uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
---|---|
Journal | Journal of Cell Biology |
Volume | 160 |
Issue number | 7 |
Pages (from-to) | 1009-15 |
Number of pages | 7 |
ISSN | 0021-9525 |
DOIs | |
Publication status | Published - 31 Mar 2003 |
- Animals, Cell Adhesion, Cell Movement, Cells, Cultured, Collagen, Collagenases, Endocytosis, Fibroblasts, Fibronectins, Gene Deletion, Matrix Metalloproteinase 13, Membrane Glycoproteins, Mice, Receptors, Cell Surface, Receptors, Mitogen, Receptors, Urokinase Plasminogen Activator, Transferrin, Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
Research areas
ID: 180823055