General description
A cell-permeable, prodrug form of the GGTase I inhibitor GGTI-297 (Cat. No. 345882). Inhibits the processing of Rap 1A (IC50 = 3 μM) but had no effect on the processing of H-Ras even at concentrations of 15 μM. Also arrests cells in the G0/G1 phase of the cell cycle, induces apoptosis and enhances nitric oxide synthase-2 induction by IL-1β.
A cell-permeable, prodrug form of the GGTase I inhibitor GGTI-297 (Cat. No. 345882). Inhibits the processing of Rap 1A (IC50 = 3 μM) but has no effect on the processing of H-Ras even at concentrations of 15 μM. Inhibits PDGF-receptor tyrosine phosphorylation. Also arrests cells in the G0/G1 phase of the cell cycle, induces apoptosis, and enhances iNOS induction by IL-1β.
A cell-permeable, prodrug form of the GGTase I inhibitor GGTI-297.
Biochem/physiol Actions
Target IC50:3 μM against processing of Rap 1A
Physical form
Supplied as a trifluoroacetate salt.
Preparation Note
Degas DMSO just prior to reconstitution
Following reconstitution, aliquot and freeze (-20°C). Unstable in solution; reconstitute just prior to use.
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
J D Finder et al.
The Journal of biological chemistry, 272(21), 13484-13488 (1997-05-23)
Recently, we have designed farnesyltransferase and geranylgeranyltransferase I inhibitors (FTI-277 and GGTI-298) that selectively block protein farnesylation and geranylgeranylation, respectively. In this study, we describe the opposing effects of these inhibitors on interleukin-1beta (IL-1beta)-stimulated induction of nitric-oxide synthase-2 (NOS-2) in
A Vogt et al.
The Journal of biological chemistry, 272(43), 27224-27229 (1997-10-27)
Recently we have shown that in fibroblasts (NIH 3T3 and Rat-1 cells) inhibition of protein geranylgeranylation leads to a G0/G1 arrest, whereas inhibition of protein farnesylation does not affect cell cycle distribution. Here we demonstrate that in human tumor cells
K Miquel et al.
Cancer research, 57(10), 1846-1850 (1997-05-15)
The mechanism by which the geranylgeranyltransferase I inhibitor GGTI-298 and the farnesyltransferase inhibitor FTI-277 inhibit human tumor growth is not known. Herein, we demonstrate that in the human lung adenocarcinoma A549 cells, GGTI-298 induced a G1-G0 block whereas FTI-277 induced
A Vogt et al.
Oncogene, 13(9), 1991-1999 (1996-11-07)
In order to assess the relative contributions of farnesylated and/or geranylgeranylated proteins on cell cycle progression from G1 to S phase we designed potent and selective farnesyltransferase (FTI-277) and geranylgeranyltransferase-I (GGTI-298) inhibitors. Flow cytometry studies showed that treatment of NIH3T3
T F McGuire et al.
The Journal of biological chemistry, 271(44), 27402-27407 (1996-11-01)
We have used specific inhibitors for farnesyltransferase (FTase) and geranylgeranyltransferase (GGTase) I as well as combinations of lovastatin with geranylgeraniol (GGOH) or farnesol (FOH) to investigate the role of protein prenylation in platelet-derived growth factor (PDGF)-induced PDGF receptor tyrosine phosphorylation.
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