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Volumn 42, Issue 19, 1999, Pages 3800-3808

Novel farnesol and geranylgeraniol analogues: A potential new class of anticancer agents directed against protein prenylation

Author keywords

[No Author keywords available]

Indexed keywords

3 ALLYLFARNESOL; 3 ALLYLGERANYLGERANIOL; 3 ETHYLFARNESOL; 3 PHENYLFARNESOL; 3 VINYLFARNESOL; 3 VINYLGERANYLGERANIOL; ANTINEOPLASTIC AGENT; UNCLASSIFIED DRUG;

EID: 0033598364     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm9902786     Document Type: Article
Times cited : (57)

References (45)
  • 1
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F. L.; Casey, P. J. Protein Prenylation: Molecular Mechanisms and Functional Consequences. Annu. Rev. Biochem. 1996, 65, 241-269.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 2
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • Casey, P. J.; Seabra, M. C. Protein Prenyltransferases. J. Biol. Chem. 1996, 271, 5289-5292.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.C.2
  • 3
    • 0030865773 scopus 로고    scopus 로고
    • Ras farnesyltransferase: A new therapeutic target
    • (a) Leonard, D. M. Ras Farnesyltransferase: A New Therapeutic Target. J. Med. Chem. 1997, 40, 2971-2990.
    • (1997) J. Med. Chem. , vol.40 , pp. 2971-2990
    • Leonard, D.M.1
  • 4
    • 0030962347 scopus 로고    scopus 로고
    • The potential of farnesyltransferase inhibitors as cancer chemotherapeutics
    • (b) Gibbs, J. B.; Oliff, A. The Potential of Farnesyltransferase Inhibitors as Cancer Chemotherapeutics. Annu. Rev. Pharmacol. Toxicol. 1997, 37, 143-166.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 143-166
    • Gibbs, J.B.1    Oliff, A.2
  • 5
    • 0030749458 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors and cancer treatment: Targeting simply ras?
    • (c) Cox, A. D.; Der, C. J. Farnesyltransferase Inhibitors and Cancer Treatment: Targeting Simply Ras? Biochim. Biophys. Acta 1997, 1333, F51-F71.
    • (1997) Biochim. Biophys. Acta , vol.1333
    • Cox, A.D.1    Der, C.J.2
  • 6
    • 0033016719 scopus 로고    scopus 로고
    • Cell growth inhibition by farnesyltransferase inhibitors is mediated by gain of geranylgeranylated RhoB
    • Du, W.; Lebowitz, P. F.; Prendergast, G. C. Cell Growth Inhibition by Farnesyltransferase Inhibitors Is Mediated by Gain of Geranylgeranylated RhoB. Mol. Cell. Biol. 1999, 19, 1831-1840.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1831-1840
    • Du, W.1    Lebowitz, P.F.2    Prendergast, G.C.3
  • 7
    • 0032493641 scopus 로고    scopus 로고
    • A farnesyl-protein transferase inhibitor induces p21 expression and G1 block in p53 wild-type tumor cells
    • Sepp-Lorenzino, L.; Rosen, N. A farnesyl-protein transferase inhibitor induces p21 expression and G1 block in p53 wild-type tumor cells. J. Biol. Chem. 1998, 273, 20243-20251.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20243-20251
    • Sepp-Lorenzino, L.1    Rosen, N.2
  • 9
    • 0028884392 scopus 로고
    • A stereoselective palladium/copper-catalyzed route to isoprenoids: Synthesis and biological evaluation of 13-methylidenefarnesyl diphosphate
    • Gibbs, R. A.; Krishnan, U.; Dolence, J. M.; Poulter, C. D. A Stereoselective Palladium/Copper-Catalyzed Route to Isoprenoids: Synthesis and Biological Evaluation of 13-Methylidenefarnesyl Diphosphate. J. Org. Chem. 1995, 60, 7821-7829.
