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糖蛋白Ic-IIa作为人血小板上一种不依赖激活的纤连蛋白受体发挥作用。

Glycoprotein Ic-IIa functions as an activation-independent fibronectin receptor on human platelets.

作者信息

Piotrowicz R S, Orchekowski R P, Nugent D J, Yamada K Y, Kunicki T J

机构信息

Blood Center of Southeastern Wisconsin, Milwaukee 53233.

出版信息

J Cell Biol. 1988 Apr;106(4):1359-64. doi: 10.1083/jcb.106.4.1359.

DOI:10.1083/jcb.106.4.1359
PMID:2966181
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2115005/
Abstract

Soluble fibronectin binds specifically to glycoprotein (GP) IIb-IIIa on thrombin-activated platelets, and this binding is not observed with platelets of patients with Glanzmann's thrombasthenia (GT) which lack GPIIb-IIIa. Here we report that GT platelets retain the ability to interact with fibronectin-coated surfaces. Adhesion to fibronectin does not require platelet activation and is inhibited by soluble fibronectin, antibodies specific for fibronectin, peptides containing the sequence Arg-Gly-Asp and polyclonal antibodies specific for band 3 of the chicken embryo fibroblast fibronectin receptor (anti-band 3). Using anti-band 3, we have purified a second fibronectin receptor from human platelets, a heterodimer composed of glycoproteins previously designated GPIc and GPIIa. The GPIc-IIa complex is found on both GT and normal platelets and appears to be identical to the GP138 kD-GP160 kD complex recently immunopurified by Giancotti et al. (1986. Exp. Cell Res. 163:47-62) and by Sonnenberg et al. (1987. J. Biol. Chem. 268:10376-10383). In this report, we provide the first evidence that GPIc-IIa actually mediates adhesion of platelets to fibronectin-coated surfaces. GPIc-IIa thus represents a second functional fibronectin receptor, distinct from GPIIb-IIIa, that is largely responsible for the adhesion of nonactivated platelets to fibronectin-coated surfaces.

摘要

可溶性纤维连接蛋白特异性结合凝血酶激活血小板上的糖蛋白(GP)IIb-IIIa,而在缺乏GPIIb-IIIa的血小板无力症(GT)患者的血小板中未观察到这种结合。在此我们报告,GT血小板保留了与纤维连接蛋白包被表面相互作用的能力。与纤维连接蛋白的黏附不需要血小板激活,且可被可溶性纤维连接蛋白、纤维连接蛋白特异性抗体、含精氨酸-甘氨酸-天冬氨酸序列的肽以及鸡胚成纤维细胞纤维连接蛋白受体带3特异性多克隆抗体(抗带3)所抑制。利用抗带3,我们从人血小板中纯化出了第二种纤维连接蛋白受体,它是一种异二聚体,由先前命名为GPIc和GPIIa的糖蛋白组成。GPIc-IIa复合物存在于GT血小板和正常血小板中,且似乎与最近由詹科蒂等人(1986年。《实验细胞研究》163:47 - 62)以及索南伯格等人(1987年。《生物化学杂志》268:10376 - 10383)免疫纯化得到的GP138 kD - GP160 kD复合物相同。在本报告中,我们首次提供证据表明GPIc-IIa实际上介导血小板与纤维连接蛋白包被表面的黏附。因此,GPIc-IIa代表了第二种功能性纤维连接蛋白受体,不同于GPIIb-IIIa,它在很大程度上负责未激活血小板与纤维连接蛋白包被表面的黏附。

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Involvement of fibronectin, Von Willebrand factor, and fibrinogen in platelet interaction with solid substrata.纤连蛋白、血管性血友病因子和纤维蛋白原在血小板与固体基质相互作用中的作用。
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