Leukotriene B4 (LTB4) ω-hydroxylase activity in human neutrophil microsomes was significantly inhibited by antisera against three rabbit ω-hydroxylase P-450s, lung prostaglandin ω-hydroxylase (P-450p-2), small intestine prostaglandin A ω-hydroxylase (P-450ia), and kidney fatty acid ω-hydroxylase (P-450kd). In contrast, the activity is not affected by antibodies raised against the phenobarbital-inducible forms of P-450s from both rabbits and rats. These findings suggest that the LTB4 ω-hydroxylase (P-450LTBω) is structurally related to a group of rabbit ω-hydroxylase P-450s. The antiserum raised against P-450p-2 also inhibited the NADPH-dependent oxidation of 20-hydroxy LTB4 to 20-oxo LTB4 and 20-carboxy LTB4 by the microsomes, supporting that P-450LTBω is able to catalyze the subsequent oxidation of 20-hydroxy LTB4 as well as the ω-hydroxylation of LTB4.
|Number of pages||7|
|Publication status||Published - 1990|
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