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PMID: 6328487 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Synthesis and characterization of cDNA encoding a cartilage-specific short collagen.

Ninomiya Y, Olsen BR

Abstract

Hyaline cartilage contains a unique set of collagenous proteins. Type II collagen is the most abundant, constituting about 85% of the total cartilage collagen. In addition, several minor collagenous components have been described. To study the structure and developmental regulation of chondrocyte-specific collagens, we have constructed a cDNA library from embryonic chicken sternal cartilage mRNA. We report here on the isolation and characterization of a 3200 base-pair-long cDNA that codes for a collagenous polypeptide of unusual structure in that the total length of the molecule is only about half of pro alpha 1(II) collagen chains. The mRNA for this polypeptide is considerably smaller than mRNA encoding the pro alpha chains of interstitial collagens. In addition, the peptide encoded by the cDNA appears to contain at least three domains with triple-helical potential separated by short, noncollagenous peptides. Between the three collagenous domains are several cysteinyl residues.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cartilage/metabolism Chick Embryo Cloning, Molecular Collagen/genetics DNA/metabolism DNA Restriction Enzymes DNA, Recombinant/analysis Extraembryonic Membranes/metabolism Molecular Weight
Chemicals
DNA, Recombinant Collagen DNA DNA Restriction Enzymes
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ninomiya Y
Olsen B R
References (30)
30 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1984-05-00
Pages
3014-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC345211
Subset
IM
Grants
NIADDK NIH HHS · AM 21471 · United States
Databases
GENBANK
K01702
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