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Platelet membrane glycoproteins IIb and IIIa are substrates of purified pp60 c‐src protein tyrosine kinase
Author(s) -
Findik Duygu,
Reuter Christoph,
Presek Peter
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80138-9
Subject(s) - glycoprotein , platelet membrane glycoprotein , glycoprotein ib , phosphorylation , tyrosine , microbiology and biotechnology , tyrosine phosphorylation , proto oncogene tyrosine protein kinase src , platelet , membrane glycoproteins , biochemistry , chemistry , tyrosine kinase , receptor tyrosine kinase , immunoprecipitation , receptor , biology , gene , immunology
Human platelet glycoproteins IIb and IIIa form the receptor for fibrinogen, von Willebrand factor and fibronectin. Isolated human glycoproteins IIb‐IIIa are phosphorylated by purified pp60 c‐src protein tyrosine kinase. Analysis of the phosphorylated proteins on SDS‐PAGE showed that under reducing conditions both phosphoproteins change their relative molecular masses from 135 to 120 kDa and from 97 to 105 kDa, which are characteristic properties of glycoproteins IIb‐IIIa. Phosphorylated proteins could be immunoprecipitated with an antiserum against glycoproteins IIb‐IIIa but not by control serum. Some kinetic properties of the glycoprotein phosphorylations are also investigated. How the glycoprotein IIb‐IIIa complex acquires its receptor activity in stimulated platelets is unknown; however, phosphorylation could be an important mechanism.