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Titolo:
Platelet glycoprotein V binds to collagen and participates in platelet adhesion and aggregation
Autore:
Moog, S; Mangin, P; Lenain, N; Strassel, C; Ravanat, C; Schuhler, S; Freund, M; Santer, M; Kahn, M; Nieswandt, B; Gachet, C; Cazenave, JP; Lanza, F;
Indirizzi:
Etab Francais Sang Alsace, INSERM U 311, F-67065 Strasbourg, France Etab Francais Sang Alsace Strasbourg France F-67065 5 Strasbourg, France Univ Penn, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104Univ Penn, Philadelphia, PA 19104 USA Univ Witten Herdecke, Klinikum Wuppertal, Wuppertal, Germany Univ Witten Herdecke Wuppertal Germany um Wuppertal, Wuppertal, Germany
Titolo Testata:
BLOOD
fascicolo: 4, volume: 98, anno: 2001,
pagine: 1038 - 1046
SICI:
0006-4971(20010815)98:4<1038:PGVBTC>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-BLOOD PLATELETS; VON-WILLEBRAND-FACTOR; THROMBUS FORMATION; IMMUNOGLOBULIN SUPERFAMILY; MEMBRANE-GLYCOPROTEINS; RECEPTOR INTERACTIONS; VONWILLEBRAND-FACTOR; MICE LACKING; GAMMA-CHAIN; IB-ALPHA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Lanza, F Etab Francais Sang Alsace, INSERM U 311, 10 Rue Spielmann,BP 36, F-67065 Strasbourg, France Etab Francais Sang Alsace 10 Rue Spielmann,BP 36Strasbourg France F-67065
Citazione:
S. Moog et al., "Platelet glycoprotein V binds to collagen and participates in platelet adhesion and aggregation", BLOOD, 98(4), 2001, pp. 1038-1046

Abstract

Glycoprotein V (GPV) is a subunit of the platelet GPlb-V-IX receptor for von Willebrand factor and thrombin. GPV is cleaved from the platelet surfaceduring activation by thrombin, but its role in hemostasis is still unknown. It is reported that GPV knockout mice had a decreased tendency to form arterial occluding thrombi in an intravital thrombosis model and abnormal platelet interaction with the subendothellum. In vitro, GPV-deficient platelets exhibited defective adhesion to a collagen type I-coated surface under flow or static conditions. Aggregation studies demonstrated a decreased response of the GPV-deficient platelets to collagen, reflected by an increased lag phase and reduced amplitude of aggregation. Responses to adenosine diphosphate, arachidonic acid, and the thromboxane analog U46619 were normal butwere enhanced to low thrombin concentrations. The defect of GPV null platelets made them more sensitive to inhibition by the anti-GPVI monoclonal antibody (mAb) JAQ1, and this was also the case in aspirin- or apyrase-treatedplatelets. Moreover, an mAb (V.3) against the extracellular domain of human GPV selectively inhibited collagen-induced aggregation in human or rat platelets. V.3 injected in rats as a bolus decreased the ex vivo collagen aggregation response without affecting the platelet count. Finally, surface plasmon resonance studies demonstrated binding of recombinant soluble GPV on a collagen-coupled matrix. In conclusion, GPV binds to collagen and appearsto be required for normal platelet responses to this agonist. (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 19/01/20 alle ore 00:27:13