Abstract
The degradation of type IX collagen, a minor collagen in cartilage, was examined by treatment with three different types of matrix metalloproteinases (MMPs) purified from the culture medium of rheumatoid synovial cells. Neither MMP-1 (collagenase) nor MMP-2 (so-called 'gelatinase') could digest type IX collagen, but MMP-3 (stromelysin) readily degraded it into smaller fragments. This suggests that MMP-3 may be responsible for the pathological degradation and/or normal turnover of type IX collagen.
| Original language | English |
|---|---|
| Pages (from-to) | 473-476 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 244 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1989 Feb 27 |
Keywords
- Degradation
- Extracellular matrix
- Proteinase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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Cite this
Okada, Y., Konomi, H., Yada, T., Kimata, K., & Nagase, H. (1989). Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells. FEBS Letters, 244(2), 473-476. https://doi.org/10.1016/0014-5793(89)80586-1