期刊
FRONTIERS IN BIOSCIENCE-LANDMARK
卷 14, 期 -, 页码 2103-2114出版社
BIOSCIENCE RESEARCH INST-BRI
DOI: 10.2741/3365
关键词
Collagen receptor; Internalization Receptor; Intracellular Collagen Degradation; Collagenolysis; Matrix Metalloproteinases; Endocytic Pathway; Lysosomal Collagen Breakdown; Review
资金
- EU [LSHC-CT-2003-503297]
- Danish Cancer Society
- Danish Cancer Research Foundation
- Danish Medical Research Council
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
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