TAILIEUCHUNG - Báo cáo khoa học: Collagen I regulates matrix metalloproteinase-2 activation in osteosarcoma cells independent of S100A4

This work investigates the effect of cell–collagen I interactions on the syn-thesis and activation of MMP-2, as well as synthesis of MT1-MMP and TIMP-1, by using anin vitro model with 3D fibrillar and 2D monomeric collagen. | ỊFEBS Journal Collagen I regulates matrix metalloproteinase-2 activation in osteosarcoma cells independent of S100A4 Renate Elenjord1 Jasmine B. Allen2 Harald T. Johansen3 Hanne Kildalsen1 Gunbj0rg Svineng2 Gunhild M. M landsmo1 4 Thrina Loennechen1 and Jan-Olof Winberg2 1 Department of Pharmacy University of Tromso Norway 2 Department of MedicalBiochemistry University of Tromso Norway 3 Schoolof Pharmacy University of Oslo Norway 4 Department of Tumor Biology The Norwegian Radium Hospital Oslo Norway Keywords collagen I extracellular matrix inhibitors of matrix metalloproteinases matrix metalloproteinases S100A4 Correspondence . Winberg Department of Medical Biochemistry Institute of MedicalBiology University of Tromso 9037 Tromso Norway Fax 47 776 45350 Tel 47 776 45488 E-mail janow@ Received 9 December 2008 revised 6 July 2009 accepted 20 July 2009 doi This work investigates the effect of cell-collagen I interactions on the synthesis and activation of MMP-2 as well as synthesis of MT1-MMP and TIMP-1 by using an in vitro model with 3D fibrillar and 2D monomeric collagen. In order to reveal whether the metastasis-associated protein S100A4 can influence the cell s response to the two forms of collagen osteosarcoma cell lines with high and low endogenous levels of S100A4 were used. Attachment of osteosarcoma cells to 3D fibrillar and 2D monomeric collagen resulted in opposite effects on MMP-2 activation. Attachment to 3D fibrillar collagen decreased activation of proMMP-2 with a corresponding reduction in MT1-MMP. By contrast attachment to monomeric collagen increased the amount of fully active MMP-2. This was caused by a reduction in TIMP-1 levels when cells were attached to monomeric 2D collagen. The effect of collagen on proMMP-2 activation was independent of endogenous S100A4 levels whereas synthesis of TIMP-1 was dependent on S100A4. When cells were attached to monomeric collagen cells with a high level of .

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