HUMAN PLATELET GLYCOPROTEIN-V - CHARACTERIZATION OF THE POLYPEPTIDE AND THE RELATED IB-V-IX RECEPTOR SYSTEM OF ADHESIVE, LEUCINE-RICH GLYCOPROTEINS
HUMAN PLATELET GLYCOPROTEIN-V - CHARACTERIZATION OF THE POLYPEPTIDE AND THE RELATED IB-V-IX RECEPTOR SYSTEM OF ADHESIVE, LEUCINE-RICH GLYCOPROTEINS
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DOI：
10.1073/pnas.90.18.8327
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发表时间：
1993-09-15
影响因子：
11.1
通讯作者：
ROTH, GJ
中科院分区：
文献类型：
--
作者：
HICKEY, MJ;HAGEN, FS;ROTH, GJ
人血小板糖蛋白 (GP) V (M(r) 83,300) 的主要结构在此报告，是表面糖蛋白 Ib-V-IX 系统 (GPs Ibalpha、Ibbeta、V、IX) 的一部分，构成血管性血友病因子 (vWf) 的受体，并介导血小板与动脉循环中受损血管表面的粘附，这是止血的关键起始事件。系统成员共享身体关联、富含亮氨酸的糖蛋白 (LRG) 结构和先天性缺陷状态，即 Bernard-Soulier 综合征。通过PCR技术和血小板cDNA模板，获得了1.4 kb的GP V cDNA序列，编码469个GP V氨基酸。然后分离出基因组 3.5-kb BamHI 片段，其中包括 3.46 kb 的 GPV cDNA 序列：1.7-kb 开放阅读框加上 5' 和 1.8 kb 3' 非翻译区的 2 个碱基。 Northern 印迹分析揭示了 3.8、4.2 和 5.2 kb 的三种 GP V 血小板转录物。存在 16 个氨基酸的信号肽。成熟 GP V 是一种 544 个氨基酸的跨膜蛋白，具有 504 个氨基酸的胞外结构域，在“侧翼-LRG 中心-侧翼”阵列中包含一组 15 个串联 LRG 重复序列 [Roth, G. J. (1991) Blood 77, 5-19]，以及 8 个假定的 N 连接糖基化位点和凝血酶和酶切位点。钙蛋白酶。 GP V 是一种跨膜、粘附性 LRG 蛋白，在动脉中 vWf/剪切依赖性血小板粘附的 Ib-V-IX 受体的表达和/或功能中发挥着不确定但可能至关重要的作用。
Human platelet glycoprotein (GP) V (M(r) 83,300), whose primary structure is reported here, is a part of the Ib-V-IX system of surface glycoproteins (GPs Ibalpha, Ibbeta, V, IX) that constitute the receptor for von Willebrand factor (vWf) and mediate the adhesion of platelets to injured vascular surfaces in the arterial circulation, a critical initiating event in hemostasis. System members share physical associations, leucine-rich glycoprotein (LRG) structures, and a congenital deficiency state, Bernard-Soulier syndrome. With PCR techniques and platelet cDNA templates, 1.4 kb of GP V cDNA sequence was obtained that encodes 469 GP V amino acids. A genomic 3.5-kb BamHI fragment was then isolated that includes 3.46 kb of GPV cDNA sequence: the 1.7-kb open reading frame plus 2 bases of the 5' and 1.8 kb of the 3' untranslated regions. Northern blot analysis reveals three GP V platelet transcripts of 3.8, 4.2, and 5.2 kb. A 16-amino acid signal peptide is present. Mature GP V is a 544-amino acid transmembrane protein with a 504-amino acid extracellular domain that encompasses a set of 15 tandem LRG repeats in a ''flank-LRG center-flank'' array [Roth, G. J. (1991) Blood 77, 5-19] along with eight putative N-linked glycosylation sites and cleavage sites for thrombin and calpain. GP V is a transmembrane, adhesive LRG protein that plays an undefined, but potentially critical, role in the expression and/or function of the Ib-V-IX receptor for vWf/shear-dependent platelet adhesion in arteries.