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血小板反应蛋白与血小板糖蛋白GPIa-IIa和GPIIb-IIIa的相互作用。

Interaction of thrombospondin with platelet glycoproteins GPIa-IIa and GPIIb-IIIa.

作者信息

Kowalska M A, Tuszynski G P

机构信息

Department of Medicine, Medical College of Pennsylvania, Philadelphia 19129.

出版信息

Biochem J. 1993 Nov 1;295 ( Pt 3)(Pt 3):725-30. doi: 10.1042/bj2950725.

DOI:10.1042/bj2950725
PMID:8240284
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1134620/
Abstract

The interaction of human thrombospondin (TSP) with GPIa-IIa and GPIIb-IIIa was studied. The binding for both proteins became time-independent after 60 min. A 7-fold excess concentration of unlabelled GPIa-IIa added either initially, or after time-dependent binding, resulted in a 50% inhibition of GPIa-IIa bound to TSP. GPIa-IIa and GPIIb-IIIa specifically bound TSP since: (a) the binding of GPIIb-IIIa to TSP was dependent on the presence of 1 mM MgCl2 and 1 mM CaCl2, whereas binding of GPIa-IIa was ion-independent. (b) The binding was saturable, with dissociation constants of 0.69 +/- 0.17 microM and 3.77 +/- 1.02 microM for GPIa-IIa and GPIIb-IIIa respectively. (c) GPIIb-IIIa and GPIa-IIa did not significantly bind to BSA. (d) GPIIb-IIIa bound fibrinogen ion-specifically, whereas little or no binding of GPIa-IIa was detectable. (e) Both GPIIb-IIIa and GPIa-IIa bound collagen in an ion-independent manner. (f) GPIIb-IIIa did not compete with GPIa-IIa for binding to TSP. (g) Binding of GPIa-IIa to TSP was inhibited with anti-(GPIa-IIa) (6F1), whereas mouse IgG and anti-(GPIIb-IIIa) (AP-2) had no effect. (h) The interaction of GPIa-IIa with TSP is 5.5-fold more favourable than that of GPIIb-IIIa suggesting that GPIa-IIa may be a preferred binding protein for TSP-mediated platelet adhesion.

摘要

研究了人血小板反应蛋白（TSP）与糖蛋白Ia-IIa（GPIa-IIa）和糖蛋白IIb-IIIa（GPIIb-IIIa）的相互作用。60分钟后，两种蛋白质的结合均与时间无关。无论是最初添加，还是在时间依赖性结合后添加7倍过量浓度的未标记GPIa-IIa，均导致与TSP结合的GPIa-IIa被抑制50%。GPIa-IIa和GPIIb-IIIa特异性结合TSP的原因如下：（a）GPIIb-IIIa与TSP的结合依赖于1 mM氯化镁（MgCl2）和1 mM氯化钙（CaCl2）的存在，而GPIa-IIa的结合不依赖离子。（b）结合是可饱和的，GPIa-IIa和GPIIb-IIIa的解离常数分别为0.69±0.17 microM和3.77±1.02 microM。（c）GPIIb-IIIa和GPIa-IIa与牛血清白蛋白（BSA）无明显结合。（d）GPIIb-IIIa特异性结合纤维蛋白原离子，而几乎检测不到GPIa-IIa的结合或未检测到其结合。（e）GPIIb-IIIa和GPIa-IIa均以不依赖离子的方式结合胶原蛋白。（f）GPIIb-IIIa不与GPIa-IIa竞争结合TSP。（g）抗（GPIa-IIa）（6F1）抑制GPIa-IIa与TSP的结合，而小鼠免疫球蛋白（IgG）和抗（GPIIb-IIIa）（AP-2）无作用。（h）GPIa-IIa与TSP的相互作用比GPIIb-IIIa更有利5.5倍，这表明GPIa-IIa可能是TSP介导的血小板黏附的首选结合蛋白。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c454/1134620/398ea3807190/biochemj00100-0107-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c454/1134620/398ea3807190/biochemj00100-0107-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c454/1134620/398ea3807190/biochemj00100-0107-a.jpg

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本文引用的文献

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Identification and characterization of a tumor cell receptor for CSVTCG, a thrombospondin adhesive domain.血小板反应蛋白粘附结构域CSVTCG的肿瘤细胞受体的鉴定与表征
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Interaction of AP-2, a monoclonal antibody specific for the human platelet glycoprotein IIb-IIIa complex, with intact platelets.AP-2（一种针对人血小板糖蛋白IIb-IIIa复合物的单克隆抗体）与完整血小板的相互作用。
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