Imai K, Kusakabe M, Sakakura T, Nakanishi I, Okada Y
Department of Pathology, School of Medicine, Kanazawa University, Ishikawa, Japan.
FEBS Lett. 1994 Sep 26;352(2):216-8. doi: 10.1016/0014-5793(94)00960-0.
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.
