Identification and immunolocalization of type X collagen at the ligament-bone interface

Christopher Niyibizi, Camilla Sagarriga Visconti, Gary Gibson, Karl Kavalkovich

Research output: Contribution to journalArticle

71 Scopus citations

Abstract

In some ligaments, ligamentous collagen fibrils attach to bone by first passing through non-mineralized and mineralized fibrocartilage present at the ligament-bone interface. To understand better the function of these fibrocartilages, collagens present at the femoral insertion of the bovine medial collateral ligament were isolated and characterized. Types II and IX collagens were identified in pepsin digests of the tissue in addition to type X collagen originally thought to be associated with the cartilages undergoing endochondral bone formation. Presence of type X collagen was confirmed by immunoblotting and by immunofluorescence localization using laser confocal microscopy. Type X collagen was localized predominantly in the mineralized zone of the ligament insertion. These data indicate that type X collagen may play a role in ligament attachment to bone.

Original languageEnglish (US)
Pages (from-to)584-589
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume222
Issue number2
DOIs
StatePublished - May 15 1996

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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