The 45 kDa collagen-binding fragment of fibronectin induces matrix metalloproteinase-13 synthesis by chondrocytes and aggrecan degradation by aggrecanases.

@article{Stanton2002The4K,
  title={The 45 kDa collagen-binding fragment of fibronectin induces matrix metalloproteinase-13 synthesis by chondrocytes and aggrecan degradation by aggrecanases.},
  author={H. Stanton and L. Ung and A. Fosang},
  journal={The Biochemical journal},
  year={2002},
  volume={364 Pt 1},
  pages={
          181-90
        }
}
  • H. Stanton, L. Ung, A. Fosang
  • Published 2002
  • Medicine, Biology
  • The Biochemical journal
  • Fragments of fibronectin occur naturally in vivo and are increased in the synovial fluid of arthritis patients. We have studied the 45 kDa fragment (Fn-f 45), representing the N-terminal collagen-binding domain of fibronectin, for its ability to modulate the expression of metalloproteinases by porcine articular chondrocytes in vitro. We report that stimulation of cultured chondrocytes, or cartilage explants, with Fn-f 45 increased the levels of matrix metalloproteinase-13 (MMP-13; collagenase-3… CONTINUE READING
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    28

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