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Urokinase Receptor (CD87) Clustering in Detergent-Insoluble Adhesion Patches Leads to Cell Adhesion Independently of Integrins

机译:洗涤剂不溶性粘附斑中的尿激酶受体(CD87)聚集导致细胞粘附独立于整联蛋白。

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摘要

The urokinase-type plasminogen activator receptor (uPAR) is a glycosylphosphatidyl inositol-anchored protein that mediates cell adhesion to the extracellular matrix protein vitronectin (VN). We demonstrate here that this cell adhesion process is accompanied by the formation of an adhesion patch characterized by an accumulation of uPAR into areas of direct contact between the cell and the matrix. The adhesion patch requires the glycolipid anchor and develops only on a VN-coated substrate, but not on fibronectin. It consists of detergent-insoluble microdomains that accumulate F-actin and tyrosine-phosphorylated proteins, but not 1 integrins. Lack of inhibition of adhesion in the presence of integrin-blocking reagents and adhesion on a VN fragment without the RGD sequence indicated that the adhesion of uPAR-bearing cells on VN could occur independently of integrins. Hence, uPAR-mediated cell adhesion on VN relies on the formation of a unique cellular structure that we have termed "detergent-insoluble adhesion patch" (DIAP).
机译:尿激酶型纤溶酶原激活剂受体(uPAR)是糖基磷脂酰肌醇锚定蛋白,介导细胞与细胞外基质蛋白玻连蛋白(VN)的粘附。我们在这里证明,这种细胞粘附过程伴随着粘附斑块的形成,其特征是uPAR积累到细胞与基质之间直接接触的区域中。粘附贴剂需要糖脂锚定物,并且仅在VN涂层的基底上而不在纤连蛋白上发育。它由不溶于洗涤剂的微区组成,这些微区积聚了F-肌动蛋白和酪氨酸磷酸化的蛋白质,但没有1个整联蛋白。在没有整联蛋白封闭剂的情况下缺乏对粘附的抑制以及在没有RGD序列的VN片段上的粘附均表明含uPAR的细胞在VN上的粘附可能独立于整联蛋白而发生。因此,uPAR介导的细胞在VN上的粘附依赖于独特细胞结构的形成,我们称其为“洗涤剂不溶性粘附斑”(DIAP)。

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