Transformation of prostacyclin (PGI2) to a biologically active metabolite: 5(6)-oxido-PGI1 by cytochrome P450-dependent epoxygenase.
The renal epoxygenase has been demonstrated to be an active pathway for the conversion of PGI2 to a new, previously unreported, metabolite. This metabolite was isolated and identified by radiogas-chromatography-mass spectrometry as 5-hydroxy-6-keto PGF1 alpha. Its structure was further confirmed by comparison of the mass-spectra to that of the synthetic standard. The formation of 5-hydroxy-6-keto PGF1 alpha in the kidney suggested epoxidation of prostacyclin via the renal epoxygenase as an alternative pathway of PGI2 metabolism.
Wong
P Y
PY
Department of Physiology and Medicine, New York Medical College, Valhalla 10595.
D015121:6-Ketoprostaglandin F1 alpha / Q000031:analogs & derivatives* / Q000302:isolation & purification / Q000378:metabolism; D000818:Animals; D001711:Biotransformation; D000090762:Cytochrome P-450 CYP2J2; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D011464:Epoprostenol / Q000378:metabolism*; D008401:Gas Chromatography-Mass Spectrometry; D007668:Kidney / Q000201:enzymology*; D008297:Male; D010105:Oxygenases / Q000378:metabolism*; D010477:Perfusion; D011817:Rabbits
D015121:6-Ketoprostaglandin F1 alpha; D003577:Cytochrome P-450 Enzyme System; C070400:5-hydroxy-6-ketoprostaglandin F1 alpha; D011464:Epoprostenol; D010105:Oxygenases; D000090762:Cytochrome P-450 CYP2J2