Abstract
The present report describes the presence of an arachidonic-acid-selective, dithiothreitol-insensitive phospholipase A 2 enzyme activity in human neutrophil cytosol. The enzyme activity is eluted from Mono Q FPLC column between 350 to 450 mM salt and translocates from cytosol to membrane in a calcium dependent fashion. Furthermore, the PLA 2 activity in the cytosol is quantitatively precipitated by the antibodies against U937 cPLA 2. The neutrophil enzyme also migrates as ≈110 kDa protein on SDS polyacrylamide gels. These studies indicate that the PLA 2 enzyme present in human neutrophil cytosol is identical to the previously reported U937 cPLA 2 (Clark et al. (1990) Proc. Natl. Acad. Sci. USA 87, 7708 and Clark et al. (1991) Cell 65, 1043).
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