Farnesyltransferase is one of the three members of the family of prenyltransferases that catalyzes the formation of a thio-ether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the farnesyl protein. In general, substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. The farnesyltransferase inhibitors, such as LB 42708 (Axon 1794), induce growth arrest and apoptosis in various human cancer cells by inhibiting the posttranslational activation of Ras. As a result, they suppress the release of vascular endothelial growth factor (VEGF) from tumor cells. Subsequently LB 42708 can suppress angiogenesis in vitro and in vivo by blocking the mitogen-activated protein kinase kinase/extracellular signal-regulated kinase/p38 mitogen-activated protein kinase (MAPK) and phosphatidylinositol 3-kinase (PI3K)/Akt/endothelial nitric-oxide synthase pathways in endothelial cells without altering FAK/Src activation[1].