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. 1984 Jul 15;221(2):477-82.
doi: 10.1042/bj2210477.

The Ca2+-activated polyphosphoinositide phosphodiesterase of human and rabbit neutrophil membranes

S Cockcroft, J M Baldwin, D Allan

The Ca2+-activated polyphosphoinositide phosphodiesterase of human and rabbit neutrophil membranes

S Cockcroft et al. Biochem J. .

Abstract

Addition of Ca2+ to a plasma-membrane fraction derived from human or rabbit neutrophils led to the specific breakdown of polyphosphoinositides. The degradation products were identified as diacylglycerol and inositol bis- and tris-phosphate, thus demonstrating the presence of a Ca2+-activated phospholipase C. The newly generated diacylglycerol resembled the polyphosphoinositides in its fatty acid composition, and in the presence of MgATP2- it was converted into phosphatidate. These results therefore demonstrate the presence in neutrophil plasma membranes not only of polyphosphoinositide phosphodiesterase but also of diacylglycerol kinase.

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