Recent studies have suggested a possible role for extracellular ATP in neutrophil function. This report provides evidence for the existence of an ecto-protein kinase activity on the surface of human neutrophils capable of phosphorylating intrinsic cell membrane proteins as well as exogenous proteins. Addition of extracellular [γ-32P]ATP to neutrophils resulted in rapid incorporation of 32P into cellular proteins that were sensitive to trypsin. The ability of adherent cells to phosphorylate the exogenous substrate casein, while no protein kinase activity was released into the supernate, provided further evidence for a cell surface associated protein kinase activity.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - May 31 1988|
Bibliographical noteFunding Information:
Ecto-kinase assay. Normal human neutrophils, prepared from heparinized venous blood by dextran sedimentation at 1 x g followed by Ficoll-Hypaque +Supported by NIH grant #CA36248, the Leukemia Task Force, and the Masonic Memorial Hospital Fund Inc.
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