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Effects of protein kinase C activation on human platelet cyclic AMP metabolism
Author(s) -
Bushfield Mark,
Hopple Sara L.,
Gibson Iain F.,
Murdoch Fiona A.,
MacIntyre D.Euan
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80390-3
Subject(s) - adenylate kinase , cyclase , protein kinase c , protein kinase a , adenosine , staurosporine , chemistry , phorbol , endogeny , biochemistry , endocrinology , signal transduction , medicine , enzyme , biology
Treatment of intact human platelets with the tumour‐promoting phorbol ester, phorbol 12‐myristate 13‐acetate (PMA), specifically inhibited PGD 2 ‐induced cyclic AMP formation without affecting the regulation of cyclic AMP metabolism by PGI 2 , PGE 1 , 6‐keto‐PGE 1 , adenosine or adrenaline. This action of PMA was: (i) concentration‐dependent; (ii) not mediated by evoked formation or release of endogenous regulators of adenylate cyclase activity (thromboxane A 2 or ADP); (iii) mimicked by 1,2‐dioctanoylglycerol (DiC 8 ) but not by 4α‐phorbol 12,13‐didecanoate (which does not activate protein kinase C); (iv) attenuated by Staurosporine. These results indicate that activation of protein kinase C in platelets may provide a regulatory mechanism to abrogate the effects of the endogenous adenylate cyclase stimulant PGD 2 without compromising the effects of exogenous stimulants of adenylate cyclase (PGI 2 , 6‐keto‐PGE 1 , adenosine).