Evidence for ecto-protein kinase activity on the surface of human neutrophils

Kathryn E. Dusenbery; John R. Mendiola; Keith M. Skubitz

doi:10.1016/S0006-291X(88)81182-3

Evidence for ecto-protein kinase activity on the surface of human neutrophils

Kathryn E. Dusenbery, John R. Mendiola, Keith M. Skubitz

Research output: Contribution to journal › Article › peer-review

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Abstract

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)
Pages (from-to)	7-13
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	153
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(88)81182-3
State	Published - May 31 1988

Bibliographical note

Funding 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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title = "Evidence for ecto-protein kinase activity on the surface of human neutrophils",

abstract = "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.",

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note = "Funding 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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AU - Dusenbery, Kathryn E.

AU - Mendiola, John R.

AU - Skubitz, Keith M.

N1 - Funding 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.

PY - 1988/5/31

Y1 - 1988/5/31

N2 - 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.

AB - 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.

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Evidence for ecto-protein kinase activity on the surface of human neutrophils

Abstract

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