Calcium-dependent oxidation of 5,8,11-icosatrienoic acid by the cyclooxygenase enzyme system

W. J. Elliott, A. R. Morrison, H. Sprecher, P. Needleman

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Abstract

Mead (5,8,11-icosatrienoic) acid was found to be metabolized by the cyclooxygenase enzyme system of ram seminal vesicle microsomes in a calcium-dependent manner. Although the enzyme converted Mead acid to products more slowly and less completely than the isomeric 8,11,14-icosatrienoic acid, both oxidations were inhibitable by indomethacin. Experiments using purified cyclooxygenase confirmed the participation of this enzyme system in the calcium-dependent oxidation. The products of the oxidation were separated by high performance liquid chromatography and analyzed by ultraviolet and gas chromatography-mass spectrometry. The spectra obtained were consistent with the products having the structures 13-hydroxy-5,8,11-icosatrienoate (the major product), 11-hydroxy-5,8,12-icosatrienoate, 9-hydroxy-5,7,11-icosatrienoate, and two isomeric 8,11-dihydroxy-5,9,12-icosatrienoates. No prostaglandin-like, cyclized products could be identified. This report is only the second to illustrate a calcium-dependent oxidation of a poly-unsaturated fatty acid by a cyclooxygenase enzyme system and further extends the metabolic potential of Mead acid.

Original languageEnglish
Pages (from-to)6719-6724
Number of pages6
JournalJournal of Biological Chemistry
Volume261
Issue number15
StatePublished - 1986

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