Conference
IMPORTANCE OF LARGE VON WILLEBRAND FACTOR (vWF) MULTIMERS IN vWF INTERACTION WITH PLATELET GLYCOPROTEIN IIb/IIIa
| العنوان: | IMPORTANCE OF LARGE VON WILLEBRAND FACTOR (vWF) MULTIMERS IN vWF INTERACTION WITH PLATELET GLYCOPROTEIN IIb/IIIa |
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| المؤلفون: | Yamamoto, M, Ando, Y, Watanabe, K, Iri, H, Araki, Y, Murata, M, Murakami, H, Satoh, K, Ikeda, Y |
| المصدر: | XIth International Congress on Thrombosis and Haemostasis ; Thrombosis and Haemostasis ; ISSN 2567-689X |
| بيانات النشر: | Schattauer GmbH |
| سنة النشر: | 1987 |
| الوصف: | Recently it has been reported that, in addition to binding to glycoprotein (GP) lb, vWF also interacts with GPIIb/IIIa, although the physiological relevance of this interaction is not completeley clear. In this paper, we have investigated the role of different size of vWF multimers in vWF-mediated platelet aggregation. Different size of vWF multimers were purified from human plasma through Sephacryl S-1000 column according to the method of Fowler et al. Fractions were analysed by SDS-agarose gel electrophoresis by the method of Ruggeri et al. When each fraction was examined for ristocetin cofactor activity (RCo), only larger multimers exhibited significant RCo. The maximum extent of ristocetin-induced platelet agglutination by larger multimers (10 μg/ml) was 80%, while that of intermediate and lower multimers at the same concentration was 20% and 0%, respectively. Each fraction was then added to washed platelet suspensions in the presence of 10 μM ADP and 0.3 mM CaCl2. Only larger multimers induced platelet aggregation, while intermediate and lower multimers failed to induce platelet aggregation. The maximum extent of aggregation in the presence of larger multimers (10 μg/ml) was 70% of that in the presence of fibrinogen instead. Similar experiments were peformed using platelet-rich plasma from a patient with afibrinogenemia in stead of washed normal platelets. ADP caused significant aggregation only when purified vWF larger multimers or fibrinogen was added. This vWF-mediated aggregation was completely inhibited by monoclonal antibody to GPIIb/IIIa (1 μg/ml) and synthetic peptide, Arg-Gly-Asp-Ser, (1 mM). Our results indicate that larger multimers of vWF play major roles in vWF interaction with GPIIb/IIIa. |
| نوع الوثيقة: | conference object |
| اللغة: | unknown |
| DOI: | 10.1055/s-0038-1644096 |
| DOI: | 10.1055/s-0038-1644096.pdf |
| الاتاحة: | http://dx.doi.org/10.1055/s-0038-1644096 http://www.thieme-connect.de/products/ejournals/pdf/10.1055/s-0038-1644096.pdf |
| رقم الانضمام: | edsbas.ED461BBC |
| قاعدة البيانات: | BASE |
| DOI: | 10.1055/s-0038-1644096 |
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