Cytochrome P450 dependent metabolism of arachidonic acid in bovine corneal epithelium.

Microsomes prepared from bovine corneal epithelium metabolized 14C-arachidonic acid into two unidentified products, separated by thin-layer chromatography and called Peaks I and II. Each peak was further separated by high performance liquid chromatography into two metabolites. The formation of these metabolites was dependent on the addition of NADPH and inhibited by carbon monoxide and SKF-525A, suggesting a cytochrome P450-dependent mechanism. The presence of cytochrome P450 in the corneal epithelium was assessed directly by measurement of the carbon monoxide reduced spectrum and indirectly by measuring aryl hydrocarbon hydroxylase activity. The activity of aryl hydrocarbon hydroxylase was protein- and NADPH-dependent and was inhibited by SKF-525A.