Zinc increases the affinity of phorbol ester receptor in T lymphocytes

Péter Csermely, Márta Szamel, Klaus Resch, János Somogyi

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

In the primary structure of the major phorbol ester receptor, protein kinase C the presence of putative metal (zinc) binding sites has been suggested. We have demonstrated earlier that zinc activates protein kinase C and contributes to its binding to plasma membranes in T lymphocytes. Here we report that zinc increases the phorbol ester binding affinity of cytosolic protein kinase C. The effect of zinc on the membrane-bound enzyme is much less pronounced. Our results raise the possibility that cytosolic protein kinase C is a mixture of isoenzymes with different sensitivity towards zinc ions.

Original languageEnglish
Pages (from-to)578-583
Number of pages6
JournalBiochemical and biophysical research communications
Volume154
Issue number2
DOIs
Publication statusPublished - Jul 29 1988

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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