Effects of the proteinase inhibitor tetra-p-amidinophenoxyneopentane on in vitro adhesion and invasiveness of tumor cells.

Some of the biological processes which enhance the metastatic capacity of tumor cells are associated with the activation of proteinases. In this paper we examined the effects of aromatic polyamidines on "in vitro" invasiveness of tumor cell lines. In addition to their antiproteinase activity, aromatic polyamidines exhibit antiproliferative activity toward tumor cell lines and inhibit expression of specific oncogenes. The results obtained show that the aromatic polyamidine TAPP-Br does not affect attachment, but inhibits the "in vitro" invasiveness of tumor cells cultured on a reconstituted basement membrane composed by laminin, type IV collagen, entactin, heparan sulphate proteoglycans. Our data suggest that this and related compounds should be further studied as experimental antitumor agents.