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Originally published In Press as doi:10.1074/jbc.M101182200 on April 19, 2001

J. Biol. Chem., Vol. 276, Issue 26, 24352-24359, June 29, 2001
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Control of Heterotypic Fibril Formation by Collagen V Is Determined by Chain Stoichiometry*

Hélène Chanut-DelalandeDagger , Agnès Fichard, Simonetta Bernocco§, Robert Garrone, David J. S. Hulmes, and Florence Ruggiero

From the Institut de Biologie et Chimie des Protéines, Unite Mixte de Recherche, Centre National de la Recherche Scientifique 5086, Université Claude Bernard Lyon I, 69367 Lyon Cedex 07, France

Although the collagen V heterotrimer is known to be involved in the control of fibril assembly, the role of the homotrimer in fibrillar organization has not yet been examined. Here, the production of substantial amounts of recombinant collagen V homotrimer has allowed a detailed study of its role in homotypic and heterotypic fibril formation. After removal of terminal regions by pepsin digestion, both the collagen V heterotrimer and homotrimer formed thin homotypic fibrils, thus showing that diameter limitation is at least in part an intrinsic property of the collagen V triple helix. When mixed with collagen I, however, various complementary approaches indicated that the collagen V heterotrimer and homotrimer exerted different effects in heterotypic fibril formation. Unlike the heterotrimer, which was buried in the fibril interior, the homotrimer was localized as thin filamentous structures at the surface of wide collagen I fibrils and did not regulate fibril assembly. Its localization at the fibril surface suggests that the homotrimer can act as a molecular linker between collagen fibrils or macromolecules in the extracellular matrix or both. Thus, depending on their respective distribution in tissues, the different collagen V isoforms might fulfill specific biological functions.

* This work was supported by the Association pour la Recherche contre le Cancer and by a program of the European Community (Contract BIO-4-CT96-0537).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Recipient of a fellowship from the Ministère de la Recherche.

§ Recipient of a fellowship from the Fondation pour la Recherche Médicale.

To whom correspondence should be addressed: Institut de Biologie et Chimie des Protéines, Unite Mixte de Recherche, Centre National de la Recherche Scientifique 5086, Université Claude Bernard Lyon I, 7 Passage du Vercors, 69367 Lyon Cedex 07, France. Tel.: 33-4-72-72-26-57; Fax: 33-4-72-72-26-02; E-mail: f.ruggiero@ibcp.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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