The developmentally regulated type X collagen gene contains a long open reading frame without introns

Y. Ninomiya, M. Gordon, M. van der Rest, T. Schmid, T. Linsenmayer, B. R. Olsen

Research output: Contribution to journalArticlepeer-review

122 Scopus citations


Type X collagen is a recently discovered product of hypertrophic chondrocytes that is localized to presumptive mineralization zones of hyaline cartilage. Thus, in the epiphyseal growth plate of long bones it is present only in the zone of hypertrophic chondrocytes and absent in the resting and rapidly growing cartilage and in bone. Type X collagen represents, therefore, a transient and developmentally regulated collagen which is synthesized by a subpopulation of chrondrocytes. We report here the isolation and characterization of cDNA and genomic clones specific for the chicken protein. The results demonstrate that the polypeptide chains of this collagen contain three distinct domains; a short non-collagenous, amino-terminal region, a collagenous domain of 460 amino acid residues, and a non-collagenous, carboxyl-terminal domain of 170 amino acid residues. The nucleotide sequence of the gene shows that these domains are encoded by a long open reading frame that is not interrupted by introns. Examination of the amino acid sequence derived from this nucleotide sequence reveals the presence of a hydrophobic segment localized 10 amino acid residues upstream from the translational stop codon. The length and sequence characteristics of this segment raise the intriguing possibility that Type X collagen polypeptides may contain a transmembrane segment.

Original languageEnglish (US)
Pages (from-to)5041-5050
Number of pages10
JournalJournal of Biological Chemistry
Issue number11
StatePublished - 1986
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Biochemistry
  • Cell Biology


Dive into the research topics of 'The developmentally regulated type X collagen gene contains a long open reading frame without introns'. Together they form a unique fingerprint.

Cite this