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Volumn 47, Issue 49, 2008, Pages 13016-13025

Benomyl and colchicine synergistically inhibit cell proliferation and mitosis: Evidence of distinct binding sites for these agents in tubulin

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFUNGAL AGENTS; CELL CULTURE; CELL PROLIFERATION; FUNGICIDES; LANTHANUM COMPOUNDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

EID: 57449091909     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801136q     Document Type: Article
Times cited : (41)

References (33)
  • 1
    • 0002770413 scopus 로고
    • Benzimidazole fungicides: Mechanism of action and biological impact
    • Davidse, L. C. (1986) Benzimidazole fungicides: Mechanism of action and biological impact. Annu. Rev. Phytopathol. 24, 43-65.
    • (1986) Annu. Rev. Phytopathol , vol.24 , pp. 43-65
    • Davidse, L.C.1
  • 2
    • 4243315437 scopus 로고
    • Fluorimetric determination of the fungicide benomyl after solvolysis
    • Garcia-Sánchez, F., and Aguilar-Gallardo, A. (1994) Fluorimetric determination of the fungicide benomyl after solvolysis. Mikrochim. Acta 116, 211-218.
    • (1994) Mikrochim. Acta , vol.116 , pp. 211-218
    • Garcia-Sánchez, F.1    Aguilar-Gallardo, A.2
  • 3
    • 0019826241 scopus 로고
    • Fate of benomyl and its degradation compound methyl 2-benzimidazolecarbamate on apple foliage
    • Chiba, M., and Veres, D. F. (1981) Fate of benomyl and its degradation compound methyl 2-benzimidazolecarbamate on apple foliage. J. Agric. Food Chem. 29, 588-590.
    • (1981) J. Agric. Food Chem , vol.29 , pp. 588-590
    • Chiba, M.1    Veres, D.F.2
  • 4
    • 0017602345 scopus 로고
    • Differential binding of methyl benzimidazol-2-yl carbamate to fungal tubulin as a mechanism of resistance to this antimitotic agent in mutant strains of Aspergillus nidulans
    • Davidse, L. C., and Flach, W. (1977) Differential binding of methyl benzimidazol-2-yl carbamate to fungal tubulin as a mechanism of resistance to this antimitotic agent in mutant strains of Aspergillus nidulans. J. Cell Biol. 72, 174-193.
    • (1977) J. Cell Biol , vol.72 , pp. 174-193
    • Davidse, L.C.1    Flach, W.2
  • 5
    • 2542603198 scopus 로고    scopus 로고
    • Antimitotic antifungal compound benomyl inhibits brain microtubule polymerization and dynamics and cancer cell proliferation at mitosis, by binding to a novel site in tubulin
    • Gupta, K., Bishop, J., Peck, A., Brown, J., Wilson, L., and Panda, D. (2004) Antimitotic antifungal compound benomyl inhibits brain microtubule polymerization and dynamics and cancer cell proliferation at mitosis, by binding to a novel site in tubulin. Biochemistry 43, 6645-6655.
    • (2004) Biochemistry , vol.43 , pp. 6645-6655
    • Gupta, K.1    Bishop, J.2    Peck, A.3    Brown, J.4    Wilson, L.5    Panda, D.6
  • 6
    • 33747394797 scopus 로고    scopus 로고
    • Suppression of microtubule dynamics by benomyl decreases tension across kinetochore pairs and induces apoptosis in cancer cells
    • Rathinasamy, K., and Panda, D. (2006) Suppression of microtubule dynamics by benomyl decreases tension across kinetochore pairs and induces apoptosis in cancer cells. FEBS J. 273, 4114-4128.
    • (2006) FEBS J , vol.273 , pp. 4114-4128
    • Rathinasamy, K.1    Panda, D.2
  • 7
    • 0019876086 scopus 로고
    • Purification of yeast tubulin by self-assembly in vitro
    • Kilmartin, J. V. (1981) Purification of yeast tubulin by self-assembly in vitro. Biochemistry 20, 3629-3633.
    • (1981) Biochemistry , vol.20 , pp. 3629-3633
    • Kilmartin, J.V.1
  • 8
    • 48849115866 scopus 로고    scopus 로고
    • Microtubule assembly dynamics: An attractive target for anticancer drugs
    • Singh, P., Rathinasamy, K., Mohan, R., and Panda, D. (2008) Microtubule assembly dynamics: An attractive target for anticancer drugs. IUBMB Life 60, 368-375.
    • (2008) IUBMB Life , vol.60 , pp. 368-375
    • Singh, P.1    Rathinasamy, K.2    Mohan, R.3    Panda, D.4
  • 9
    • 37449001322 scopus 로고    scopus 로고
    • How do microtubule-targeted drugs work? An overview
    • Jordan, M. A., and Kamath, K. (2007) How do microtubule-targeted drugs work? An overview. Curr. Cancer Drug Targets 7, 730-742.
    • (2007) Curr. Cancer Drug Targets , vol.7 , pp. 730-742
    • Jordan, M.A.1    Kamath, K.2
  • 10
    • 56549120027 scopus 로고    scopus 로고
