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J. Biol. Chem., Vol. 283, Issue 36, 24506-24513, September 5, 2008

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Supramolecular Interactions in the Dermo-epidermal Junction Zone

ANCHORING FIBRIL-COLLAGEN VII TIGHTLY BINDS TO BANDED COLLAGEN FIBRILS^*

Daniela Villone, Anja Fritsch, Manuel Koch^¶, Leena Bruckner-Tuderman¹, Uwe Hansen², and Peter Bruckner²³

From the Institute for Physiological Chemistry and Pathobiochemistry, University Hospital of Münster, 48149 Münster, the Department of Dermatology, University Medical Center Freiburg, 79104 Freiburg, and the ^¶Center for Biochemistry and Department of Dermatology, Medical Faculty, University of Cologne, D-50931 Cologne, Germany

The dermis and the epidermis of normal human skin are functionally separated by a basement membrane but, together, form a stable structural continuum. Anchoring fibrils reinforce this connection by insertion into the basement membrane and by intercalation with banded collagen fibrils of the papillary dermis. Structural abnormalities in collagen VII, the major molecular constituent of anchoring fibrils, lead to a congenital skin fragility condition, dystrophic epidermolysis bullosa, associated with skin blistering. Here, we characterized the molecular basis of the interactions between anchoring fibrils and banded collagen fibrils. Suprastructural fragments of the dermo-epidermal junction zone were generated by mechanical disruption and by separation with magnetic Immunobeads. Anchoring fibrils were tightly attached to banded collagen fibrils. In vitro binding studies demonstrated that a von Willebrand factor A-like motif in collagen VII was essential for binding of anchoring fibrils to reconstituted collagen I fibrils. Since collagen I and VII molecules reportedly undergo only weak interactions, the attachment of anchoring fibrils to collagen fibrils depends on supramolecular organization of their constituents. This complex is stabilized in situ and resists dissociation by strong denaturants.

Received for publication, March 27, 2008 , and in revised form, July 1, 2008.

^* This work was supported by the Deutsche Forschungsgemeinschaft SFB 492 Grants A2 (to P. B.), KO 2247/3-1 (to M. K.), and Br 1475/8-2 (to L. B.-T.). 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 Supported by the German Ministry of Education and Science, Kompetenznetz "Epidermolysis Bullosa."

² Both authors contributed equally to this work.

³ To whom correspondence should be addressed: Münster University Hospital, Physiological Chemistry and Pathobiochemistry, Waldeyerstrasse 15, 48149 Münster, Germany. Tel.: 49-251-8355591; Fax: 49-251-8355596; E-mail: peter.bruckner{at}uni-muenster.de.

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