Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
INVOLVEMENT OF PROTEIN-TYROSINE KINASE P72(SYK) IN COLLAGEN-INDUCED SIGNAL-TRANSDUCTION IN PLATELETS
Autore:
FUJII C; YANAGI S; SADA K; NAGAI K; TANIGUCHI T; YAMAMURA H;
Indirizzi:
FUKUI MED SCH,DEPT BIOCHEM MATSUOKA FUKUI 91011 JAPAN FUKUI MED SCH,DEPT BIOCHEM MATSUOKA FUKUI 91011 JAPAN FUKUI MED SCH,DEPT OPHTHALMOL MATSUOKA FUKUI JAPAN KOBE UNIV,BIOSIGNAL RES CTR KOBE 657 JAPAN
Titolo Testata:
European journal of biochemistry
fascicolo: 1, volume: 226, anno: 1994,
pagine: 243 - 248
SICI:
0014-2956(1994)226:1<243:IOPKPI>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
WHEAT-GERM-AGGLUTININ; CELL-ANTIGEN RECEPTOR; ACTIVATION; PHOSPHORYLATION; THROMBIN; KINASE-P72(SYK); CONCANAVALIN; ASSOCIATION; MECHANISMS; BLOOD;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
27
Recensione:
Indirizzi per estratti:
Citazione:
C. Fujii et al., "INVOLVEMENT OF PROTEIN-TYROSINE KINASE P72(SYK) IN COLLAGEN-INDUCED SIGNAL-TRANSDUCTION IN PLATELETS", European journal of biochemistry, 226(1), 1994, pp. 243-248

Abstract

Previous studies have demonstrated that activation of platelets by collagen results in a dramatic increase in tyrosine phosphorylation of several cellular proteins, including pp125(FAK), through the interaction of collagen with integrin alpha(2) beta(1) (GP Ia-IIa). In this study, we report that p72(syk) is a potential candidate for the protein-tyrosine phosphorylation event following collagen stimulation in porcineplatelets. Washed platelets were stimulated with collagen and the activation of p72(syk) was assessed in an immunoprecipitation kinase assay. The activity of p72(syk) increased within 1 min, reached a maximum at 5 min after stimulation by collagen, and the phosphorylation at tyrosine residues of p72(syk) in platelets also occurred in the same timecourse as the activation of p72(syk). Prior treatment of platelets with cytochalasin D to inhibit actin polymerization, or with aspirin andapyrase to inhibit the secondary reaction, or EGTA and the acetoxymethyl ester of -bis-(o-aminophenoxy)-ethane-N,N,N',N'-tetraacetic acid to chelate both extracellular and intracellular Ca2+, did not affect the activation of p72(syk) induced by collagen. Furthermore, herbimycin A, a potent protein tyrosine-kinase inhibitor, was capable of reducingcollagen-evoked p72(syk) activation, Ca2+ mobilization and platelet aggregation. These results suggest that upon stimulation by collagen p72(syk) is physically activated by a process that is independent of theeffects of Ca2+, ADP, and actin polymerization, and may participate in the regulation of Ca2+ mobilization mediated by collagen in platelets.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 17:29:09