期刊
JOURNAL OF CELL BIOLOGY
卷 160, 期 7, 页码 1009-1015出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200211091
关键词
cell adhesion; integrin; matrix internalization; matrix metallo-proteinase; uPAR
类别
The uptake and lysosomal degradation of collagen by fibroblasts constitute a major pathway in the turnover of connective tissue. However, the molecular mechanisms governing this pathway are poorly understood. Here, we show that the urokinase plasminogen activator receptor-associated protein (uPARAP)/Endo180, a novel mesenchymally expressed member of the macrophage mannose receptor family of endocytic receptors, is a key player in this process. Fibroblasts from mice with a targeted deletion in the uPARAP/Endo180 gene displayed a near to complete abrogation of collagen endocytosis. Furthermore, these cells had diminished initial adhesion to a range of different collagens, as well as impaired migration on fibrillar collagen. These studies identify a central function of uPARAP/Endo180 in cellular collagen interactions.
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