Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Fibrinogen binding to the integrin alpha(IIb)beta(3) modulates store-mediated calcium entry in human platelets
Autore:
Rosado, JA; Meijer, EMY; Hamulyak, K; Novakova, I; Heemskerk, JWM; Sage, SO;
Indirizzi:
Univ Cambridge, Dept Physiol, Cambridge CB2 3EG, England Univ Cambridge Cambridge England CB2 3EG iol, Cambridge CB2 3EG, England Univ Maastricht, Dept Biochem, Maastricht, Netherlands Univ Maastricht Maastricht Netherlands Biochem, Maastricht, Netherlands Univ Maastricht, Dept Human Biol, Maastricht, Netherlands Univ MaastrichtMaastricht Netherlands an Biol, Maastricht, Netherlands Acad Hosp Maastricht, Dept Internal Med, Haematol Lab, Haemostasis Lab, Maastricht, Netherlands Acad Hosp Maastricht Maastricht Netherlands ab, Maastricht, Netherlands St Radboud Hosp, Dept Haematol, Nijmegen, Netherlands St Radboud Hosp Nijmegen Netherlands pt Haematol, Nijmegen, Netherlands
Titolo Testata:
BLOOD
fascicolo: 9, volume: 97, anno: 2001,
pagine: 2648 - 2656
SICI:
0006-4971(20010501)97:9<2648:FBTTIA>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE PHOSPHORYLATION; GLYCOPROTEIN IIB/IIIA RECEPTOR; FURA-2-LOADED HUMAN-PLATELETS; IIB-IIIA COMPLEX; CA2+ ENTRY; ACTIN POLYMERIZATION; PLASMA-MEMBRANE; STIMULATED PLATELETS; ACTIVATED PLATELETS; BLOOD-PLATELETS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Sage, SO Univ Cambridge, Dept Physiol, Downing St, Cambridge CB2 3EG, England Univ Cambridge Downing St Cambridge England CB2 3EG 3EG, England
Citazione:
J.A. Rosado et al., "Fibrinogen binding to the integrin alpha(IIb)beta(3) modulates store-mediated calcium entry in human platelets", BLOOD, 97(9), 2001, pp. 2648-2656

Abstract

Effects of the occupation of integrin alpha (IIb)beta (3) by fibrinogen onCa++ signaling in fura-2-loaded human platelets were investigated. Adding fibrinogen to washed platelet suspensions inhibited increases in cytosolic [Ca++] concentrations ([Ca++](i)) evoked by adenosine diphosphate (ADP) andthrombin in a concentration-dependent manner in the presence of external Ca++ but not in the absence of external Ca++ or in the presence of the nonselective cation channel blocker SKF96365, indicating selective inhibition ofCa++ entry. Fibrinogen also inhibited store-mediated Ca++ entry (SMCE) activated after Ca++ store depletion using thapsigargin. The inhibitory effectof fibrinogen was reversed if fibrinogen binding to alpha (IIb)beta (3) was blocked using RDGS or abciximab and was absent in platelets from patientshomozygous for Glanzmann thrombasthenia, Fibrinogen was without effect on SMCE once activated. Activation of SMCE in platelets occurs through conformational coupling between the intracellular stores and the plasma membrane and requires remodeling of the actin cytoskeleton. Fibrinogen inhibited actin polymerization evoked by ADP or thapsigargin in control cells and in cells loaded with the Ca++ chelator dimethyl BAPTA. It also inhibited the translocation of the tyrosine kinase p60(src) to the cytoskeleton. These resultsindicate that the binding of fibrinogen to integrin alpha (IIb)beta (3) inhibits the activation of SMCE in platelets by a mechanism that may involve modulation of the reorganization of the actin cytoskeleton and the cytoskeletal association of p60(src). This action may be important in intrinsic negative feedback to prevent the further activation of platelets subjected to low-level stimuli in vivo. (Blood.2001;97:2648-2656) (C) 2001 by The American Society of Hematology.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 00:51:46