Degradation of the cartilage collagen matrix associated with changes in chondrocytes in osteoarthrosis. Assessment by loss of background fluorescence and immunodetection of matrix components

J Orthop Res. 2001 Jan;19(1):33-42. doi: 10.1016/S0736-0266(00)00008-5.


Articular cartilage damage and eventual loss is the primary pathological change seen in osteoarthrosis (OA). In this study we have investigated the link between turnover of the collagen matrix and changes in chondrocytes. The background fluorescence of articular cartilage, as indicated by its emission spectrum and resistance to extraction was generated by the slow non-enzymic modification of the collagen matrix by advanced glycation end products (AGEs). Assessment of changes in background fluorescence in sections of articular cartilage provided a narrative of collagen degradation. Patients without OA pathology typically had a uniform strong background fluorescence throughout the depth of the cartilage. Cartilage from OA patients showed a range of changes in background fluorescence dependent on depth from the articular surface and proximity to overt lesions. Loss of background fluorescence was centered on chondrocytes, more extensive near the surface and associated with detection of the proteoglycan epitope 7D4. Expression of type X collagen was seen in articular cartilage in the region of the interface of with subchondral bone in most OA patients but was not associated with prominent, pericellular, loss of background fluorescence. These observations are consistent with progressive cartilage damage in OA, whereby collagen turnover and loss of surface integrity is associated with chondrocyte activity similar to that seen in immature articular cartilage.

MeSH terms

  • Aged
  • Cartilage, Articular / metabolism*
  • Chondrocytes / metabolism*
  • Collagen / metabolism*
  • Epitopes
  • Fluorescence
  • Glycation End Products, Advanced / metabolism
  • Humans
  • Immunohistochemistry
  • Middle Aged
  • Osteoarthritis / metabolism*
  • Proteoglycans / analysis
  • Proteoglycans / immunology


  • Epitopes
  • Glycation End Products, Advanced
  • Proteoglycans
  • Collagen