Efficient plasma membrane expression of a functional platelet glycoprotein Ib-IX complex requires the presence of its three subunits.
Efficient plasma membrane expression of a functional platelet glycoprotein Ib-IX complex requires the presence of its three subunits.
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DOI：
10.1016/s0021-9258(18)42354-x
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发表时间：
1992-06
期刊：
影响因子：
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通讯作者：
José A López;B. Leung;C. Reynolds;Chester Q. Li;J. Fox
中科院分区：
文献类型：
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作者：
José A López;B. Leung;C. Reynolds;Chester Q. Li;J. Fox
血小板质膜的糖蛋白（GP） Ib-IX复合物介导血小板对受损血管壁的粘附。该复合物由GP Ib α、GP Ib β和GP IX三种跨膜多肽组成，这些多肽均不存在于遗传性出血性疾病Bernard-Soulier综合征患者的血小板中。在本研究中，我们报道了重组受体在三种细胞系中的稳定表达，并证明了该复合物的三个亚基是其在质膜上有效表达所必需的。表达的复合物通过与肌动蛋白结合蛋白的相互作用与转染细胞的细胞骨架结合，并结合其配体血管性血友病因子。这些数据表明，Bernard-Soulier综合征中质膜GP Ib-IX复合物的缺乏可能是由影响其三个亚基中的任何一个的突变引起的。
The glycoprotein (GP) Ib-IX complex of the platelet plasma membrane mediates the adhesion of platelets to damaged blood vessel wall. The complex is composed of three membrane-spanning polypeptides, GP Ib alpha, GP Ib beta, and GP IX, all of which are absent from the platelets of patients with the hereditary bleeding disorder Bernard-Soulier syndrome. In this study we report stable expression of the recombinant receptor in three cell lines and demonstrate that the three subunits of the complex are necessary for its efficient expression on the plasma membrane. The expressed complex associates with the cytoskeleton of the transfected cells through an interaction with actin-binding protein and binds its ligand, von Willebrand factor. These data suggest that the lack of plasma membrane GP Ib-IX complex in the Bernard-Soulier syndrome could potentially arise from mutations affecting any one of its three subunits.