Abstract:
:In thrombin-stimulated platelets alpha IIb beta 3 integrin engagement triggers both phosphatidylinositol 3',4'-bisphosphate synthesis and calpain activation. We checked the possible involvement of calpains in phosphatidylinositol 3-kinase signalling pathway using a cell permeant specific inhibitor of calpains, calpeptin. In conditions where thrombin-induced platelet aggregation and secretion were not impaired, we found a dose-dependent inhibition of phosphatidylinositol 3,4-bisphosphate synthesis by calpeptin from 50 micrograms/ml. Moreover, pretreatment of platelets by both calpeptin and the peptide RGDS, an inhibitor of fibrinogen binding to activated alpha IIb beta 3 integrin, did not induce additive effects on phosphatidylinositol 3,4-bisphosphate inhibition. Finally, the p85 regulatory subunit of phosphatidylinositol 3-kinase was still translocated to the cytoskeleton in calpeptin-treated platelets. These data indicate that calpains are involved in the regulation of alpha IIb beta 3 integrin-dependent phosphatidylinositol 3-kinase signalling pathway.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Montsarrat N,Racaud-Sultan C,Mauco G,Plantavid M,Payrastre B,Breton-Douillon M,Chap Hdoi
10.1016/s0014-5793(97)00079-3subject
Has Abstractpub_date
1997-03-03 00:00:00pages
23-6issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00079-3journal_volume
404pub_type
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