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J. Biol. Chem., Vol. 281, Issue 37, 27461-27470, September 15, 2006

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Collagen XII Interacts with Avian Tenascin-X through Its NC3 Domain^*

Guido Veit, Uwe Hansen, Douglas R. Keene^¶, Peter Bruckner, Ruth Chiquet-Ehrismann^||, Matthias Chiquet^||, and Manuel Koch^**1

From the Center for Biochemistry, ^**Department of Dermatology, and Center for Molecular Medicine Cologne, Medical Faculty, University of Cologne, D-50931 Cologne, Germany, Institut für Physiologische Chemie und Pathobiochemie, Universitätsklinikum Münster, 48129 Münster, Germany, ^¶Shriners Hospital for Children Research Center, Portland, Oregon 97239, and ^||Friedrich Miescher Institute, 4002 Basel, Switzerland

Large oligomeric proteins often contain several binding sites for different molecules and can therefore induce formation of larger protein complexes. Collagen XII, a multidomain protein with a small collagenous region, interacts with fibrillar collagens through its C-terminal region. However, no interactions to other extracellular proteins have been identified involving the non-collagenous N-terminal NC3 domain. To further elucidate the components of protein complexes present close to collagen fibrils, different extracellular matrix proteins were tested for interaction in a solid phase assay. Binding to the NC3 domain of collagen XII was found for the avian homologue of tenascin-X that in humans is linked to Ehlers-Danlos disease. The binding was further characterized by surface plasmon resonance spectroscopy and supported by immunohistochemical co-localization in chick and mouse tissue. On the ultrastructural level, detection of collagen XII and tenascin-X by immunogold labeling confirmed this finding.

Received for publication, April 3, 2006 , and in revised form, July 14, 2006.

^* This work was supported by an award from the Alexander von Humboldt Foundation, the Federal Ministry of Education and Research in Germany, Deutsche Forschungsgemeinschaft Grant SFB 589 P1, KO 2247/2-1, Köln Fortune (to M. K.), and Grant SFB 492, A2 (to P. B.). 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 To whom correspondence should be addressed: Center for Biochemistry, Medical Faculty, University of Cologne, Joseph-Stelzmann-Str. 52, D-50931 Cologne, Germany. Tel.: 49-221-478-6990; Fax: 49-221-478-6977; E-mail: Manuel.Koch{at}uni-koeln.de.

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