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Originally published In Press as doi:10.1074/jbc.M604131200 on May 25, 2006
J. Biol. Chem., Vol. 281, Issue 30, 21546-21557, July 28, 2006
Expression of Type XXIII Collagen mRNA and Protein*
Manuel Koch ¶,
Guido Veit ,
Sigmar Stricker||,
Pinaki Bhatt**,
Stefanie Kutsch ,
Peihong Zhou**,
Elina Reinders ,
Rita A. Hahn**,
Rich Song**,
Robert E. Burgeson1,
Donald R. Gerecke**,
Stefan Mundlos|| , and
Marion K. Gordon**2
From the
Center for Biochemistry, Department of Dermatology, and ¶Center for Molecular Medicine Cologne, University of Cologne, Joseph-Stelzmann Strasse 52, 50931 Cologne, Germany, ||Development and Disease Group, Max Planck Institute for Molecular Genetics, 14195 Berlin, Germany,  Institute for Medical Genetics, University Medicine Charité, 13353 Berlin, Germany, and **Department of Pharmacology and Toxicology, Ernest Mario School of Pharmacy and the Environmental and Occupational Health Sciences Institute, Rutgers University, Piscataway, New Jersey 08854
Collagen XXIII is a member of the transmembranous subfamily of collagens containing a cytoplasmic domain, a membrane-spanning hydrophobic domain, and three extracellular triple helical collagenous domains interspersed with non-collagenous domains. We cloned mouse, chicken, and human 1(XXIII) collagen cDNAs and showed that this non-abundant collagen has a limited tissue distribution in non-tumor tissues. Lung, cornea, brain, skin, tendon, and kidney are the major sites of expression. In contrast, five transformed cell lines were tested for collagen XXIII expression, and all expressed the mRNA. In vivo the 1(XXIII) mRNA is found in mature and developing organs, the latter demonstrated using stages of embryonic chick cornea and mouse embryos. Polyclonal antibodies were generated in guinea pig and rabbit and showed that collagen XXIII has a transmembranous form and a shed form. Comparison of collagen XXIII with its closest relatives in the transmembranous subfamily of collagens, types XIII and XXV, which have the same number of triple helical and non-collagenous regions, showed that there is a discontinuity in the alignment of domains but that striking similarities remain despite this.
Received for publication, May 1, 2006
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY898961
[GenBank]
, AF410792
[GenBank]
, and AY876377
[GenBank]
.
* This work was supported by Deutsche Forschungsgemeinschaft Grant SFB 589 P1 (to M. K.), an award from the Alexander von Humboldt Foundation (to M. K.), the Federal Ministry of Education and Research in Germany (to M. K.), and Grant HL67708 (to D. R. G.), NIEHS Center Grant ES05022, and NEI Grant EY09056 (to MKG) from the National Institutes of Health. 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.
The on-line version of this article (available at http://www.jbc.org) contains supplemental material.
1 Emeritus of the Cutaneous Biology Research Center, Massachusetts General Hospital East, Harvard Medical School, Charlestown, MA 02129.
2 To whom correspondence should be addressed: Dept. of Pharmacology and Toxicology, Ernest Mario School of Pharmacy, Rutgers University, 170 Frelinghuysen Rd., Piscataway, NJ 08854. Tel.: 732-445-3751; Fax: 732-445-0119; E-mail: magordon{at}eohsi.rutgers.edu.

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Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
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