Rhodostomin inhibits the transforming growth factor-beta 1-enhanced adhesion activity of ROS 17/2.8 osteosarcoma cells

We have investigated the effect of transforming growth factor-beta 1 (TGF-b eta 1) on the in vitro adhesion activity of the rat osteosarcoma cell lines (ROS 17/2.8) to extracellular matrix substrata, including fibronectin, typ e I and IV collagen, as well as laminin. The interaction of Arg-Gly-Asp (RG D) and rhodostomin, an RGD containing snake venom, with TGF-beta 1 on the c ell adhesion was also evaluated. The results showed that incubation with va rious concentration of TGF-beta 1 (1-15 ng/ml) significantly increased the adhesion activity (1.4 to 2.5 folds) of ROS 17/2.8 to fibronectin and type I collagen (p<0.01), whereas the adhesion activity to laminin and type IV c ollagen was slightly elevated (1.1 to 1.5 folds). The peak effect of TGF-be ta 1 on the cell adhesion occurred after pretreatment of ROS 17/2.8 with TG F-beta 1 for 6 hours. Treatment with Arg-Gly-Asp-Ser (RGDS) and rhodostomin effectively suppressed the TGF-beta 1-enhanced adhesion activity to fibron ectin and type I collagen. This study demonstrated that the up-regulated ce ll adhesion activity of ROS 17/2.8 cells by the TGF-beta 1 can be inhibited by the rhodostomin. (C) 2000 Tohoku University Medical Press.