Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Ester doai
Patent
1993-10-28
1996-10-22
Goldberg, Jerome D.
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Ester doai
514722, A61K 3122, A61K 3108
Patent
active
055677290
ABSTRACT:
Farnesyl derivatives, particularly farnesyl acetate, are used to reduce the level of protein farnesylation in a mammalian host. The activity of proteins which require farnesylation for function is thereby reduced. The compounds may be administered to patients to reduce the overall level of ras protein activity, either alone or in conjunction with other drugs which act as competitive inhibitors of farnesyl protein transferase.
REFERENCES:
patent: 5185248 (1993-02-01), Barbacid et al.
Cox and Der, (1992) Current Opinions in Cell Biology 4:1008-1016. Protein Prenylation: more than just glue?.
G. James, et al. (1993) Science 260:1937-1942. Benzodiazopine peptidomimetics: potent inhibitors of ras farnesylation in animal cells.
N. Kohl, et al. (1993) Science 260:1934-1936. Selective inhibition of ras-dependent transformation by a farnesyltransferase inhibitor.
J. Gibbs, et al. (1993) Journal of Biological Chemistry 268:7617-7620. Selective inhibition of farnesyl-protein transferase blocks ras processing in vivo.
DeClue, et al. (1991) Cancer Research 51:712-717. Inhibition of cell growth by lovastatin is independent of ras function.
D. Pompliano, et al. (1992) Biochemistry 31:3800-3807. Steady-state kinetic mechanism of ras farnesyl:protein transferase.
Der and Cox (1991) Cancer Cells 3:331. Isoprenoid modification and plasma membrane association: critical factors for ras oncogenicity.
Cox, et al. (1992) Molecular and Cellular Biology 12:2606-2615. Specific isoprenoid modification is required for function of normal, but not oncogenic, ras protein.
Kato, et al. (1992) P.N.A.S. 89:6403-6407. Isporenoid addition to ras protein is the critical modification for its membrane association and transforming activity.
Sinensky and Lutz (1992) BioEssays 14:25-31. The prenylation of proteins.
Bradfute David L.
Meigs Thomas E.
Simoni Robert D.
Bradfute David L.
Goldberg Jerome D.
Meigs Thomas E.
Rowland Bertram I.
Sherwood Pamela J.
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