| Autor: |
Bushfield M; Department of Pharmacology, University of Glasgow, Scotland., Hopple SL, Gibson IF, Murdoch FA, MacIntyre DE |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 1987 Oct 05; Vol. 222 (2), pp. 299-304. |
| DOI: |
10.1016/0014-5793(87)80390-3 |
| Abstrakt: |
Treatment of intact human platelets with the tumour-promoting phorbol ester, phorbol 12-myristate 13-acetate (PMA), specifically inhibited PGD2-induced cyclic AMP formation without affecting the regulation of cyclic AMP metabolism by PGI2, PGE1, 6-keto-PGE1, 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 A2 or ADP); (iii) mimicked by 1,2-dioctanoylglycerol (DiC8) but not by 4 alpha-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 PGD2 without compromising the effects of exogenous stimulants of adenylate cyclase (PGI2, 6-keto-PGE1, adenosine). |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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