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

Lars H Engelholm; Karin List; Sarah Netzel-Arnett; Edna Cukierman; David J Mitola; Hannah Aaronson; Lars Kjøller; Jørgen K Larsen; Kenneth M. Yamada; Dudley K Strickland; Kenn Holmbeck; Keld Danø; Henning Birkedal-Hansen; Niels Behrendt; Thomas H. Bugge

doi:10.1083/jcb.200211091

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

Lars H Engelholm, Karin List, Sarah Netzel-Arnett, Edna Cukierman, David J Mitola, Hannah Aaronson, Lars Kjøller, Jørgen K Larsen, Kenneth M. Yamada, Dudley K Strickland, Kenn Holmbeck, Keld Danø, Henning Birkedal-Hansen, Niels Behrendt, Thomas H. Bugge

Engelholm Group

132 Citationer (Scopus)

Abstract

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.

Originalsprog	Engelsk
Tidsskrift	Journal of Cell Biology
Vol/bind	160
Udgave nummer	7
Sider (fra-til)	1009-15
Antal sider	7
ISSN	0021-9525
DOI	https://doi.org/10.1083/jcb.200211091
Status	Udgivet - 31 mar. 2003

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10.1083/jcb.200211091

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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. (2003). uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion. Journal of Cell Biology, 160(7), 1009-15. https://doi.org/10.1083/jcb.200211091

Engelholm, LH, List, K, Netzel-Arnett, S, Cukierman, E, Mitola, DJ, Aaronson, H, Kjøller, L, Larsen, JK, Yamada, KM, Strickland, DK, Holmbeck, K, Danø, K, Birkedal-Hansen, H, Behrendt, N & Bugge, TH 2003, 'uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion', Journal of Cell Biology, bind 160, nr. 7, s. 1009-15. https://doi.org/10.1083/jcb.200211091

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title = "uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion",

abstract = "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.",

keywords = "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",

author = "Engelholm, {Lars H} and Karin List and Sarah Netzel-Arnett and Edna Cukierman and Mitola, {David J} and Hannah Aaronson and Lars Kj{\o}ller and Larsen, {J{\o}rgen K} and Yamada, {Kenneth M.} and Strickland, {Dudley K} and Kenn Holmbeck and Keld Dan{\o} and Henning Birkedal-Hansen and Niels Behrendt and Bugge, {Thomas H.}",

year = "2003",

month = mar,

day = "31",

doi = "10.1083/jcb.200211091",

language = "English",

volume = "160",

pages = "1009--15",

journal = "Journal of Cell Biology",

issn = "0021-9525",

publisher = "Rockefeller University Press",

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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

SN - 0021-9525

VL - 160

SP - 1009

EP - 1015

JO - Journal of Cell Biology

JF - Journal of Cell Biology

IS - 7

ER -

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

Abstract

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