Abstract
The degradation of tenascin purified from human melanoma cells was examined by treatment with matrix metalloproteinases (MMPs) and serine proteinases. Among eight different types of proteinases examined, MMP-1, -3, and -7, cathepsin G and leukocyte elastase could digest tenascin, but MMP-2, MMP-9 and thrombin did not. This suggests that tenascin may be readily catabolized by extracellular matrix-degrading proteinases found in the pathophysiological conditions.
Original language | English |
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Pages (from-to) | 216-218 |
Number of pages | 3 |
Journal | FEBS Letters |
Volume | 352 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1994 Sep 26 |
Externally published | Yes |
Keywords
- Matrix metalloproteinase
- Serine proteinase
- Tenascin
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology