Membrane-type matrix metalloproteinases.
Matrix metalloproteinases (MMP) degrade components of extracellular matrix (ECM), and thereby regulate formation, remodeling and maintenance of tissue. Abnormal function of cell surface proteases associated with malignant tumors may contribute directly to the invasive and malignant nature of the cells. Among the MMP's associated with the tumor cell surface, gelatinase A is believed to be particularly important, since it degrades type IV collagen, and is activated in a tumor specific manner, correlating with tumor spread and poor prognosis. Activation of pro-gelatinase A is uniquely regulated by a cell-mediated mechanism. This study describes an in vitro model that mimics the cell-surface activation mechanism. The expression of MT-MMP could not be detected in normal epithelial cells, but can be seen in transformed epithelial carcinoma cells.
Seiki
M
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Department of Cancer Cell Research, Institute of Medical Science, University of Tokyo, Japan.
D000818:Animals; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000502:physiology; D018093:Gelatinases / Q000502:physiology; D006801:Humans; D053504:Matrix Metalloproteinases, Membrane-Associated; D008666:Metalloendopeptidases / Q000235:genetics / Q000502:physiology*; D009361:Neoplasm Invasiveness; D014158:Transcription, Genetic
D004792:Enzyme Precursors; D018093:Gelatinases; D053504:Matrix Metalloproteinases, Membrane-Associated; D008666:Metalloendopeptidases; C069860:progelatinase