Premium
Zn 2+ enhances protein tyrosine kinase activity of human platelet membranes
Author(s) -
Findik Duygu,
Presek Peter
Publication year - 1988
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(88)81232-8
Subject(s) - platelet , membrane , chemistry , tyrosine , tyrosine kinase , biochemistry , microbiology and biotechnology , biophysics , medicine , biology , signal transduction
In human platelet membranes enhanced tyrosine phosphorylation of certain proteins was observed when Zn 2+ instead of Mg 2+ or Mn 2+ was used as a divalent cation for the kinase reaction. An enhanced level of phosphate incorporation into tyrosine residues occurred into a 68 kDa polypeptide besides the 45 kDa and 105 kDa proteins. Preincubation of platelet membranes with TBR‐IgG showed a concentration‐dependent inhibition of the phosphorylation of the 45, 68 and 105 kDa proteins. Moreover, pp60 c‐src , representing the major protein tyrosine kinase activity in platelets, was found to be stimulated by Zn 2+ . The data, thus, support the assumption that pp60 c‐src kinase is responsible for Zn 2+ stimulated tyrosine phosphorylation.