Alfano Daniela, Franco Paola, Stoppelli Maria Patrizia
Institute of Genetics and Biophysics "Adriano Buzzati-Traverso", National Research Council, Naples, Italy.
Front Cell Dev Biol. 2022 Apr 8;10:818616. doi: 10.3389/fcell.2022.818616. eCollection 2022.
Urokinase-type plasminogen activator receptor (uPAR or CD87) is a glycosyl-phosphatidyl-inositol anchored (GPI) membrane protein. The uPAR primary ligand is the serine protease urokinase (uPA), converting plasminogen into plasmin, a broad spectrum protease, active on most extracellular matrix components. Besides uPA, the uPAR binds specifically also to the matrix protein vitronectin and, therefore, is regarded also as an adhesion receptor. Complex formation of the uPAR with diverse transmembrane proteins, including integrins, formyl peptide receptors, G protein-coupled receptors and epidermal growth factor receptor results in intracellular signalling. Thus, the uPAR is a multifunctional receptor coordinating surface-associated pericellular proteolysis and signal transduction, thereby affecting physiological and pathological mechanisms. The uPAR-initiated signalling leads to remarkable cellular effects, that include increased cell migration, adhesion, survival, proliferation and invasion. Although this is beyond the scope of this review, the uPA/uPAR system is of great interest to cancer research, as it is associated to aggressive cancers and poor patient survival. Increasing evidence links the uPA/uPAR axis to epithelial to mesenchymal transition, a highly dynamic process, by which epithelial cells can convert into a mesenchymal phenotype. Furthermore, many reports indicate that the uPAR is involved in the maintenance of the stem-like phenotype and in the differentiation process of different cell types. Moreover, the levels of anchor-less, soluble form of uPAR, respond to a variety of inflammatory stimuli, including tumorigenesis and viral infections. Finally, the role of uPAR in virus infection has received increasing attention, in view of the Covid-19 pandemics and new information is becoming available. In this review, we provide a mechanistic perspective, via the detailed examination of consolidated and recent studies on the cellular responses to the multiple uPAR activities.
尿激酶型纤溶酶原激活物受体(uPAR或CD87)是一种糖基磷脂酰肌醇锚定(GPI)膜蛋白。uPAR的主要配体是丝氨酸蛋白酶尿激酶(uPA),它将纤溶酶原转化为纤溶酶,纤溶酶是一种广谱蛋白酶,对大多数细胞外基质成分具有活性。除uPA外,uPAR还特异性结合基质蛋白玻连蛋白,因此也被视为一种黏附受体。uPAR与多种跨膜蛋白(包括整合素、甲酰肽受体、G蛋白偶联受体和表皮生长因子受体)形成复合物会导致细胞内信号传导。因此,uPAR是一种多功能受体,可协调表面相关的细胞周围蛋白水解和信号转导,从而影响生理和病理机制。uPAR启动的信号传导会导致显著的细胞效应,包括增加细胞迁移、黏附、存活、增殖和侵袭。尽管这超出了本综述的范围,但uPA/uPAR系统在癌症研究中备受关注,因为它与侵袭性癌症和患者生存率低有关。越来越多的证据将uPA/uPAR轴与上皮-间质转化联系起来,上皮-间质转化是一个高度动态的过程,上皮细胞可通过该过程转化为间充质表型。此外,许多报道表明uPAR参与维持干细胞样表型以及不同细胞类型的分化过程。此外,无锚定的可溶性uPAR水平会对多种炎症刺激作出反应,包括肿瘤发生和病毒感染。最后,鉴于新冠疫情,uPAR在病毒感染中的作用受到越来越多的关注,并且新信息不断涌现。在本综述中,我们通过详细研究关于细胞对多种uPAR活性反应的已有的和最新的研究,提供了一个机制方面的观点。