[Analysis of platelet surface conformation in thrombin-induced aggregation].

S Nomura, H Nagata, M Yanabu, M Suzuki, T Soga, S Ohga, K Kondo, N Sone, C Kitada, H Kitajima
{"title":"[Analysis of platelet surface conformation in thrombin-induced aggregation].","authors":"S Nomura,&nbsp;H Nagata,&nbsp;M Yanabu,&nbsp;M Suzuki,&nbsp;T Soga,&nbsp;S Ohga,&nbsp;K Kondo,&nbsp;N Sone,&nbsp;C Kitada,&nbsp;H Kitajima","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>We used flow cytometry to investigate the change of platelet membrane glycoproteins (GPIb and GP IIb/IIIa) and the distributions of fibrinogen (Fbg), thrombospondin (TSP) and fibronectin (Fn) on the surface of thrombin-stimulated platelets. The binding of a monoclonal antibody directed at the von Willebrand factor binding site on GPIb decreased in thrombin-stimulated platelets. This antibody caused a reactive delay in thrombin-induced aggregation, but had little influence on aggregability. Slight thrombin-induced aggregation was observed even after blocking the binding of Fbg to GP II b/IIIa. The new expression of GP II b/IIIa was detected on the surface of thrombin-stimulated platelets, whereas there was little increase of Fbg dependent on this GP II b/IIIa. An increase of TSP after thrombin stimulation was observed on the surface of platelets of healthy controls and patients with Glanzmann's thrombasthenia (Type I). The level of on platelet surface was slightly increased by thrombin stimulation. The mechanism involved in thrombin-induced aggregation appears to differ from that in ADP-induced aggregation.</p>","PeriodicalId":76233,"journal":{"name":"Nihon Ketsueki Gakkai zasshi : journal of Japan Haematological Society","volume":"52 5","pages":"895-905"},"PeriodicalIF":0.0000,"publicationDate":"1989-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nihon Ketsueki Gakkai zasshi : journal of Japan Haematological Society","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

We used flow cytometry to investigate the change of platelet membrane glycoproteins (GPIb and GP IIb/IIIa) and the distributions of fibrinogen (Fbg), thrombospondin (TSP) and fibronectin (Fn) on the surface of thrombin-stimulated platelets. The binding of a monoclonal antibody directed at the von Willebrand factor binding site on GPIb decreased in thrombin-stimulated platelets. This antibody caused a reactive delay in thrombin-induced aggregation, but had little influence on aggregability. Slight thrombin-induced aggregation was observed even after blocking the binding of Fbg to GP II b/IIIa. The new expression of GP II b/IIIa was detected on the surface of thrombin-stimulated platelets, whereas there was little increase of Fbg dependent on this GP II b/IIIa. An increase of TSP after thrombin stimulation was observed on the surface of platelets of healthy controls and patients with Glanzmann's thrombasthenia (Type I). The level of on platelet surface was slightly increased by thrombin stimulation. The mechanism involved in thrombin-induced aggregation appears to differ from that in ADP-induced aggregation.

[凝血酶诱导聚集的血小板表面构象分析]。
采用流式细胞术观察血小板膜糖蛋白(GPIb和GP IIb/IIIa)的变化以及凝血酶刺激血小板表面纤维蛋白原(Fbg)、血小板反应蛋白(TSP)和纤连蛋白(Fn)的分布。在凝血酶刺激的血小板中,针对血管性血友病因子结合位点的单克隆抗体在GPIb上的结合减少。该抗体在凝血酶诱导的聚集中引起反应性延迟,但对聚集性影响不大。即使阻断Fbg与GP II b/IIIa的结合,也观察到轻微的凝血酶诱导的聚集。在凝血酶刺激的血小板表面检测到GP II b/IIIa的新表达,而依赖于这种GP II b/IIIa的Fbg几乎没有增加。凝血酶刺激后,健康对照和Glanzmann血栓减少症(I型)患者血小板表面TSP水平升高,凝血酶刺激后血小板表面TSP水平略有升高。凝血酶诱导的聚集的机制似乎不同于adp诱导的聚集。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信