PMID: 2108026Mar 10, 1990Paper

Platelet protein phosphorylation and protein kinase C activation by phorbol esters with different biological activity and a novel synergistic response with Ca2+ ionophore

European Journal of Biochemistry
S F BrooksA Aitken

Abstract

Phorbol esters with different biological activities have been tested for their ability to induce the phosphorylation of human platelet proteins. We have shown that only the potent platelet aggregatory phorbol esters were able to stimulate the phosphorylation of proteins of 76, 68, 47, 30 and 20 kDa in intact platelets. The ability of these esters to stimulate phosphorylation of the 47-kDa protein ('p47') correlated with their ability to cause platelet aggregation. When a non-platelet aggregatory deoxyphorbol (12-deoxyphorbol 13-phenylacetate 20-acetate) was combined with a subthreshold dose of the Ca2+ ionophore, A23187, a large increase in phosphorylation of p47 and a fourfold decrease in Ka was observed. This was in contrast to a barely detectable stimulation of phosphorylation at micromolar levels of this phorbol ester in the absence of the ionophore. This synergism was not evident for the potent platelet aggregatory derivatives. The Ka for DOPPA with a mixture of total platelet protein kinase C was 530 nM in the absence of calcium decreasing to 120 nM in the presence of calcium. In the presence of calcium, 12-deoxyphorbol 13-phenylacetate 20-acetate was shown to stimulate preferentially one of the isoforms of protein kinase C.

References

Jun 28, 1985·Biochemical and Biophysical Research Communications·A J Sytkowski, D M Wojchowski
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Citations

Apr 1, 1991·Journal of Ethnopharmacology·F J Evans
Dec 1, 1996·Alcoholism, Clinical and Experimental Research·R A DeitrichK Gill
Sep 8, 2011·International Ophthalmology Clinics·Rajesh C RaoJoan W Miller

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