Cleavage of cartilage oligomeric matrix protein (thrombospondin-5) by matrix metalloproteinases and a disintegrin and metalloproteinase with thrombospondin motifs.

@article{Dickinson2003CleavageOC,
  title={Cleavage of cartilage oligomeric matrix protein (thrombospondin-5) by matrix metalloproteinases and a disintegrin and metalloproteinase with thrombospondin motifs.},
  author={Sally C. Dickinson and Mireille N Vankemmelbeke and David John Buttle and Krisztina Rosenberg and Dick Heineg{\aa}rd and Anthony P Hollander},
  journal={Matrix biology : journal of the International Society for Matrix Biology},
  year={2003},
  volume={22 3},
  pages={
          267-78
        }
}
Cartilage oligomeric matrix protein (COMP) is a pentameric glycoprotein present in cartilage, tendon and ligament. Fragments of the molecule are present in the diseased cartilage, synovial fluid and serum of patients with knee injuries, osteoarthritis and rheumatoid arthritis. Although COMP is a substrate for several matrix metalloproteinases (MMPs), the enzymes responsible for COMP degradation in vivo have yet to be identified. In this study we utilised well-established bovine cartilage… CONTINUE READING

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