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J. Biol. Chem., Vol. 279, Issue 21, 22514-22521, May 21, 2004

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A Novel Marker of Tissue Junctions, Collagen XXII^*

Manuel Koch, Joerg Schulze, Uwe Hansen¶, Todd Ashwodt||, Douglas R. Keene**, William J. Brunken, Robert E. Burgeson||, Peter Bruckner¶, and Leena Bruckner-Tuderman¶¶

From the Department of Dermatology, University of Freiburg, 79104 Freiburg, Germany, ^||Cutaneous Biology Research Center, Massachusetts General Hospital/Harvard Medical School, Charlestown, Massachusetts 02129, Center for Biochemistry, Medical Faculty University of Cologne, 50931 Cologne, Germany, ^**Shriners Hospital for Children, Portland, Oregon 97201, Anatomy and Cell Biology, Departments of Neuroscience, and Ophthalmology, Tufts University School of Medicine, Boston, Massachusetts 02111, ^¶Department of Biochemistry, University of Muenster, 48129 Münster, Germany

Here we describe a novel specific component of tissue junctions, collagen XXII. It was first identified by screening an EST data base and subsequently expressed as a recombinant protein and characterized as an authentic tissue component. The COL22A1 gene on human chromosome 8q24.2 encodes a collagen that structurally belongs to the FACIT protein family (fibril-associated collagens with interrupted triple helices). Collagen XXII exhibits a striking restricted localization at tissue junctions such as the myotendinous junction in skeletal and heart muscle, the articular cartilage-synovial fluid junction, or the border between the anagen hair follicle and the dermis in the skin. It is deposited in the basement membrane zone of the myotendinous junction and the hair follicle and associated with the extrafibrillar matrix in cartilage. In situ hybridization of myotendinous junctions revealed that muscle cells produce collagen XXII, and functional tests demonstrated that collagen XXII acts as a cell adhesion ligand for skin epithelial cells and fibroblasts. This novel gene product, collagen XXII, is the first specific extracellular matrix protein present only at tissue junctions.

Received for publication, January 17, 2004 , and in revised form, March 8, 2004.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AF406780.

^* This work was supported in part by an award from the Alexander von Humboldt Foundation sponsored by the German Federal Ministry of Education and Research (to M. K.), the German Research Council, Deutsche Forschungsgemeinschaft Grants Nr. Br 1475/7-1/KO 2247/1-1 (to L. B.-T. and M. K.), SFB 492-A2 (to P. B.), and SFB 492-A3 (to L. B.-T.), Public Health Service Grant R01 NS39502 (to R. E. B. and W. J. B.), and a Shiseido award to the Cutaneous Biology Research Center Harvard Medical School (to R. E. 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.

Both authors contributed equally to this work.

^¶¶ To whom correspondence should be addressed: Dept. of Dermatology, University of Freiburg, Hauptstrasse 7, 79104 Freiburg, Germany. Tel.: 49-7612706716; Fax: 49-7612706936; E-mail: bruckner_tuderman{at}haut.ukl.uni-freiburg.de.

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