Interaction between the carboxyl-terminal heparin-binding domain of fibronectin and (-)-epigallocatechin gallate.
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.
Sazuka
M
M
School of Food and Nutritional Sciences, University of Shizuoka, Japan.
Isemura
M
M
Isemura
S
S
D000970:Antineoplastic Agents / Q000494:pharmacology*; D002392:Catechin / Q000031:analogs & derivatives* / Q000494:pharmacology; D002448:Cell Adhesion / Q000187:drug effects; D005353:Fibronectins / Q000187:drug effects* / Q000378:metabolism; D006801:Humans; D008175:Lung Neoplasms / Q000188:drug therapy / Q000378:metabolism
D000970:Antineoplastic Agents; D005353:Fibronectins; D002392:Catechin; C045651:epigallocatechin gallate