caa a22 4500 378893114 CHVBK 20180305123500.0 cr unu---uuuuu 161128e20040205xx s 000 0 eng 10.1515/BC.2004.031 doi (NATIONALLICENCE)gruyter-10.1515/BC.2004.031 Behrendt N. The urokinase receptor (uPAR) and the uPAR-associated protein (uPARAP/ Endo180): membrane proteins engaged in matrix turnover during tissue remodeling [Elektronische Daten] [N. Behrendt] The breakdown of the barriers formed by extracellular matrix proteins is a pre-requisite for all processes of tissue remodeling. Matrix degradation reactions take part in specific physiological events in the healthy organism but also represent a crucial step in cancer invasion. These degradation processes involve a highly organized interplay between proteases and their cellular binding sites as well as specific substrates and internalization receptors. This review article is focused on two components, the urokinase plasminogen activator receptor (uPAR) and the uPAR-associated protein (uPARAP, also designated Endo180), that are considered crucially engaged in matrix degradation. uPAR and uPARAP have highly diverse functions, but on certain cell types they interact with each other in a process that is still incompletely understood. uPAR is a glycosyl-phosphatidylinositol-anchored glycoprotein on the surface of various cell types that serves to bind the urokinase plasminogen activator and localize the activation reactions in the proteolytic cascade system of plasminogen activation. uPARAP is an integral membrane protein with a pronounced role in the internalization of collagen for intracellular degradation. Both receptors have additional functions that are currently being unraveled. The present discussion of uPAR and uPARAP is centered on their protein structure and molecular and cellular function. Copyright © 2004 by Walter de Gruyter GmbH & Co. KG Biochemistry nationallicence Molecular biology nationallicence Cellular biology nationallicence Biological Chemistry Walter de Gruyter 385/2(2004-02-05), 103-136 1431-6730 385:2<103 2004 385 bchm https://doi.org/10.1515/BC.2004.031 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1515/BC.2004.031 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Behrendt N. NATIONALLICENCE 773 0- Biological Chemistry Walter de Gruyter 385/2(2004-02-05), 103-136 1431-6730 385:2<103 2004 385 bchm CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence SWISSBIB 16006614X BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter