Zn2+ enhances protein tyrosine kinase activity of human platelet membranes

Duygu Findik, Peter Presek

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

In human platelet membranes enhanced tyrosine phosphorylation of certain proteins was observed when Zn2+ instead of Mg2+ or Mn2+ 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, pp60c-src, representing the major protein tyrosine kinase activity in platelets, was found to be stimulated by Zn2+. The data, thus, support the assumption that pp60c-src kinase is responsible for Zn2+ stimulated tyrosine phosphorylation.

Original languageEnglish (US)
Pages (from-to)51-56
Number of pages6
JournalFEBS Letters
Volume235
Issue number1-2
DOIs
Publication statusPublished - Aug 1 1988

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Keywords

  • (Human platelet membrane)
  • Phosphoprotein pp60
  • Phosphotyrosyl-protein phosphatase
  • Protein tyrosine kinase
  • Zn

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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