Zinc can increase the activity of protein kinase C and contributes to its binding to plasma membranes in T lymphocytes

P. Csermely, M. Szamel, K. Resch, J. Somogyi

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Abstract

In the primary structure of protein kinase C, the presence of a putative metal-binding site has been suggested (Parker, P.J., Coussens, L., Totty, N., Rhee, L., Young, S., Chen, E., Stabel, S., Waterfield, M.D., and Ullrich, A. (1986) Science 233, 853-859). In the present report, we demonstrate that the most abundant intracellular heavy metal, zinc, can increase the activity of cytosolic protein kinase C. Zinc reversibly binds the enzyme to plasma membranes, and it may contrribute to the calcium-induced binding as well. The intracellular heavy metal chelator N,N,N',N'-tetrakis (2-pyridylmethyl) ethylenediamine prevents the phorbol ester- and antigen-induced translocation of protein kinase C. This effect can be totally reversed by the concomitant addition of Zn2+, while Fe2+ and Mn2+ are only partially counteractive. Our results suggest that zinc can activate protein kinase C and contributes to its binding to plasma membranes in T lymphocytes induced by Ca2+, phorbol ester, or antigen.

Original languageEnglish
Pages (from-to)6487-6490
Number of pages4
JournalJournal of Biological Chemistry
Volume263
Issue number14
Publication statusPublished - 1988

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T-cells
Cell membranes
Protein Kinase C
Zinc
Cell Membrane
T-Lymphocytes
Phorbol Esters
Heavy Metals
Antigens
Chelating Agents
Metals
Binding Sites
Calcium
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Zinc can increase the activity of protein kinase C and contributes to its binding to plasma membranes in T lymphocytes. / Csermely, P.; Szamel, M.; Resch, K.; Somogyi, J.

In: Journal of Biological Chemistry, Vol. 263, No. 14, 1988, p. 6487-6490.

Research output: Contribution to journalArticle

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