Matrix metalloproteinase-2 contributes to cancer cell migration on collagen.

作者: Lei Xu , Ricky Tong , David M. Cochran , Rakesh K. Jain

DOI: 10.1158/0008-5472.CAN-04-4313

关键词: FibronectinType I collagenCell cultureCancer cellBiochemistryMatrix metalloproteinaseCell migrationCell biologySignal transductionCollagen receptorBiology

摘要: Matrix metalloproteinases (MMP) are central to tissue penetration by cancer cells, as tumors expand and form metastases, but the mechanism which MMP-2 contributes cell migration is not well understood. In present experiments, both a broad-spectrum MMP inhibitor isolated collagen binding domain (CBD) from inhibited on native type I collagen. These results verified involvement of MMPs in general showed that MMP-2, specifically, involving interaction with To exclude potential overlapping effects MMP-9, additional experiments also contributed MMP-9-/- cells. investigate whether homologous CBD human fibronectin migration, we first fragmentation feature breast several fragments contained CBD. However, recombinant did alter This lack effect was explored competitive protein-protein assays, affinity for exceeds fibronectin. Furthermore, whereas gelatinolytic activities tumor extracts, such an inhibition characteristic corresponding domain. Together, our provide evidence important determinant behavior segment

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