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

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 journal › Article › peer-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 language	English (US)
Pages (from-to)	353-360
Number of pages	8
Journal	Journal of Lipid Mediators
Volume	6
Issue number	1-3
State	Published - Dec 1 1992
Externally published	Yes

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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Functional aspects of eicosanoid hydroxylation by lung and kidney cytochromes P450. Expression of cDNAs in mammalian cells and E. coli. / Masters, B. S.S.; Clark, J. E.; Roman, L. J.; Nishimoto, M.; McCabe, T. J.; Ortiz De Montellano, P. R.; Plopper, Charles; Gebremedhin, D.; Ma, Y. H.; Harder, D. R.; Roman, R. J.

In: Journal of Lipid Mediators, Vol. 6, No. 1-3, 01.12.1992, p. 353-360.

Research output: Contribution to journal › Article › peer-review

Masters, B. S.S. ; Clark, J. E. ; Roman, L. J. ; Nishimoto, M. ; McCabe, T. J. ; Ortiz De Montellano, P. R. ; Plopper, Charles ; Gebremedhin, D. ; Ma, Y. H. ; Harder, D. R. ; Roman, R. J. / Functional aspects of eicosanoid hydroxylation by lung and kidney cytochromes P450. Expression of cDNAs in mammalian cells and E. coli. In: Journal of Lipid Mediators. 1992 ; Vol. 6, No. 1-3. pp. 353-360.

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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.",

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