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First published online April 24, 2006
doi: 10.1242/10.1242/jcs.02921

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Interactions of primary fibroblasts and keratinocytes with extracellular matrix proteins: contribution of ₂ß₁ integrin

¹ Department of Dermatology, Medical Faculty, University of Cologne, 50931 Cologne, Germany
² Center for Biochemistry, Medical Faculty, University of Cologne, 50931 Cologne, Germany
⁴ Institute for Vegetative Physiology, Medical Faculty, University of Cologne, 50931 Cologne, Germany
³ Department of Biomedicine, Division of Physiology, University of Bergen, 5020 Bergen, Norway
⁵ Center for Molecular Medicine Cologne (CMMC), University of Cologne, 50931 Cologne, Germany

^* Author for correspondence (e-mail: aumailley{at}uni-koeln.de)

Accepted 25 January 2006

The ₂ß₁ integrin is a collagen-binding protein with very high affinity for collagen I. It also binds several other collagens and laminins and it is expressed by many cells, including keratinocytes and fibroblasts in the skin. In the past, ₂ß₁ integrin was suggested to be responsible for cell attachment, spreading and migration on monomeric collagen I and contraction of three-dimensional collagen lattices. In view of these functions, normal development and fertility in integrin ₂-deficient mice, which we generated by targeting the integrin ₂ gene, came as a surprise. This suggested the existence of compensatory mechanisms that we investigate here using primary fibroblasts and keratinocytes isolated from wild-type and ₂-deficient mice, antibodies blocking integrin function and downregulation of integrin ₂ expression. The results show that the ₂ß₁ integrin is absolutely required for keratinocyte adhesion to collagens whereas for fibroblasts other collagen-binding integrins partially back-up the lack of ₂ß₁ in simple adhesion to collagen monomers. A prominent requirement for ₂ß₁ integrins became apparent when fibroblasts executed mechanical tasks of high complexity in three-dimensional surroundings, such as contracting free-floating collagen gels and developing isometric forces in tethered lattices. The deficits observed for ₂-deficient fibroblasts appeared to be linked to alterations in the distribution of force-bearing focal adhesions and deregulation of Rho-GTPase activation.

Key words: Fibroblast, Keratinocyte, Adhesion, Migration, Force, RhoGTPase

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