Cloning of a cDNA for a new member of the class of fibril-asssociated collagens with interrupted triple helices

M. K. Gordon, P. Castagnola, B. Dublet, T. F. Linsenmayer, M. Van der Rest, R. Mayne, B. R. Olsen

Research output: Contribution to journalArticlepeer-review

Abstract

cDNA from embryonic chick skin has been isolated and characterized which encodes a novel member of the FACIT (fibril-associated collagen with interrupted triple helices) group whose other known members are collagen types IX and XII. Nucleotide sequence analysis of the cDNA, combined with characterization of a pepsin-resistant fragment of the protein from embryonic chick skin, demonstrates that the collagen chain is more closely related to the chain of type XII collagen than to those of type IX. It is most similar to a collagen, type XIV, recently identified in bovine skin. It is possible, therefore, that the cDNA codes for a chain of chicken type XIV collagen. From the additional data on molecular structure obtained by sequencing the cDNA, the FACIT family appears to consist of at least two classes of molecules: one of which contains the three chains of type IX collagen, and a second which includes the chains of collagen types XII and XIV.

Original languageEnglish
Pages (from-to)333-338
Number of pages6
JournalEuropean Journal of Biochemistry
Volume201
Issue number2
Publication statusPublished - 1991

ASJC Scopus subject areas

  • Biochemistry

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