Human and sheep growth-plate cartilage type X collagen synthesis and the influence of tissue storage

G. J. Gibson, K. T. Francki, J. J. Hopwood, B. K. Foster

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


Direct comparison of type X collagen synthesized by human sheep and chick growth-plate cartilage has shown that the human type X collagen is similar to the chick in both its molecular mass, containing component α-chains of 59 kDa with helical regions of 45 kDa and apparent absence of disulphide-stabilized aggregates, whereas the sheep type X collagen has slightly larger α-chains (63 kDa) accounted for by a longer helical region (49 kDa) that contains cystine residues essential for the formation of the high-mo]ecular-mass aggregates found with this species. Type X collagen from all three species showed heterogeneity in primary collagen structure as revealed by Staphylococcus aureus V8 proteinase-generated peptide maps. Collagen synthesis by growth-plate cartilage in culture particularly synthesis of type IX and X collagen was shown to be very sensitive to prior storage and suggests caution in thc interpretation of changes detected when examining collagen synthesis by growth plates in culture.

Original languageEnglish
Pages (from-to)513-520
Number of pages8
JournalBiochemical Journal
Issue number2
Publication statusPublished or Issued - 1991

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this