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Biochem Biophys Res Commun. 1998 Nov 9;252(1):51-5.

Tyrosine unphosphorylated platelet SHP-1 is a substrate for calpain.

Author information

1
INSERM U 428, UFR des Sciences Pharmaceutiques et Biologiques, Université René Descartes, Paris Cedex 06, 4 Avenue de l'Observatoire, 75270, France.

Abstract

The platelet phosphotyrosine phosphatase (PTP) SHP-1 is tyrosine phosphorylated during thrombin-induced activation. Stimulation of platelets by the ionophore A23187 in the presence of CaCl2 induced a calpain dependent cleavage of SHP-1. SHP-1 proteolysis was undetectable during thrombin-induced stimulation. When SHP-1 was tyrosine phosphorylated by thrombin, further addition of A23187 failed to induce its cleavage. In the presence of tyrphostin to inhibit thrombin-induced SHP-1 tyrosine phosphorylation, SHP-1 was cleaved. Thus, only the tyrosine unphosphorylated form of SHP-1 was a substrate for calpain. A23187 induced the disappearance of all platelet phosphotyrosine proteins and a two-fold increase in PTP activity, both inhibited by pervanadate, a PTP inhibitor, but unaffected by calpeptin, a calpain inhibitor. The data show that SHP-1 is either tyrosine phosphorylated or cleaved by calpain, and suggest that SHP-1 cleavage does not contribute to A23187-induced PTP activity.

PMID:
9813145
DOI:
10.1006/bbrc.1998.9593
[Indexed for MEDLINE]

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