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Dominant Role of the Protein-Tyrosine Phosphatase CD148 in Regulating Platelet Activation Relative to Protein-Tyrosine Phosphatase-1B
Author(s) -
Jun Mori,
Yingjie Wang,
Stuart Ellison,
Silke Heising,
Benjamin G. Neel,
Michel L. Tremblay,
Steve P. Watson,
Yotis A. Senis
Publication year - 2012
Publication title -
arteriosclerosis thrombosis and vascular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.007
H-Index - 270
eISSN - 1524-4636
pISSN - 1079-5642
DOI - 10.1161/atvbaha.112.300447
Subject(s) - protein tyrosine phosphatase , proto oncogene tyrosine protein kinase src , platelet activation , tyrosine phosphorylation , phosphorylation , platelet , tyrosine , chemistry , kinase , tyrosine kinase , phosphatase , microbiology and biotechnology , glycoprotein , receptor tyrosine kinase , biology , biochemistry , receptor , immunology
The receptor-like protein-tyrosine phosphatase (PTP) CD148 and the nontransmembrane PTP1-B have been shown to be net positive regulators of Src family kinases in platelets. In the present study, we compared the relative contributions of these PTPs in platelet activation by the major glycoprotein, glycoprotein VI, α(IIb)β(3), and C-type lectin-like receptor 2 (CLEC-2).

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