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Calcium‐binding myeloid protein (P8,14) is phosphorylated in fMet‐Leu‐Phe‐stimulated neutrophils

In this report, we show that the pl4 subunit of calcium‐binding myeloid protein complex (p8,14) is phosphorylated in human neutrophils stimulated with either fMet‐Leu‐Phe, phorbol myristate acetate, or a calcium ionophore. Trifluoperazine, a calmodulin antagonist, caused hyperphosphorylation of pi 4 in intact resting neutrophils. Freincubation of resting cells with 10‐20 nM calyculin A, a potent protein phosphatase inhibitor, also caused enhanced labeling of pi 4, which was further progressively increased on stimulation with fMLP. Thus, the phosphorylation level of pi 4 in resting as well as in stimulated neutrophils appears to be controlled by an active protein phosphatase. The phosphorylation of pi 4 by a chemoattractant and by a phorbol ester is a novel finding supporting the current belief that p8,14 myeloid protein may play an important role in the metabolism of myeloid cells.