Echistatin inhibits Lewis lung carcinoma cell-matrix adhesion in vitro and experimental metastasis in vivo.

Echistatin, a low molecular weight, RGD-containing protein isolated from the venom of Echis carinatus, inhibited Lewis lung carcinoma cell (3LL) adhesion to immobilized fibronectin and laminin. The inhibition was specific, noncytotoxic, dose-dependent and fully reversible. Echistatin showed a stronger activity in inhibiting cell adhesion to fibronectin rather than to laminin and it resulted about 3-fold more effective than kistrin, an other ROD-snake venom protein, in inhibiting 3LL cell attachment to both substrates. The ability of echistatin to modulate experimental metastasis formation in vivo was also evaluated. A 20% inhibition of the lung metastasis spread with respect to controls was observed when 3LL cells and echistatin were coinjected i.m. into male C57BL/6NCr1BR mice. When echistatin was administered i.p. 1 mu g/g of body weight/72 h x 4 doses into mice bearing Lewis lung carcinoma, it promoted only a 15% inhibition of tumor growth but inhibited by 45% lung metastasis formation. These results demonstrate that echistatin is able to inhibit metastasis attachment and spreading in experimental system in vivo independently by its effect on the primary tumor.
AuthorsD Spalleticernia, C Squillacioti, R Dellamorte, P Laccetti, N Staiano
JournalInternational journal of oncology (Int J Oncol) Vol. 11 Issue 4 Pg. 757-63 (Oct 1997) ISSN: 1019-6439 [Print] Greece
PMID21528271 (Publication Type: Journal Article)

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