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J. Biol. Chem., Vol. 281, Issue 6, 3494-3504, February 10, 2006

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Collagen XXVIII, a Novel von Willebrand Factor A Domain-containing Protein with Many Imperfections in the Collagenous Domain^*

Guido Veit, Birgit Kobbe, Douglas R. Keene, Mats Paulsson^¶, Manuel Koch^¶||1, and Raimund Wagener¹²

From the Center for Biochemistry, ^¶Center for Molecular Medicine, and ^||Department of Dermatology, Medical Faculty, University of Cologne, D-50931 Cologne, Germany and the Shriners Hospital for Children Research Center, Portland, Oregon 97239

Here we describe a novel collagen belonging to the class of von Willebrand factor A (VWA) domain-containing proteins. This novel protein was identified by screening the EST data base and was subsequently recombinantly expressed and characterized as an authentic tissue component. The COL28A1 gene on human chromosome 7p21.3 and on mouse chromosome 6A1 encodes a novel protein that structurally resembles the beaded filament-forming collagens. The collagenous domain contains several very short interruptions arranged in a repeat pattern. As shown for other novel minor collagens, the expression of collagen XXVIII protein in mouse is very restricted. In addition to small amounts in skin and calvaria, the major signals were in dorsal root ganglia and peripheral nerves. By immunoelectron microscopy, collagen XXVIII was detected in the sciatic nerve, at the basement membrane of certain Schwann cells surrounding the nerve fibers. Even though the protein is present in the adult sciatic nerve, collagen XXVIII mRNA was only detected in sciatic nerve of newborn mice, indicating that the protein persists for an extended period after synthesis.

Received for publication, August 24, 2005 , and in revised form, November 16, 2005.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AJ890449 [GenBank] -AJ890453 for mouse and human collagen XXVIII cDNA.

^* This work was supported by Deutsche Forschungsgemeinschaft Grants WA 1338/2-3 and SFB 589, the Köln Fortune program of the Medical Faculty of the University of Cologne, the Maria-Pesch-Stiftung, a career development award from the Alexander von Humboldt Foundation and the German Federal Ministry of Education and Research (to M. K.). 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 Equivalent senior authors.

² To whom correspondence should be addressed: Institute for Biochemistry II, 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: raimund.wagener{at}uni-koeln.de.

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