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J. Biol. Chem., Vol. 276, Issue 25, 23120-23126, June 22, 2001
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From the Chick cDNA clones for a new member of the FACIT
(fibril-associated collagens with interrupted triple helices) subfamily
have been isolated and sequenced. The collagen chain encoded by these cDNAs was assigned the next consecutive number, making it the The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF312825.
1(XX) Collagen, a New Member of the Collagen Subfamily,
Fibril-associated Collagens with Interrupted Triple
Helices*
,,
Cutaneous Biology Research Center,
Massachusetts General Hospital East, Harvard Medical School,
Charlestown, Massachusetts 02129, the § School of Nursing,
University of Pennsylvania, Philadelphia, Pennsylvania 19104, and the
¶ Department of Pharmacology and Toxicology, School of Pharmacy
and Environmental and Occupational Health Sciences Institute, Rutgers
University, Piscataway, New Jersey 08854
1(XX) collagen chain. Assignment of type XX collagen to the FACIT family was based on sequence similarities to types XII and XIV collagen. Type XX collagen mRNA is not abundant in the chick
embryo. It is most prevalent in corneal epithelium. It is also
detectable by reverse transcription polymerase chain reaction in
embryonic skin, sternal cartilage, and tendon, but is barely detectable in calvaria, notochord, or neural retina at select stages of
development, suggesting that it is not expressed in these tissues. The
cDNA predicts that the 1(XX) collagen polypeptide is smaller
than the short forms of collagen XII and XIV. A polyclonal antibody against a synthetic 1(XX) peptide reacts with polypeptide bands of
185, 170, and 135 kDa by Western blot analysis. From its similarity to
types XII and XIV collagen, type XX is expected to bind to collagen
fibrils, projecting the amino-terminal domains away from the fibrillar
surface. The projecting NC 3 domains are predicted to
be about half the length of those of collagen XIV.
*
This study was supported in part by National Institutes of
Health Grant EY09056 (to M. K. G.) and by the Cutaneous Biology Research Center, Massachusetts General Hospital, which receives a
research grant from Shisiedo Co., Ltd., Japan.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.
To whom correspondence should be addressed: Dept. of
Pharmacology and Toxicology, EOHSI, School of Pharmacy, Rutgers
University, 170 Frelinghuysen Rd., Piscataway, NJ 08854. Tel.:
732-445-3751; Fax: 732-445-0119; E-mail:
magordon@eohsi.rutgers.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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