    • (1995) J. Org. Chem. , vol.60 , pp. 7821-7829
    • Gibbs, R.A.1    Krishnan, U.2    Dolence, J.M.3    Poulter, C.D.4
  • 13
    • 0031055466 scopus 로고    scopus 로고
    • Differential prenyl pyrophosphate binding to mammalian protein geranylgeranyltransferase i and protein farnesyltransferase and its consequence on the specificity of protein prenylation
    • Yokoyama, K.; Zimmerman, K.; Scholten, J.; Gelb, M. H. Differential Prenyl Pyrophosphate Binding to Mammalian Protein Geranylgeranyltransferase I and Protein Farnesyltransferase and Its Consequence on the Specificity of Protein Prenylation. J. Biol. Chem. 1997, 272, 3944-3952.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3944-3952
    • Yokoyama, K.1    Zimmerman, K.2    Scholten, J.3    Gelb, M.H.4
  • 14
    • 0029609580 scopus 로고
    • Yeast protein farnesyltransferase: Steady-state kinetic studies of substrate binding
    • Dolence, J. M.; Cassidy, P. B.; Mathis, J. R. Yeast Protein Farnesyltransferase: Steady-State Kinetic Studies of Substrate Binding. Biochemistry 1995, 34, 16687-16694.
    • (1995) Biochemistry , vol.34 , pp. 16687-16694
    • Dolence, J.M.1    Cassidy, P.B.2    Mathis, J.R.3
  • 15
    • 0030968859 scopus 로고    scopus 로고
    • Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo
    • (a) Rowell, C. A.; Kowalczyk, J. J.; Lewis, M. D.; Garcia, A. M. Direct Demonstration of Geranylgeranylation and Farnesylation of Ki-Ras in Vivo. J. Biol. Chem. 1997, 272, 14093-14097.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14093-14097
    • Rowell, C.A.1    Kowalczyk, J.J.2    Lewis, M.D.3    Garcia, A.M.4
  • 17
    • 0028810275 scopus 로고
    • Disruption of oncogenic K-Ras4B processing and signaling by a potent geranylgeranyltransferase I inhibitor
    • Lerner, E. C.; Qian, Y.; Hamilton, A. D.; Sebti, S. M. Disruption of Oncogenic K-Ras4B Processing and Signaling by a Potent Geranylgeranyltransferase I Inhibitor. J. Biol. Chem. 1995, 270, 26770-26773.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26770-26773
    • Lerner, E.C.1    Qian, Y.2    Hamilton, A.D.3    Sebti, S.M.4
  • 18
    • 0029938011 scopus 로고    scopus 로고
    • Geranylgeranyl diphosphate-based inhibitors of posttranslational geranylgeranylation of cellular proteins
    • Macchia, M.; Jannitti, N.; Gervasi, G.; Danesi, R. Geranylgeranyl Diphosphate-Based Inhibitors of Posttranslational Geranylgeranylation of Cellular Proteins. J. Med. Chem. 1996, 39, 1352-1356.
    • (1996) J. Med. Chem. , vol.39 , pp. 1352-1356
    • Macchia, M.1    Jannitti, N.2    Gervasi, G.3    Danesi, R.4
  • 19
    • 0033594336 scopus 로고    scopus 로고
    • Disruption of oncogenic K-Ras4B processing and signaling by a potent geranylgeranyltransferase I inhibitor
    • For a very recent report of a highly selective peptide-based GGTase I inhibitor, see: Vasudevan, A.; Qian, Y.; Vogt, A.; Blaskovich, M. A.; Ohkanda, J.; Sebti, S. M.; Hamilton, A. D. Disruption of Oncogenic K-Ras4B Processing and Signaling by a Potent Geranylgeranyltransferase I Inhibitor. J. Med. Chem. 1999, 42, 1333-1340.
    • (1999) J. Med. Chem. , vol.42 , pp. 1333-1340
    • Vasudevan, A.1    Qian, Y.2    Vogt, A.3    Blaskovich, M.A.4    Ohkanda, J.5    Sebti, S.M.6    Hamilton, A.D.7
  • 20
    • 0028909191 scopus 로고
    • Specific labeling of isoprenylated proteins: Application to study inhibitors of the posttranslational farnesylation and geranylgeranylation
    • Danesi, R.; McLellan, C. A.; Meyers, C. E. Specific Labeling of Isoprenylated Proteins: Application to Study Inhibitors of the Posttranslational Farnesylation and Geranylgeranylation. Biochem. Biophys. Res. Commun. 1995, 206, 637-643.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 637-643
    • Danesi, R.1    McLellan, C.A.2    Meyers, C.E.3
  • 21
    • 0031589542 scopus 로고    scopus 로고
    • Novel salvage pathway utilizing farnesol and geranylgeraniol for protein isoprenylation
    • Crick, D. C.; Andres, D. A.; Waechter, C. J. Novel Salvage Pathway Utilizing Farnesol and Geranylgeraniol for Protein Isoprenylation. Biochem. Biophys. Res. Commun. 1997, 237, 483-487.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 483-487
    • Crick, D.C.1    Andres, D.A.2    Waechter, C.J.3
  • 22
    • 0032524373 scopus 로고    scopus 로고
    • Phosphorylation of farnesol in rat liver microsomes: Properties of farnesol kinase and farnesyl phosphate kinase
    • Bentinger, M.; Grunler, J.; Peterson, E.; Swiezewska, E.; Dallner, G. Phosphorylation of Farnesol in Rat Liver Microsomes: Properties of Farnesol Kinase and Farnesyl Phosphate Kinase. Arch. Biochem. Biophys. 1998, 353, 191-198.
