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Titolo:
RAFTK/Pyk2 involvement in platelet activation is mediated by phosphoinositide 3-kinase
Autore:
Koziak, K; Kaczmarek, E; Park, SY; Fu, Y; Avraham, S; Avraham, H;
Indirizzi:
Beth Israel Deaconess Med Ctr, Harvard Inst Med, Div Expt Med, Boston, MA 02115 USA Beth Israel Deaconess Med Ctr Boston MA USA 02115 d, Boston, MA 02115 USA Beth Israel Deaconess Med Ctr, Harvard Inst Med, Dept Med, Boston, MA 02115 USA Beth Israel Deaconess Med Ctr Boston MA USA 02115 d, Boston, MA 02115 USA
Titolo Testata:
BRITISH JOURNAL OF HAEMATOLOGY
fascicolo: 1, volume: 114, anno: 2001,
pagine: 134 - 140
SICI:
0007-1048(200107)114:1<134:RIIPAI>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
TYROSINE KINASE RAFTK; THROMBIN RECEPTORS; COLLAGEN; PHOSPHORYLATION;
Keywords:
platelet; PI3K; RAFTK; Pyk2; SHP-2; thrombin receptor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
18
Recensione:
Indirizzi per estratti:
Indirizzo: Avraham, H Beth Israel Deaconess Med Ctr, Harvard Inst Med, Div Expt Med, Boston, MA 02115 USA Beth Israel Deaconess Med Ctr Boston MA USA 02115 MA 02115 USA
Citazione:
K. Koziak et al., "RAFTK/Pyk2 involvement in platelet activation is mediated by phosphoinositide 3-kinase", BR J HAEM, 114(1), 2001, pp. 134-140

Abstract

Platelet activation by different agonists initiates a signalling cascade involving the phosphorylation of several protein kinases, which control key regulatory events. Previously, we demonstrated that the related adhesion focal tyrosine kinase (RAFTK, Pyk2) was involved in an early phase of platelet activation, independent of integrin and glycoprotein IIb-IIIa activation. In this study, we demonstrate that RAFTK is co-immunoprecipitated with phosphoinositide 3-kinase (PI3K) upon platelet activation, and that thrombin, ADP and collagen induced the phosphorylation of both PI3K and RAFTK. A low dose of thrombin (0.015 U/ml) induced RAFTK phosphorylation and platelet aggregation in a PI3K activity-dependent manner, whereas a high dose of thrombin (0.1 U/ml) induced these events in a PI3K activity-independent manner. ADP and collagen also induced RAFTK phosphorylation and platelet aggregation in a PI3K activity-dependent manner, similar to that of the low-dose thrombin. Furthermore, protein tyrosine phosphatase activity was associated with RAFTK in response to platelet activation, and was found to be that of protein tyrosine phosphatase-2 (SHP-2). The association of SHP-2 with RAFTK was PI3K-dependent and was increased upon RAFTK phosphorylation. Taken together, our results strongly suggest that the involvement of RAFTK in platelet activation is mediated via the PI3K pathway.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 17:16:27