Leukotriene D4-metabolizing activity of human neutrophils.
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概要
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Leukotriene D<SUB>4</SUB>-metabolizing activity was studied using human neutrophils. Leukotriene D<SUB>4</SUB> was rapidly converted to leukotriene E<SUB>4</SUB> during incubation with intact neutrophils. The subcellular localization of leukotriene D<SUB>4</SUB>-metabolizing enzyme was examined, and leukotriene D<SUB>4</SUB>-metabolizing activity was found to be present in the particulate fraction which consists of cell surface membrane and granules, but not in the nuclear and cytosol fractions. When neutrophils were modified chemically with diazotized sulfanilic acid, a poorly permeant reagent which inactivates cell surface enzymes selectively, the leukotriene D<SUB>4</SUB>-metabolizing activity of intact neutrophils was significantly inhibited. When neutrophils were stimulated with phorbol myristate acetate, a secretagogue, leukotriene D<SUB>4</SUB>-metabolizing activity was found to be released extracellularly. Among enzyme inhibitors examined, o-phenanthroline, a metal chelator strongly inhibited both the leuko-triene D<SUB>4</SUB>-metabolizing activities of intact neutrophils and extracellularly released enzyme. These results would suggest that leukotriene D<SUB>4</SUB>-metabolizing metalloenzymes which convert leukotriene D<SUB>4</SUB> to leukotriene E<SUB>4</SUB>, are located on the cell surface membrane and in the granules of human neutrophils.
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