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
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
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
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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 -