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J. Biol. Chem., Vol. 279, Issue 30, 31956-31963, July 23, 2004

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Integrin-mediated Cell Adhesion to Type I Collagen Fibrils^*

Johanna Jokinen¶, Elina Dadu¶, Petri Nykvist, Jarmo Käpylä, Daniel J. White, Johanna Ivaska||, Piia Vehviläinen, Hilkka Reunanen, Hannu Larjava, Lari Häkkinen, and Jyrki Heino**

From the Department of Biological and Environmental Science, University of Jyväskylä, Jyväskylä FI-40014, Finland,Department of Oral Biological and Medical Sciences, Faculty of Dentistry, University of British Columbia, Vancouver BC-V6T1Z3, Canada, ^||VTT Medical Biotechnology, University of Turku, Centre for Biotechnology, Turku FI-20520, Finland, and ^**Department of Biochemistry and Food Chemistry, University of Turku, Turku FI-20014, Finland

In the integrin family, the collagen receptors form a structurally and functionally distinct subgroup. Two members of this subgroup, ₁₁ and ₂₁ integrins, are known to bind to monomeric form of type I collagen. However, in tissues type I collagen monomers are organized into large fibrils immediately after they are released from cells. Here, we studied collagen fibril recognition by integrins. By an immunoelectron microscopy method we showed that integrin ₂I domain is able to bind to classical D-banded type I collagen fibrils. However, according to the solid phase binding assay, the collagen fibril formation appeared to reduce integrin ₁I and ₂I domain avidity to collagen and to lower the number of putative I domain binding sites on it. Respectively, cellular ₁₁ integrin was able to mediate cell spreading significantly better on monomeric than on fibrillar type I collagen matrix, whereas ₂₁ integrin appeared still to facilitate both cell spreading on fibrillar type I collagen matrix and also the contraction of fibrillar type I collagen gel. Additionally, ₂₁ integrin promoted the integrin-mediated formation of long cellular projections typically induced by fibrillar collagen. Thus, these findings suggest that ₂₁ integrin is a functional cellular receptor for type I collagen fibrils, whereas ₁₁ integrin may only effectively bind type I collagen monomers. Furthermore, when the effect of soluble I domains on type I collagen fibril formation was tested in vitro, the observations suggest that integrin type collagen receptors might guide or even promote pericellular collagen fibrillogenesis.

Received for publication, February 9, 2004 , and in revised form, May 7, 2004.

^* This work was financially supported by the Academy of Finland, Canadian Institutes for Health Research, the Finnish Cancer Association, the National Graduate School in Informational and Structural Biology, and the Sigrid Jusélius Foundation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ These two authors contributed equally to this work.

To whom correspondence should be addressed: Dept. of Biochemistry and Food Chemistry, Turku FI-20014, University of Turku, Finland. Tel.: 358-2-3336879; Fax: 358-2-3336860; E-mail: jyrki.heino{at}utu.fi.

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