Functional aspects of eicosanoid hydroxylation by lung and kidney cytochromes P450. Expression of cDNAs in mammalian cells and E. coli

B. S.S. Masters, J. E. Clark, L. J. Roman, M. Nishimoto, T. J. McCabe, P. R. Ortiz De Montellano, Charles Plopper, D. Gebremedhin, Y. H. Ma, D. R. Harder, R. J. Roman

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

A gene subfamily of cytochromes P450 with catalytic activity toward various eicosanoid substrates has been studied with a variety of techniques in this laboratory, including purification and characterization, localization at the tissue and subcellular levels, physiological function, and cloning and expression in prokaryotic and eukaryotic systems. This paper reports experiments directed toward determining the function of the cytochrome P4504A metabolite, 20-hydroxyarachidonic acid (20-hydroxyeicosatetraenoic acid; 20-HETE), in cellular ion flux, immunohistochemical localization in lung, the effects of a mechanism-based inhibitor, 12-hydroxy-16-heptadecynoic acid (12-HHDYA) on PGE1 ω-hydroxylation, and the structure-function determinants which govern the activities of the enzymes encoded by this gene subfamily.

Original languageEnglish (US)
Pages (from-to)353-360
Number of pages8
JournalJournal of Lipid Mediators
Volume6
Issue number1-3
StatePublished - Dec 1 1992
Externally publishedYes

Keywords

  • ω-hydroxylation
  • 20-hydroxyarachidonate
  • chimeric constructs
  • COS-1 cell expression
  • CYP4A gene subfamily
  • cytochromes P4504A
  • E. coli-expressed P4504A4
  • eicosanoids
  • immunohistochemical localization
  • mechanism-based inhibition
  • patch-clamp study

ASJC Scopus subject areas

  • Immunology
  • Pharmacology

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