrome P-450 Gene Expression

The Regulation of Cytochrome P-450 Gene Expression Scientific interest in cytochrome P-4S0 has increased dramatically since the unheralded discovery in 1958 of a hepatic microsomal carbon monoxide­ binding pigment with an absorption maximum at 450 nm (I, 2). Omura & Sato subsequently showed that the pigment had the biochemical properties of a cytochrome and designated it "P-450" because of its unusual spectral character­ istics (3-5). We now know that various forms of cytochrome P-450 exist in bacterial, plant, and animal organisms and that these hemoproteins catalyze the monoxygenation of a broad spectrum of lipophilic substrates. Biochemical analyses of cytochrome P-450 have revealed multiple isozymes, which often have broad and overlapping substrate specificities. We do not know how many forms of cytochrome P-4S0 exist; the data suggest that there may be between 30 and 100. In mammalian cells, cytochrome P-4S0-containing enzyme systems metabolize many different endogenous substances (e.g. steroids, fatty acids, prostaglandins), as well as exogenous compounds (e.g. drugs, dyes, pesticides, carcinogens) . The cytochrome P-4S0 apoproteins contain several regions of amino acid sequence homology. Presumably, these represent functionally similar domains among the different isozymes. Sequencing of cytochrome P-4S0 cDNAs andlor genes has revealed additional homology. Based on the degree of their related­ ness in DNA http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Pharmacology and Toxicology Annual Reviews

The Regulation of Cytochrome P-450 Gene Expression

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Publisher
Annual Reviews
Copyright
Copyright 1986 Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
0362-1642
eISSN
1545-4304
DOI
10.1146/annurev.pa.26.040186.002001
pmid
3521459
Publisher site
See Article on Publisher Site

Abstract

Scientific interest in cytochrome P-4S0 has increased dramatically since the unheralded discovery in 1958 of a hepatic microsomal carbon monoxide­ binding pigment with an absorption maximum at 450 nm (I, 2). Omura & Sato subsequently showed that the pigment had the biochemical properties of a cytochrome and designated it "P-450" because of its unusual spectral character­ istics (3-5). We now know that various forms of cytochrome P-450 exist in bacterial, plant, and animal organisms and that these hemoproteins catalyze the monoxygenation of a broad spectrum of lipophilic substrates. Biochemical analyses of cytochrome P-450 have revealed multiple isozymes, which often have broad and overlapping substrate specificities. We do not know how many forms of cytochrome P-4S0 exist; the data suggest that there may be between 30 and 100. In mammalian cells, cytochrome P-4S0-containing enzyme systems metabolize many different endogenous substances (e.g. steroids, fatty acids, prostaglandins), as well as exogenous compounds (e.g. drugs, dyes, pesticides, carcinogens) . The cytochrome P-4S0 apoproteins contain several regions of amino acid sequence homology. Presumably, these represent functionally similar domains among the different isozymes. Sequencing of cytochrome P-4S0 cDNAs andlor genes has revealed additional homology. Based on the degree of their related­ ness in DNA

Journal

Annual Review of Pharmacology and Toxicology – Annual Reviews

Published: Apr 1, 1986

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