uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion
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uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion. / Engelholm, Lars H; List, Karin; Netzel-Arnett, Sarah; Cukierman, Edna; Mitola, David J; Aaronson, Hannah; Kjøller, Lars; Larsen, Jørgen K; Yamada, Kenneth M.; Strickland, Dudley K; Holmbeck, Kenn; Danø, Keld; Birkedal-Hansen, Henning; Behrendt, Niels; Bugge, Thomas H.
I: Journal of Cell Biology, Bind 160, Nr. 7, 31.03.2003, s. 1009-15.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion
AU - Engelholm, Lars H
AU - List, Karin
AU - Netzel-Arnett, Sarah
AU - Cukierman, Edna
AU - Mitola, David J
AU - Aaronson, Hannah
AU - Kjøller, Lars
AU - Larsen, Jørgen K
AU - Yamada, Kenneth M.
AU - Strickland, Dudley K
AU - Holmbeck, Kenn
AU - Danø, Keld
AU - Birkedal-Hansen, Henning
AU - Behrendt, Niels
AU - Bugge, Thomas H.
PY - 2003/3/31
Y1 - 2003/3/31
N2 - 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.
AB - 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.
KW - Animals
KW - Cell Adhesion
KW - Cell Movement
KW - Cells, Cultured
KW - Collagen
KW - Collagenases
KW - Endocytosis
KW - Fibroblasts
KW - Fibronectins
KW - Gene Deletion
KW - Matrix Metalloproteinase 13
KW - Membrane Glycoproteins
KW - Mice
KW - Receptors, Cell Surface
KW - Receptors, Mitogen
KW - Receptors, Urokinase Plasminogen Activator
KW - Transferrin
KW - Comparative Study
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
U2 - 10.1083/jcb.200211091
DO - 10.1083/jcb.200211091
M3 - Journal article
C2 - 12668656
VL - 160
SP - 1009
EP - 1015
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 7
ER -
ID: 180823055