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J. Biol. Chem., Vol. 282, Issue 16, 11805-11816, April 20, 2007

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A Comparative Analysis of the Fibulin Protein Family

BIOCHEMICAL CHARACTERIZATION, BINDING INTERACTIONS, AND TISSUE LOCALIZATION^*

Naoyuki Kobayashi, Günter Kostka¹, Jörg H. O. Garbe, Douglas R. Keene, Hans Peter Bächinger^¶, Franz-Georg Hanisch^||, Dessislava Markova^**, Takeshi Tsuda, Rupert Timpl², Mon-Li Chu^**, and Takako Sasaki³

From the Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany, the Shriners Hospital for Children and the ^¶Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, Oregon 97239, the ^||Institute for Biochemistry II, Medical Faculty, and Center for Molecular Medicine Cologne (CMMC), University of Cologne, D-50931 Cologne, Germany, the ^**Department of Dermatology and Cutaneous Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, and Nemours Cardiac Center and Nemours Biomedical Research, Alfred I. DuPont Hospital for Children, Wilmington, Delaware 19899

Fibulins are a family of five extracellular matrix proteins characterized by tandem arrays of epidermal growth factor-like domains and a C-terminal fibulin-type module. They are widely distributed and often associated with vasculature and elastic tissues. In this study, we expressed the three more recently identified family members, fibulin-3, fibulin-4, and fibulin-5, as recombinant proteins in mammalian cells. The purified proteins showed short rod structures of 20 nm with a globule at one end, after rotary shadowing and electron microscopy. Two forms of mouse fibulin-3 were purified, and the O-glycan profiles of the larger form were characterized. Polyclonal antibodies raised against the purified proteins did not show any cross-reactivity with other family members and were used to assess the levels and localization of the fibulins in mouse tissues. Their binding interactions, cell adhesive properties, and tissue localization were analyzed in parallel with the previously characterized fibulin-1 and -2. Binding to tropoelastin was strong for fibulin-2 and -5, moderate for fibulin-4 and -1, and relatively weak for fibulin-3. Fibulin-4, but not fibulin-3 and -5, exhibited distinct interactions with collagen IV and nidogen-2 and moderate binding to the endostatin domain from collagen XV. Cell adhesive activities were not observed for all fibulins, except mouse fibulin-2, with various cell lines tested. All five fibulins were found in perichondrium and various regions of the lungs. Immunoelectron microscopy localized fibulin-4 and -5 to fibrillin microfibrils at distinct locations. Our studies suggest there are unique and redundant functions shared by these structurally related proteins.

Received for publication, November 30, 2006 , and in revised form, February 6, 2007.

^* This work was supported by the Deutsche Forschungsgemeinschaft (DFG) (Grants Sa 1003/1 and -2), the European Commission (Grant QLK3-CT2000-00084 to R. T. and T. S.), the DFG (Grants Ha 2092/11–1 and -2 to F. G. H.), Shriners Hospital for Children (to H. P. B. and D. R. K.), and National Institutes of Health Grant GM55625 (to M. L. C.). 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.

¹ Deceased on January 19, 2006.

² Deceased on October 20, 2003.

³ To whom correspondence should be addressed: The Shriners Hospital for Children, 3101 SW Sam Jackson Park Rd., Portland, OR 97239. Tel.: 503–221-3782; Fax: 503–221-3451; E-mail: txs{at}shcc.org.

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