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) |
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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