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

  title={Tyrosine unphosphorylated platelet SHP-1 is a substrate for calpain.},
  author={Herv{\'e} Falet and Sabine Pain and Francine Rendu},
  journal={Biochemical and biophysical research communications},
  volume={252 1},
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… CONTINUE READING
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