    • (1998) Arch. Biochem. Biophys. , vol.353 , pp. 191-198
    • Bentinger, M.1    Grunler, J.2    Peterson, E.3    Swiezewska, E.4    Dallner, G.5
  • 23
    • 0026659959 scopus 로고
    • Specific isoprenoid modification is required for function of normal, but not oncogenic, Ras protein
    • Cox, A. D.; Hisaka, M. M.; Buss, J. E.; Der, C. J. Specific Isoprenoid Modification is Required for Function of Normal, but Not Oncogenic, Ras Protein. Mol. Cell. Biol. 1992, 12, 2606-2615.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2606-2615
    • Cox, A.D.1    Hisaka, M.M.2    Buss, J.E.3    Der, C.J.4
  • 24
    • 0029097751 scopus 로고
    • Analysis of ras protein expression in mammalian cells
    • Cox, A. D.; Solski, P. A.; Jordan, J. D.; Der, C. J. Analysis of Ras Protein Expression in Mammalian Cells. Methods Enzymol. 1995, 255, 195-220.
    • (1995) Methods Enzymol. , vol.255 , pp. 195-220
    • Cox, A.D.1    Solski, P.A.2    Jordan, J.D.3    Der, C.J.4
  • 25
    • 0001437041 scopus 로고
    • Intramolecular fluorescence enhancement: A continuous assay of Ras farnesyl: Protein transferase
    • Pompliano, D. L.; Gomez, R. P.; Anthony, N. J. Intramolecular Fluorescence Enhancement: A Continuous Assay of Ras Farnesyl: Protein Transferase. J. Am. Chem. Soc. 1992, 114, 7945-7946.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7945-7946
    • Pompliano, D.L.1    Gomez, R.P.2    Anthony, N.J.3
  • 26
    • 0029028589 scopus 로고
    • Continuous fluorescence assay for protein prenyltransferases
    • Cassidy, P. B.; Dolence, J. M.; Poulter, C. D. Continuous Fluorescence Assay for Protein Prenyltransferases. Methods Enzymol. 1995, 250, 30-43.
    • (1995) Methods Enzymol. , vol.250 , pp. 30-43
    • Cassidy, P.B.1    Dolence, J.M.2    Poulter, C.D.3
  • 27
    • 0023678371 scopus 로고
    • Determination of isopentenyl diphosphate and farnesyl diphosphate in tissue samples with a comment on secondary regulation of polyisoprenoid biosynthesis
    • Bruenger, E.; Rilling, H. C. Determination of Isopentenyl Diphosphate and Farnesyl Diphosphate in Tissue Samples with a Comment on Secondary Regulation of Polyisoprenoid Biosynthesis. Anal. Biochem. 1988, 173, 321-327. Note that the only known biological role of GGPP in mammalian cells is as a substrate for GGTase I and GGTase II, and thus it is reasonable to propose that its intracellular levels could be very low.
