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Originally published In Press as doi:10.1074/jbc.M212889200 on May 23, 2003

J. Biol. Chem., Vol. 278, Issue 33, 31067-31077, August 15, 2003
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A Novel and Highly Conserved Collagen (pro{alpha}1(XXVII)) with a Unique Expression Pattern and Unusual Molecular Characteristics Establishes a New Clade within the Vertebrate Fibrillar Collagen Family*

Raymond P. Boot-Handford {ddagger} §, Danny S. Tuckwell {ddagger} ¶, Darren A. Plumb {ddagger} ||, Claire Farrington Rock {ddagger} and Richard Poulsom **

From the {ddagger}Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom and the **Histopathology Unit, Cancer Research UK, 44 Lincoln's Inn Fields, London WC2A 3PX, United Kingdom

The type XXVII collagen gene codes for a novel vertebrate fibrillar collagen that is highly conserved in man, mouse, and fish (Fugu rubripes). The pro{alpha}1(XXVII) chain has a domain structure similar to that of the type B clade chains ({alpha}1(V), {alpha}3(V), {alpha}1(XI), and {alpha}2(XI)). However, compared with other vertebrate fibrillar collagens (types I, II, III, V, and XI), type XXVII collagen has unusual molecular features such as no minor helical domain, a major helical domain that is short and interrupted, and a short chain selection sequence within the NC1 domain. Pro{alpha}1(XXVII) mRNA is 9 kb and expressed by chondrocytes but also by a variety of epithelial cell layers in developing tissues including stomach, lung, gonad, skin, cochlear, and tooth. By Western blotting, type XXVII antisera recognized multiple bands of 240–110 kDa in tissue extracts and collagenous bands of 150–140 kDa in the conditioned medium of the differentiating chondrogenic ATDC5 cell line. Phylogenetic analyses revealed that type XXVII, together with the closely related type XXIV collagen gene, form a new, third clade (type C) within the vertebrate fibrillar collagen family. Furthermore, the exon structure of the type XXVII collagen gene is similar to, but distinct from, those of the genes coding for the type A or B clade pro{alpha} chains.


Received for publication, December 18, 2002 , and in revised form, May 22, 2003.

Note Added in Proof—While this paper was under review, the paper by Pace et al. (25) on collagen XXVII was published.

* 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.

Supported by Biotechnology and Biological Sciences Research Council. Present address: Bioinformatics Group, F2G Limited, The Manchester Incubator Building, Grafton St., Manchester M13 9XX, UK.

|| Supported by a Medical Research Council Ph.D. studentship.

§ Recipient of a Wellcome Trust Research Leave Award. To whom correspondence should be addressed: Wellcome Trust Centre for Cell-Matrix Research, 2.205 Stopford, School of Biological Sciences, University of Manchester, Manchester M13 9PT, UK. Fax: 161-275-5082; E-mail: ray.boot-handford{at}man.ac.uk.


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