EC Number |
Application |
Reference |
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2.5.1.59 | medicine |
enzyme GGTase-I is abundantly expressed in human primary glioma tissues. Inhibition or downregulation of GGTase-I markedly decreases the proliferation of glioma cells and induces their apoptosis, while overexpression of GGTase-I promotes cell growth in vitro. Inactivation of GGTase-I eliminates geranylgeranylation of RhoA and Rac1, prevents them from targeting to the plasma membrane, and inhibits Rac1 activity. Overexpressing wild type or constitutively active Rac1 stimulates glioma cell growth, similar to the effect of GGTase-I overexpression. Overexpressing dominant-negative Rac1 or Rac1 with the prenylation site deleted or mutated abrogates GGTase-I-induced proliferation in glioma cells |
723013 |
2.5.1.59 | medicine |
inhibitor GGTI-298 induces apoptosis and augments tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in human lung cancer cells. GGTI-298 induces DR4 and DR5 expression and reduces c-FLIP levels. Enforced c-FLIP expression or DR5 knockdown attenuates apoptosis induced by GGTI-298 and TRAIL combination. DR4 knockdown sensitizes cancer cells to GGTI298/TRAIL-induced apoptosis. The combination of GGTI-298 and TRAIL is more effective than each single agent in decreasing the levels of IkappaBalpha and p-Akt |
705670 |
2.5.1.59 | medicine |
potential target in anticancer drug research |
672535 |
2.5.1.59 | medicine |
S-prenylated enzymes are interesting targets for noncytotoxic anticancer agents |
636548 |
2.5.1.59 | medicine |
target for anti-cancer drugs |
675067 |
2.5.1.59 | molecular biology |
the GGTase-I variants with altered substrate specificity can serve as tools for studying GGTase-I substrate selectivity and the effects of prenylation pathway modifications on specific proteins |
737695 |
2.5.1.59 | pharmacology |
the enzyme is a promising therapeutic target for the treatment of various Ras-induced cancers and several other kinds of diseases |
738097 |