    • (1988) Anal. Biochem. , vol.173 , pp. 321-327
    • Bruenger, E.1    Rilling, H.C.2
  • 28
    • 0032508533 scopus 로고    scopus 로고
    • Posttranscriptional regulation of endothelial nitric oxide synthase mRNA stability by Rho GTPase
    • Laufs, U.; Liao, J. K. Posttranscriptional Regulation of Endothelial Nitric Oxide Synthase mRNA Stability by Rho GTPase. J. Biol. Chem. 1998, 273, 24266-24271.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24266-24271
    • Laufs, U.1    Liao, J.K.2
  • 29
    • 0033548675 scopus 로고    scopus 로고
    • The geranylgeranyltransferase I inhibitor GGTI-298 induces hypophosphorylation of retinoblastoma and partner switching of cyclin-dependent kinase inhibitors
    • Sun, J.; Qian, Y.; Chen, Z.; Marfurt, J.; Hamilton, A. D.; Sebti, S. M. The Geranylgeranyltransferase I Inhibitor GGTI-298 Induces Hypophosphorylation of Retinoblastoma and Partner Switching of Cyclin-dependent Kinase Inhibitors. J. Biol. Chem. 1999, 274, 6930-6934.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6930-6934
    • Sun, J.1    Qian, Y.2    Chen, Z.3    Marfurt, J.4    Hamilton, A.D.5    Sebti, S.M.6
  • 30
    • 0028967667 scopus 로고
    • Inhibition of mammalian squalene synthetase activity by zaragozic acid A is a result of competitive inhibition followed by mechanism-based irreversible inactivation
    • Lindsey, S.; Harwood, H. J., Jr. Inhibition of Mammalian Squalene Synthetase Activity by Zaragozic Acid A is a Result of Competitive Inhibition Followed by Mechanism-based Irreversible Inactivation. J. Biol. Chem. 1995, 270, 9038-9096.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9038-9096
    • Lindsey, S.1    Harwood H.J., Jr.2
  • 31
    • 0026739520 scopus 로고
    • Substrate specificity of cis-prenyltransferase in rat liver microsomes
    • Ericsson, J.; Thelin, A.; Chojnacki, T.; Dallner, G. Substrate Specificity of cis-Prenyltransferase in Rat Liver Microsomes. J. Biol. Chem. 1992, 267, 19730-19735.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19730-19735
    • Ericsson, J.1    Thelin, A.2    Chojnacki, T.3    Dallner, G.4
  • 32
    • 0029143223 scopus 로고
    • Mechanism of farnesol cytotoxicity: Further evidence for the role of PKC-dependent signal transduction in farnesol-induced apoptotic cell death
    • Voziyan, P. A.; Haug, J. S.; Melnykovych, G. Mechanism of Farnesol Cytotoxicity: Further Evidence for the Role of PKC-Dependent Signal Transduction in Farnesol-Induced Apoptotic Cell Death. Biochem. Biophys. Res. Commun. 1995, 212, 479-486.
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 479-486
    • Voziyan, P.A.1    Haug, J.S.2    Melnykovych, G.3
  • 33
    • 0031056450 scopus 로고    scopus 로고
    • Inhibition of pancreatic cancer cell growth by the dietary isoprenoids farnesol and geraniol
    • Burke, Y. D.; Stark, M. J.; Roach, S. L.; Sen, S. E.; Crowell, P. L. Inhibition of Pancreatic Cancer Cell Growth by the Dietary Isoprenoids Farnesol and Geraniol. Lipids 1997, 32, 151-156.
    • (1997) Lipids , vol.32 , pp. 151-156
    • Burke, Y.D.1    Stark, M.J.2    Roach, S.L.3    Sen, S.E.4    Crowell, P.L.5
  • 34
    • 0032476029 scopus 로고    scopus 로고
    • Competitive inhibition of choline phosphotransferase by geranylgeraniol and farnesol inhibits phosphatidylcholine synthesis and induces apoptosis in human lung adenocarcinoma A549 cells
    • Miquel, K.; Pardines, A.; Terece, F.; Selmi, S.; Favre, G. Competitive Inhibition of Choline Phosphotransferase by Geranylgeraniol and Farnesol Inhibits Phosphatidylcholine Synthesis and Induces Apoptosis in Human Lung Adenocarcinoma A549 Cells. J. Biol. Chem. 1998, 273, 26179-26186.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26179-26186
    • Miquel, K.1    Pardines, A.2    Terece, F.3    Selmi, S.4    Favre, G.5
  • 35
    • 0028848171 scopus 로고
    • The farnesyl group of H-Ras facilitates the activation of a soluble upstream activator of mitogen-activated protein kinase
    • McGeady, P.; Kuroda, S.; Shimizu, K.; Takai, Y.; Gelb, M. H. The Farnesyl Group of H-Ras Facilitates the Activation of a Soluble Upstream Activator of Mitogen-activated Protein Kinase. J. Biol. Chem. 1995, 270, 26347-26351.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26347-26351
    • McGeady, P.1    Kuroda, S.2    Shimizu, K.3    Takai, Y.4    Gelb, M.H.5
  • 36
    • 0029919472 scopus 로고    scopus 로고
    • Posttranslational modification of H-Ras is required for activation of, but not for association with, B-Raf
    • Okada, T.; Masuda, T.; Shinkai, M.; Kariya, K.; Kataoka, T. Posttranslational Modification of H-Ras Is Required for Activation of, but Not for Association with, B-Raf. J. Biol. Chem. 1996, 277, 4671-4678.
