尿激酶受体（CD87）突变体在细胞上表达的变化：与细胞黏附的相关性,Cell Biochemistry and Function

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尿激酶受体（CD87）突变体在细胞上表达的变化：与细胞黏附的相关性
Cell Biochemistry and Function ( IF 2.8 ) Pub Date : 2004-07-01 , DOI: 10.1002/cbf.1098
Sandip M. Kanse , Triantafyllos Chavakis , Alice Kuo , Khalil Bdeir , Douglas B. Cines , Klaus T. Preissner

尿激酶型纤溶酶原激活剂受体（uPAR，CD87）是糖基磷脂酰肌醇（GPI）锚定的蛋白，包含三个同源的Ly-6结构域，通过直接结合细胞外基质蛋白玻连蛋白（VN）介导整联蛋白独立的细胞粘附。为了阐明uPAR依赖的细胞在VN上粘附的结构要求，在BAF3细胞（小鼠B淋巴细胞前体）中表达了uPAR的几个糖脂锚定变体，然后进行功能分析。uPAR的单个结构域表达水平很低，两个结构域突变体的表达水平较高，而野生型uPAR的表达水平很高。已显示uPAR结构域2中的点突变可减少配体尿激酶的细胞结合，我们观察到缺乏与该突变体结合的VN。用多种单克隆抗体进行的流式细胞术表明，这些突变体中的域特异性抗原决定簇保存完好。仅表达具有全部三个结构域的完整uPAR的细胞牢固地粘附于VN底物，而其他转染的细胞均未显示出明显的细胞粘附。因此，uPAR结构域的任何改变都会降低其表达，只有完整的受体才能维持在炎症和损伤部位发现的富含VN的基质上的直接细胞粘附。版权所有©2004 John Wiley＆Sons，Ltd. 而其他转染细胞均未显示明显的细胞粘附。因此，uPAR结构域的任何改变都会降低其表达，只有完整的受体才能维持在炎症和损伤部位发现的富含VN的基质上的直接细胞粘附。版权所有©2004 John Wiley＆Sons，Ltd. 而其他转染细胞均未显示明显的细胞粘附。因此，uPAR结构域的任何改变都会降低其表达，只有完整的受体才能维持在炎症和损伤部位发现的富含VN的基质上的直接细胞粘附。版权所有©2004 John Wiley＆Sons，Ltd.

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Variability in the expression of urokinase receptor(CD87) mutants on cells: relevance to cell adhesion

The urokinase‐type plasminogen activator receptor (uPAR, CD87) is a glycosylphosphatidylinositol (GPI)‐anchored protein, containing three homologous Ly‐6 domains, that mediates integrin‐independent cell adhesion by directly binding to extracellular matrix protein vitronectin (VN). To elucidate the structural requirements for the uPAR‐dependent cell adhesion on VN, several glycolipid‐anchored variants of uPAR were expressed in BAF3 cells, (mouse pre B‐lymphocytes) followed by functional analysis. The individual domains of uPAR were expressed at very low levels, the two domain mutants were expressed to a higher level and the wild type uPAR was expressed highly. Point mutations in domain 2 of uPAR have been shown to diminish cellular binding of the ligand urokinase and we observed a lack of VN binding to this mutant. Flow cytometry with a number of monoclonal antibodies indicated that the domain‐specific antigenic determinants in these mutants were well preserved. Only the cells expressing the intact uPAR with all three domains adhered strongly to a VN substrate, whereas none of the other transfected cells showed significant cell adhesion. Hence, any alterations in the domain structure of uPAR reduce its expression and only the intact receptor can sustain the direct cell adhesion on VN‐rich matrices found at sites of inflammation and injury. Copyright © 2004 John Wiley & Sons, Ltd.

更新日期：2004-07-01

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