Polymerization of type I and III collagens is dependent on fibronectin and enhanced by integrins alpha 11beta 1 and alpha 2beta 1
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Polymerization of type I and III collagens is dependent on fibronectin and enhanced by integrins alpha 11beta 1 and alpha 2beta 1. / Velling, Teet; Risteli, Juha; Wennerberg, Krister; Mosher, Deane F; Johansson, Staffan.
I: The Journal of Biological Chemistry, Bind 277, Nr. 40, 04.10.2002, s. 37377-81.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Polymerization of type I and III collagens is dependent on fibronectin and enhanced by integrins alpha 11beta 1 and alpha 2beta 1
AU - Velling, Teet
AU - Risteli, Juha
AU - Wennerberg, Krister
AU - Mosher, Deane F
AU - Johansson, Staffan
PY - 2002/10/4
Y1 - 2002/10/4
N2 - Polymerization of the ECM proteins fibronectin and laminin has been shown to take place in close vicinity to the cell surface and be facilitated by beta(1) integrins (Lohikangas, L., Gullberg, D., and Johansson, S. (2001) Exp. Cell Res. 265, 135-144 and Wennerberg, K., Lohikangas, L., Gullberg, D., Pfaff, M., Johansson, S., and Fassler, R. (1996) J. Cell Biol. 132, 227-238). We have studied the role of collagen receptors, integrins alpha(11)beta(1) and alpha(2)beta(1), and fibronectin in collagen polymerization using fibronectin-deficient mouse embryonic fibroblast cell lines. In contrast to the earlier belief that collagen polymerization occurs via self-assembly of collagen molecules we show that a preformed fibronectin matrix is essential for collagen network formation and that collagen-binding integrins strongly enhance this process. Thus, collagen deposition is regulated by the cells, both indirectly through integrin alpha(5)beta(1)-dependent polymerization of fibronectin and directly through collagen-binding integrins.
AB - Polymerization of the ECM proteins fibronectin and laminin has been shown to take place in close vicinity to the cell surface and be facilitated by beta(1) integrins (Lohikangas, L., Gullberg, D., and Johansson, S. (2001) Exp. Cell Res. 265, 135-144 and Wennerberg, K., Lohikangas, L., Gullberg, D., Pfaff, M., Johansson, S., and Fassler, R. (1996) J. Cell Biol. 132, 227-238). We have studied the role of collagen receptors, integrins alpha(11)beta(1) and alpha(2)beta(1), and fibronectin in collagen polymerization using fibronectin-deficient mouse embryonic fibroblast cell lines. In contrast to the earlier belief that collagen polymerization occurs via self-assembly of collagen molecules we show that a preformed fibronectin matrix is essential for collagen network formation and that collagen-binding integrins strongly enhance this process. Thus, collagen deposition is regulated by the cells, both indirectly through integrin alpha(5)beta(1)-dependent polymerization of fibronectin and directly through collagen-binding integrins.
KW - Animals
KW - Cell Line
KW - Cells, Cultured
KW - Collagen Type I/chemistry
KW - Collagen Type III/chemistry
KW - Embryo, Mammalian
KW - Extracellular Matrix Proteins/chemistry
KW - Fibroblasts/physiology
KW - Fibronectins/deficiency
KW - Integrin alpha2beta1/physiology
KW - Integrins/physiology
KW - Mice
KW - Mice, Knockout
KW - Receptors, Collagen/physiology
KW - Recombinant Proteins/metabolism
KW - Transfection
U2 - 10.1074/jbc.M206286200
DO - 10.1074/jbc.M206286200
M3 - Journal article
C2 - 12145303
VL - 277
SP - 37377
EP - 37381
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 40
ER -
ID: 199433607