Collagen I regulates matrix metalloproteinase-2 activation in osteosarcoma cells independent of S100A4
作者： Renate Elenjord , Jasmine B. Allen , Harald T. Johansen , Hanne Kildalsen , Gunbjørg Svineng
DOI: 10.1111/J.1742-4658.2009.07223.X
关键词: Extracellular matrix 、 Biophysics 、 Cell 、 Endogeny 、 Cell culture 、 Enzyme activator 、 Matrix metalloproteinase 、 Collagen receptor 、 Biochemistry 、 Collagen, type I, alpha 1 、 Chemistry 、 Cell biology 、 Molecular biology
摘要: This work investigates the effect of cell-collagen I interactions on synthesis and activation MMP-2, as well MT1-MMP TIMP-1, by using an in vitro model with 3D fibrillar 2D monomeric collagen. In order to reveal whether metastasis-associated protein S100A4 can influence cell's response two forms collagen, osteosarcoma cell lines high low endogenous levels were used. Attachment cells collagen resulted opposite effects MMP-2 activation. decreased proMMP-2, a corresponding reduction MT1-MMP. By contrast, attachment increased amount fully active MMP-2. was caused TIMP-1 when attached The proMMP-2 independent levels, whereas dependent S100A4. When level showed greater than did those Taken together, this study shows that is affected between both form.
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