Interaction between the Carboxyl-terminal Heparin-binding Domain of Fibronectin and (−)-Epigallocatechin Gallate
- 1 January 1998
- journal article
- Published by Taylor & Francis in Bioscience, Biotechnology, and Biochemistry
- Vol. 62 (5) , 1031-1032
- https://doi.org/10.1271/bbb.62.1031
Abstract
We have previously reported that (-)-epigallocatechin gallate (EGCg) inhibited lung carcinoma cell adhesion to fibronectin (FN) and demonstrated its interaction with FN. In the present work, we studied the interaction between thermolysin fragments of FN and EGCg. An amino acid sequence analysis of the fragment bound by EGCg-agarose provided its identification as a carboxyl-terminal heparin-binding domain. Thus, the inhibition of cancer cell adhesion to FN by EGCg is not caused by its direct binding to the cell-binding domain containing an Arg-Gly-Asp-sequence.Keywords
This publication has 1 reference indexed in Scilit:
- Fibronectin Domains and ReceptorsPublished by Elsevier ,1989