Coordinate action of membrane‐type matrix metalloproteinase‐1 (MT1‐MMP) and MMP‐2 enhances pericellular proteolysis and invasion
作者： Hiroshi Sato , Takahisa Takino
DOI: 10.1111/J.1349-7006.2010.01498.X
关键词:
摘要: Membrane-type matrix metalloproteinase-1 (MT1-MMP) mediates cleavage of not only MMP-2/gelatinase A for activation, but also a variety substrates including type I collagen (reviewed in Cancer Sci 2005; 96: 212-7). MMP-2 activation involves tissue inhibitor MMP (TIMP)-2 as bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity is regulated complex manner depending on TIMP-2 concentration. During invasive growth tumor cells matrix, initiates denaturation into gelatin, which subsequently digested further by adjacent to MT1-MMP. Coordinate action may facilitate pericellular proteolysis, enhance invasion/migration cell growth. Tetraspanins binding proteins regulate subcellular localization compartmentalization, leading efficient proteolysis coupled with cellular function.
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