    • Kinetic stabilization of microtubule dynamic instability by benomyl increases the nuclear transport of p53
    • doi: 10.1016/j.b-cp.2008.09.001
    • Rathinasamy, K., and Panda, D. (2008) Kinetic stabilization of microtubule dynamic instability by benomyl increases the nuclear transport of p53. Biochem. Pharmacol., doi: 10.1016/j.b-cp.2008.09.001.
    • (2008) Biochem. Pharmacol
    • Rathinasamy, K.1    Panda, D.2
  • 11
    • 0018162381 scopus 로고
    • Interaction of anthelmintic benzimidazoles and benzimidazole derivatives with bovine brain tubulin
    • Friedman, P. A., and Platzer, E. G. (1978) Interaction of anthelmintic benzimidazoles and benzimidazole derivatives with bovine brain tubulin. Biochim. Biophys. Acta 544, 605-614.
    • (1978) Biochim. Biophys. Acta , vol.544 , pp. 605-614
    • Friedman, P.A.1    Platzer, E.G.2
  • 12
    • 0019313409 scopus 로고
    • Interaction of anthelmintic benzimidazoles with Ascaris suum embryonic tubulin
    • Friedman, P. A., and Platzer, E. G. (1980) Interaction of anthelmintic benzimidazoles with Ascaris suum embryonic tubulin. Biochim. Biophys. Acta 630, 271-278.
    • (1980) Biochim. Biophys. Acta , vol.630 , pp. 271-278
    • Friedman, P.A.1    Platzer, E.G.2
  • 13
    • 0034518173 scopus 로고    scopus 로고
    • Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics
    • Downing, K. H. (2000) Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics. Annu. Rev. Cell Dev. Biol. 16, 89-111.
    • (2000) Annu. Rev. Cell Dev. Biol , vol.16 , pp. 89-111
    • Downing, K.H.1
  • 14
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectra
    • Mayer, M., and Meyer, B. (1999) Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectra. Angew. Chem., Int. Ed. 35, 1784-1788.
    • (1999) Angew. Chem., Int. Ed , vol.35 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 15
    • 22244469477 scopus 로고    scopus 로고
    • Kinetic suppression of microtubule dynamic instability by griseofulvin: Implications for its possible use in the treatment of cancer
    • Panda, D., Rathinasamy, K., Santra, M. K., and Wilson, L. (2005) Kinetic suppression of microtubule dynamic instability by griseofulvin: Implications for its possible use in the treatment of cancer. Proc. Natl. Acad. Sci. U.S.A. 102, 9878-9883.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 9878-9883
    • Panda, D.1    Rathinasamy, K.2    Santra, M.K.3    Wilson, L.4
  • 16
    • 0000994406 scopus 로고
    • Analysis of combined drug effects: A new look at a very old problem
    • Chou, T. C., and Talalay, P. (1983) Analysis of combined drug effects: A new look at a very old problem. Trends Pharmacol. Sci. 4, 450-454.
    • (1983) Trends Pharmacol. Sci , vol.4 , pp. 450-454
    • Chou, T.C.1    Talalay, P.2
  • 17
    • 0036847718 scopus 로고    scopus 로고
    • Silibinin strongly synergizes human prostate carcinoma DU145 cells to doxorubicin-induced growth Inhibition, G2-M arrest, and apoptosis
    • Tyagi, A. K., Singh, R. P., Agarwal, C., Chan, D. C., and Agarwal, R. (2002) Silibinin strongly synergizes human prostate carcinoma DU145 cells to doxorubicin-induced growth Inhibition, G2-M arrest, and apoptosis. Clin. Cancer Res. 8, 3512-3519.
    • (2002) Clin. Cancer Res , vol.8 , pp. 3512-3519
    • Tyagi, A.K.1    Singh, R.P.2    Agarwal, C.3    Chan, D.C.4    Agarwal, R.5
  • 18
    • 0021118703 scopus 로고
    • Quantitative analysis of dose-effect relationships: The combined effects of multiple drugs or enzyme inhibitors
    • Chou, T. C., and Talalay, P. (1984) Quantitative analysis of dose-effect relationships: The combined effects of multiple drugs or enzyme inhibitors. Adv. Enzyme Regul. 22, 27-55.
    • (1984) Adv. Enzyme Regul , vol.22 , pp. 27-55
    • Chou, T.C.1    Talalay, P.2
  • 19
    • 0345393105 scopus 로고    scopus 로고
    • Purification of brain tubulin through two cycles of polymerization-depolymerization in a high-molarity buffer
    • Castoldi, M., and Popov, A. V. (2003) Purification of brain tubulin through two cycles of polymerization-depolymerization in a high-molarity buffer. Protein Expression Purif. 32, 83-88.
    • (2003) Protein Expression Purif , vol.32 , pp. 83-88
    • Castoldi, M.1    Popov, A.V.2
  • 20
    • 0018170308 scopus 로고
    • Reversible dissociation of the αβ dimer of tubulin from bovine brain
    • Detrich, H. W., and Williams, R. C. (1978) Reversible dissociation of the αβ dimer of tubulin from bovine brain. Biochemistry 17, 3900-3917.
    • (1978) