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Originally published In Press as doi:10.1074/jbc.M110583200 on November 28, 2001

J. Biol. Chem., Vol. 277, Issue 6, 4565-4572, February 8, 2002
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Versican Interacts with Fibrillin-1 and Links Extracellular Microfibrils to Other Connective Tissue Networks*

Zenzo IsogaiDagger §, Anders Aspberg, Douglas R. KeeneDagger , Robert N. OnoDagger , Dieter P. Reinhardt||, and Lynn Y. SakaiDagger **Dagger Dagger

From the Dagger  Shriners Hospital for Children and the ** Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, Oregon 97201, the  Department of Cell and Molecular Biology, Section for Connective Tissue Biology, University of Lund, Lund SE-22184, Sweden, and the || Department of Medical Molecular Biology, Medical University of Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany

Fibrillin-containing microfibrils are polymeric structures that are difficult to extract from connective tissues. Proteolytic digestion of tissues has been utilized to release microfibrils for study. Few of the molecules that connect microfibrils to other elements in the matrix have been identified. In this study, electron microscopic immunolocalization of anti-versican antibodies in tissues and in extracted microfibrils demonstrated that the C-terminal region of versican is found associated with fibrillin microfibrils. Extraction of microfibrils followed by treatment of microfibrils under dissociating conditions suggested that the versican C terminus is covalently bound to microfibrils. Binding assays using recombinant fibrillin-1 polypeptides and recombinant lectican lectin domains indicated that the versican lectin domain binds to specific fibrillin-1 polypeptides. The versican lectin domain also bound to molecules comigrating with authentic fibrillin-1 monomers in an assay using cell culture medium. In assays using microfibrils, the versican lectin domain demonstrated preferential binding compared with other lecticans. Binding was calcium-dependent. The binding site for versican in microfibrils is most likely within a region of fibrillin-1 between calcium-binding epidermal growth factor-like domains 11 and 21. Human mutations in this region can result in severe forms of the Marfan syndrome ("neonatal" Marfan syndrome). The connection between versican and fibrillin microfibrils may be functionally significant, particularly in cardiovascular tissues.

* This work was supported by grants from the Shriners Hospitals for Children (to D. R. K. and L. Y. S.), special coordination funds from the Science and Technology Agency of the Japanese Government (to Z. I.), a grant from the Swedish Medical Research Council (to A. A.), and Deutsche Forschungsgemeinschaft Grant Re1021/3-1 (to D. P. R.).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.

§ Present address: Dept. of Dermatology, Nagoya City University Medical School, Kawasumi 1, Mizuho-cho, Mizuho-ku, Nagoya, Aichi 467-8602, Japan.

Dagger Dagger To whom correspondence should be addressed: Shriners Hospital for Children, 3101 SW Sam Jackson Park Rd., Portland, OR 97201. Tel.: 503-221-3436; Fax: 503-221-3451; E-mail: lys@shcc.org.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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