The collagen receptor uPARAP/Endo180

作者：Engelholm Lars H^*; Ingvarsen Signe; Jurgensen Henrik J; Hillig Thore; Madsen Daniel H; Nielsen Boye S; Behrendt Niels

来源：Frontiers in Bioscience-Landmark, 2009, 14(14): 2103-2114.

DOI：10.2741/3365

• Collagen receptor
• Internalization Receptor
• Intracellular Collagen Degradation
• Collagenolysis
• Matrix Metalloproteinases
• Endocytic Pathway
• Lysosomal Collagen Breakdown
• Review

The 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

• 出版日期2009-1-1