INTERACTION BETWEEN THE CARBOXYL-TERMINAL HEPARIN-BINDING DOMAIN OF FIBRONECTIN AND (-)-EPIGALLOCATECHIN GALLATE

We have previously reported that (-)-epigallocatechin gallate (EGCg) i nhibited lung carcinoma cell adhesion to fibronectin (FN) and demonstr ated its interaction with FN, In the present work, we studied the inte raction between thermolysin fragments of FN and EGCg, An amino acid se quence analysis of the fragment bound by EGCg-agarose provided its ide ntification as a carboxyl-terminal heparin-binding domain. Thus, the i nhibition of cancer cell adhesion to FN by EGCg is not caused by its d irect binding to the cell-binding domain containing an Arg-Gly-Asp-seq uence.