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Tyrosine phosphorylation and subcellular redistribution of p125 ras guanosine triphosphatase-activating protein in human neutrophils stimulated with FMLP.

作者信息

Dusi S, Donini M, Wientjes F, Rossi F

机构信息

Institute of General Pathology, University of Verona, Italy.

出版信息

FEBS Lett. 1996 Apr 1;383(3):181-4. doi: 10.1016/0014-5793(96)00248-7.

DOI:10.1016/0014-5793(96)00248-7
PMID:8925892
Abstract

In this paper, we show that the p125 ras guanosine triphosphatase-activating protein (p125 GAP) is present in the cytosol of human neutrophils and is transiently tyrosine phosphorylated and translocated to the membranes upon cell activation with formyl-methionyl-leucyl-phenylalanine (FMLP). When concanavalin A (ConA) or phorbol 12-myristate 13-acetate (PMA), which both induced a long-lasting respiratory burst, were used as stimuli, tyrosine phosphorylation and translocation of p125 GAP did not occur.

摘要

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Tyrosine phosphorylation and subcellular redistribution of p125 ras guanosine triphosphatase-activating protein in human neutrophils stimulated with FMLP.
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