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

A number of prostaglandins and mono-hyroxylated 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. 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.