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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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uPARAP/ Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion.

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.[1]

References

  1. uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion. Engelholm, L.H., List, K., Netzel-Arnett, S., Cukierman, E., Mitola, D.J., Aaronson, H., Kjøller, L., Larsen, J.K., Yamada, K.M., Strickland, D.K., Holmbeck, K., Danø, K., Birkedal-Hansen, H., Behrendt, N., Bugge, T.H. J. Cell Biol. (2003) [Pubmed]
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