Zinc increases the affinity of phorbol ester receptor in T lymphocytes.
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.
Csermely
P
P
Inst. Biochem. I., Semmelweis Univ. Sch. Med., Budapest, Hungary.
Szamel
M
M
Resch
K
K
Somogyi
J
J
D000818:Animals; D001665:Binding Sites; D029742:Caenorhabditis elegans Proteins; D002352:Carrier Proteins; D005029:Ethylenediamines / Q000494:pharmacology; D008297:Male; D015240:Phorbol 12,13-Dibutyrate; D010703:Phorbol Esters / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism; D011817:Rabbits; D011955:Receptors, Drug / Q000378:metabolism*; D013601:T-Lymphocytes / Q000187:drug effects / Q000378:metabolism*; D015032:Zinc / Q000494:pharmacology*
D029742:Caenorhabditis elegans Proteins; D002352:Carrier Proteins; D005029:Ethylenediamines; D010703:Phorbol Esters; D011955:Receptors, Drug; C083141:phorbol ester binding protein; C027776:phorbol ester receptor; D015240:Phorbol 12,13-Dibutyrate; D011493:Protein Kinase C; D015032:Zinc; C044387:N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine