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 |
|---|---|
| Pages (from-to) | 216-218 |
| Number of pages | 3 |
| Journal | FEBS Letters |
| Volume | 352 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1994 Sep 26 |
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Keywords
- Matrix metalloproteinase
- Serine proteinase
- Tenascin
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases. / Imai, Kazushi; Kusakabe, Moriaki; Sakakura, Teruyo; Nakanishi, Isao; Okada, Yasunori.
In: FEBS Letters, Vol. 352, No. 2, 26.09.1994, p. 216-218.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases
AU - Imai, Kazushi
AU - Kusakabe, Moriaki
AU - Sakakura, Teruyo
AU - Nakanishi, Isao
AU - Okada, Yasunori
PY - 1994/9/26
Y1 - 1994/9/26
N2 - 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.
AB - 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.
KW - Matrix metalloproteinase
KW - Serine proteinase
KW - Tenascin
UR - http://www.scopus.com/inward/record.url?scp=0028124247&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028124247&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(94)00960-0
DO - 10.1016/0014-5793(94)00960-0
M3 - Article
C2 - 7523186
AN - SCOPUS:0028124247
VL - 352
SP - 216
EP - 218
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2
ER -