Interaction between Amino Propeptides of Type XI Procollagen α1 Chains

Julia Thom Oxford, Joseph DeScala, Nick Morris, Kate Gregory, Ryan Medeck, Katey Irwin, Rex Oxford, Raquel Brown, Linda Mercer, Sorcha Cusack

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

Type XI collagen is a quantitatively minor yet essential constituent of the cartilage extracellular matrix. The amino propeptide of the α1 chain remains attached to the rest of the molecule for a longer period of time after synthesis than the other amino propeptides of type XI collagen and has been localized to the surface of thin collagen fibrils. Yeast two-hybrid system was used to demonstrate that a homodimer of α1(XI) amino propeptide (α1(XI)Npp) could form in vivo. Interaction was also confirmed using multi-angle laser light scattering, detecting an absolute weight average molar mass ranging from the size of a monomer to the size of a dimer (25,000-50,000 g/mol), respectively. Binding was shown to be saturable by ELISA. An interaction between recombinant α1(XI)Npp and the endogenous α1(XI)Npp was observed, and specificity for α1(XI)Npp but not α2(XI)Npp was demonstrated by co-precipitation. The interaction between the recombinant form of α1(XI)Npp and the endogenous α1(XI)Npp resulted in a stable association during the regeneration of cartilage extracellular matrix by fetal bovine chondrocytes maintained in pellet culture, generating a protein that migrated with an apparent molecular mass of 50-60 kDa on an SDS-polyacrylamide gel.

Original languageEnglish (US)
Pages (from-to)10939-10945
Number of pages7
JournalJournal of Biological Chemistry
Volume279
Issue number12
DOIs
StatePublished - Mar 19 2004
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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