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J. Biol. Chem., Vol. 263, Issue 32, 17159-17166, 11, 1988
M Bernard, H Yoshioka, E Rodriguez, M Van der Rest, T Kimura, Y Ninomiya, BR Olsen and F Ramirez
We have isolated several overlapping cDNA clones encoding alpha 1(XI)
collagen chains from human and rat cDNA libraries. Together the human cDNAs
code for 335 uninterrupted Gly-X-Y triplets, and a 264-amino acid
C-propeptide, while the rat cDNAs cover the entire C-propeptide and about a
third of the triple-helical domain. Comparison of the human and rodent
nucleotide sequences showed a 95% sequence similarity. The identification
of the clones as alpha 1(XI) cDNAs was based on the complete identity
between the amino acid sequences of three human alpha 1(XI) cyanogen
bromide peptides and the cDNA-derived sequence. Examination of and the
cDNA-derived amino acid sequence showed a variety of structural features
characteristic of fibrillar-forming collagens. In addition, nucleotide
sequence analysis of a selected portion of the corresponding human gene
revealed the characteristic 54- base pair exon motif. We conclude therefore
that pro-alpha 1 (XI) collagen belongs to the group of fibrillar collagen
genes. We also suggest that the expression of this gene is not restricted
to cartilage, as previously thought, since the cDNA libraries from which
the clones were isolated, originated from both cartilagenous and
noncartilaginous tissues.
Cloning and sequencing of pro-alpha 1 (XI) collagen cDNA demonstrates that type XI belongs to the fibrillar class of collagens and reveals that the expression of the gene is not restricted to cartilagenous tissue
Department of Microbiology and Immunology, Morse Institute of Molecular Genetics, State University of New York, Brooklyn 11203.
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