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Animal studies have shown that tea and tea components have anti-cancer activities. Green tea and black tea catechin compounds such as (–)-epigallocatechin gallate (EGCG) and theaflavin have been investigated intensively to reveal the molecular basis for their anti-tumor activities. Adhesive interaction between tumor cells and extracellular matrix proteins such as fibronectin, laminin, and collagens is deeply involved in tumor growth, invasion, and metastasis. These extracellular proteins comprise the endothelial basement membrane, and interruption of tumor cell adhesion may be effective in the prevention of bloodborne metastasis. Interactions between tumor cells and these extracellular proteins are regulated by integrins, a family of heterodimeric transmembrane receptors. In tumor cells, integrins have been shown to mediate the organization of the extracellular matrix, adhesion to extracellular matrix proteins, and cell motility. We have reported that the binding of EGCG to Fas, presumably on the cell surface, triggers Fasmediated apoptosis in tumor cells and that EGCG impairs the adhesion of cancer cells to extracellular matrix proteins such as fibronectin and laminin by binding to fibronectin and laminin. However, it is not clear whether the binding of EGCG to tumor cells causes an impairment of cell adhesion. In the present study, we examined whether or not EGCG inhibits the adhesion of fibrosarcoma HT-1080 cells to fibronectin by binding to the fibronectin receptor, integrin β1. Involvement of Impaired Interaction with 1 Integrin in Epigallocatechin Gallate-Mediated Inhibition of Fibrosarcoma HT-1080 Cell Adhesion to Fibronectin

journal of health science

Involvement of Impaired Interaction with .BETA.1 Integrin in Epigallocatechin Gallate-Mediated Inhibition of Fibrosarcoma HT-1080 Cell Adhesion to Fibronectin