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

Pub. Date : 1998 Nov 9

PMID : 9813145






7 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Tyrosine unphosphorylated platelet SHP-1 is a substrate for calpain. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
2 The platelet phosphotyrosine phosphatase (PTP) SHP-1 is tyrosine phosphorylated during thrombin-induced activation. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
3 When SHP-1 was tyrosine phosphorylated by thrombin, further addition of A23187 failed to induce its cleavage. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
4 In the presence of tyrphostin to inhibit thrombin-induced SHP-1 tyrosine phosphorylation, SHP-1 was cleaved. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
5 In the presence of tyrphostin to inhibit thrombin-induced SHP-1 tyrosine phosphorylation, SHP-1 was cleaved. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
6 Thus, only the tyrosine unphosphorylated form of SHP-1 was a substrate for calpain. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
7 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. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens