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. 1987 Aug;21(3-4):397-9.
doi: 10.1007/BF01966527.

Metabolism of cyclooxygenase and lipoxygenase products by 15-prostaglandin dehydrogenase from human HL-60 leukemia cells

A P Agins  1 , R E Zipkin, I M Taffer
Affiliations

Metabolism of cyclooxygenase and lipoxygenase products by 15-prostaglandin dehydrogenase from human HL-60 leukemia cells

A P Agins et al. Agents Actions. 1987 Aug.

Abstract

A number of prostaglandins and mono-hydroxylated fatty acids were investigated as substrates for NAD-dependent 15-prostaglandin dehydrogenase (15-PGDH) obtained from human HL-60 cells. Lipoxygenase and cyclooxygenase-derived substrates possessing an w-6 hydroxyl moiety (15-HETE, 13-HODD and HHT) were metabolized to corresponding keto derivatives at a rate comparable to that for prostaglandins E2 and F2 alpha. 12-HETE was a poor substrate and 5-HETE was not metabolized. The w-6 hydroxy fatty acids inhibited the metabolism of PGE2 and therefore they may play a role in modulating bioactive prostaglandin levels.

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