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Originally published In Press as doi:10.1074/jbc.M008709200 on October 20, 2000

J. Biol. Chem., Vol. 276, Issue 2, 1594-1601, January 12, 2001
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Properties of the Collagen Type XVII Ectodomain
EVIDENCE FOR N- TO C-TERMINAL TRIPLE HELIX FOLDING*

Sayed K. AreidaDagger §, Dieter P. ReinhardtDagger , Peter K. MüllerDagger , Peter P. FietzekDagger , Jutta Köwitz||, M. Peter Marinkovich**, and Holger NotbohmDagger Dagger Dagger

From the Dagger  Medizinische Universität zu Lübeck, Institut für Medizinische Molekularbiologie, Ratzeburger Allee 160, D-23538 Lübeck, Germany, ** Dermatology Service, Veterans Affairs Palo Alto Health Care System, Palo Alto, California 94304 and Program in Epithelial Biology, Stanford University School of Medicine, Stanford, California 94305, and || Orthopädische Klinik, Universität Rostock, Ulmenstrasse 44, D-18057 Rostock, Germany

Collagen XVII is a transmembrane component of hemidesmosomal cells with important functions in epithelial-basement membrane interactions. Here we report on properties of the extracellular ectodomain of collagen XVII, which harbors multiple collagenous stretches. We have recombinantly produced subdomains of the collagen XVII ectodomain in a mammalian expression system. rColXVII-A spans the entire ectodomain from delta NC16a to NC1, rColXVII-B is similar but lacks the NC1 domain, a small N-terminal polypeptide rColXVII-C encompasses domains delta NC16a to C15, and a small C-terminal polypeptide rColXVII-D comprises domains NC6 to NC1. Amino acid analysis of rColXVII-A and -C demonstrated prolyl and lysyl hydroxylation with ratios for hydroxyproline/proline of 0.4 and for hydroxylysine/lysine of 0.5. A small proportion of the hydroxylysyl residues in rColXVII-C (~3.3%) was glycosylated. Limited pepsin and trypsin degradation assays and analyses of circular dichroism spectra clearly demonstrated a triple-helical conformation for rColXVII-A, -B, and -C, whereas the C-terminal rColXVII-D did not adopt a triple-helical fold. These results were further substantiated by electron microscope analyses, which revealed extended molecules for rColXVII-A and -C, whereas rColXVII-D appeared globular. Thermal denaturation experiments revealed melting temperatures of 41 °C (rColXVII-A), 39 °C (rColXVII-B), and 35 °C (rColXVII-C). In summary, our data suggest that triple helix formation in the ectodomain of ColXVII occurs with an N- to C-terminal directionality.

* This work was supported by Deutsche Forschungsgemeinschaft Grants DFG-No-147-6 (to H. N.), and Re 1021/4-1 (to D. P. R.), and National Institutes of Health Grant P01-AR 44012 (to M. P. M.).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.

§ Supported by a scholarship from the Zoological Department, Faculty of Science, University of Mansura, Mansura, Egypt.

Recipient of a Volkswagen Foundation stipend for his stay on sabbatical leave in Stanford.

Dagger Dagger To whom correspondence should be addressed. Tel.: 49-451-500-4083; Fax: 49-451-500-3637; E-mail: notbohm@molbio.mu-luebeck.de.

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