    • (1996) J. Biol. Chem. , vol.277 , pp. 4671-4678
    • Okada, T.1    Masuda, T.2    Shinkai, M.3    Kariya, K.4    Kataoka, T.5
  • 37
    • 0032488969 scopus 로고    scopus 로고
    • Evidence for a high affinity, saturable, prenylation-dependent p21Ha-ras binding site in plasma membranes
    • Siddiqui, A. A.; Garland, J. R.; Dalton, M. B.; Sinensky, M. Evidence for a High Affinity, Saturable, Prenylation-dependent p21Ha-ras Binding Site in Plasma Membranes. J. Biol. Chem. 1998, 273, 3712-3717.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3712-3717
    • Siddiqui, A.A.1    Garland, J.R.2    Dalton, M.B.3    Sinensky, M.4
  • 38
    • 0030916369 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB
    • Lebowitz, P. F.; Casey, P. J.; Prendergast, G. C.; Thissen, J. A. Farnesyltransferase Inhibitors Alter the Prenylation and Growth-stimulating Function of RhoB. J. Biol. Chem. 1997, 272, 15591-15594.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15591-15594
    • Lebowitz, P.F.1    Casey, P.J.2    Prendergast, G.C.3    Thissen, J.A.4
  • 39
    • 0033523091 scopus 로고    scopus 로고
    • Role of isoprenoid lipids on the heterotrimeric G protein γ subunit in determining effector activation
    • Myung, C.-S.; Yasuda, H.; Liu, W. W.; Harden, T. K.; Garrison, J. C. Role of Isoprenoid Lipids on the Heterotrimeric G Protein γ Subunit in Determining Effector Activation. J. Biol. Chem. 1999, 274, 16595-16603.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16595-16603
    • Myung, C.-S.1    Yasuda, H.2    Liu, W.W.3    Harden, T.K.4    Garrison, J.C.5
  • 40
    • 0030564274 scopus 로고    scopus 로고
    • Isoprenylation/methylation of proteins enhances membrane association by a hydrophobic mechanism
    • Parish, C. A.; Rando, R. R. Isoprenylation/Methylation of Proteins Enhances Membrane Association by a Hydrophobic Mechanism. Biochemistry 1996, 35, 8473-8477.
    • (1996) Biochemistry , vol.35 , pp. 8473-8477
    • Parish, C.A.1    Rando, R.R.2
  • 41
    • 0030846849 scopus 로고    scopus 로고
    • Novel modifications to the farnesyl moiety of the a-factor lipopeptide pheromone from Saccharomyces cerevisiae - A role for isoprene modifications in ligand presentation
    • In this regard, we have recently found in a different system that 3-vinylfarnesylation of the yeast a-factor lipopeptide pheromone significantly alters its biological activity, relative to the native farnesylated a-factor: Dawe, A. L.; Becker, J. M.; Jiang, Y.; Naider, F.; Eummer, J. T.; Mu, Y. Q.; Gibbs, R. A. Novel Modifications to the Farnesyl Moiety of the a-Factor Lipopeptide Pheromone from Saccharomyces cerevisiae - a Role for Isoprene Modifications in Ligand Presentation. Biochemistry 1997, 36, 12036-12044.
    • (1997) Biochemistry , vol.36 , pp. 12036-12044
    • Dawe, A.L.1    Becker, J.M.2    Jiang, Y.3    Naider, F.4    Eummer, J.T.5    Mu, Y.Q.6    Gibbs, R.A.7
  • 43
    • 85047673338 scopus 로고
    • Coupling of isoprenoid triflates with organoboron nucleophiles: Synthesis of all-trans-geranylgeraniol
    • For a preliminary report on the synthesis of 9 and 10 via a slightly different method, see: Mu, Y. Q.; Gibbs, R. A. Coupling of Isoprenoid Triflates with Organoboron Nucleophiles: Synthesis of all-trans-Geranylgeraniol. Tetrahedron Lett. 1995, 36, 5669-5672.
    • (1995) Tetrahedron Lett. , vol.36 , pp. 5669-5672
    • Mu, Y.Q.1    Gibbs, R.A.2


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