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The collagen receptor uPARAP/Endo180 Engelholm LH; Ingvarsen S; Jurgensen HJ; Hillig T; Madsen DH; Nielsen BS; Behrendt NFront Biosci (Landmark Ed) 2009[Jan]; 14 (6): 2103-14The uPAR-associated protein (uPARAP/Endo180), a type-1 membrane protein belonging to the mannose receptor family, is an endocytic receptor for collagen. Through this endocytic function, the protein takes part in a previously unrecognized mechanism of collagen turnover. uPARAP/Endo180 can bind and internalize both intact and partially degraded collagens. In some turnover pathways, the function of the receptor probably involves an interplay with certain matrix-degrading proteases whereas, in other physiological processes, redundant mechanisms involving both endocytic and pericellular collagenolysis seem to operate in parallel. On certain cell types, uPARAP/Endo180 occurs in a complex with the urokinase plasminogen activator receptor (uPAR) where it seems to fulfill other functions in addition to collagenolysis. uPARAP/Endo180 is expressed on various mesenchymal cells, including subpopulations of fibroblasts, osteoblasts and chondrocytes, generally in conjunction with matrix turnover and collagenolysis. A striking expression is found in developing bone where the collagenolytic function of uPARAP/Endo180 is one of the rate-limiting steps in growth. In murine breast tumors, the endocytic function of the receptor in collagen breakdown seems to be involved in invasive tumor growth.|Humans[MESH]|Mannose-Binding Lectins/chemistry/*metabolism[MESH]|Membrane Glycoproteins/chemistry/*metabolism[MESH]|Protein Conformation[MESH]|Receptors, Cell Surface/chemistry/*metabolism[MESH]|Receptors, Mitogen/chemistry/*metabolism[MESH] |
