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Human cytochrome P450 family 4 enzymes: function, genetic variation and regulation

Academic Article
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Overview

authors

  • Hsu, M. H.
  • Savas, U.
  • Griffin, K. J.
  • Johnson, Eric

publication date

  • 2007

journal

  • Drug Metabolism Reviews  Journal

abstract

  • The microsomal cytochrome P450 (CYP) family 4 monooxygenases are the major fatty acid omega-hydroxylases. These enzymes remove excess free fatty acids to prevent lipotoxicity, catabolize leukotrienes and prostanoids, and also produce bioactive metabolites from arachidonic acid omega-hydroxylation. In addition to endogenous substrates, recent evidence indicates that CYP4 monooxygenases can also metabolize xenobiotics, including therapeutic drugs. This review focuses on human CYP4 enzymes and updates current knowledge concerning catalytic activity profiles, genetic variation and regulation of expression. Comparative differences between the human and rodent CYP4 enzymes regarding catalytic function and conditional expression are also discussed.

subject areas

  • Animals
  • Cytochrome P-450 Enzyme System
  • Gene Expression Regulation, Enzymologic
  • Genetic Variation
  • Humans
  • Isoenzymes
  • Rodentia
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Research

keywords

  • 4A22
  • P450
  • P450 4A11
  • P4504F2
  • P4504F3B
  • cytochrome P450 4
  • fatty acid omega-hydroxylation
  • gene regulation
  • species differences
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Identity

International Standard Serial Number (ISSN)

  • 0360-2532

Digital Object Identifier (DOI)

  • 10.1080/03602530701468573

PubMed ID

  • 17786636
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Additional Document Info

start page

  • 515

end page

  • 538

volume

  • 39

issue

  • 2-3

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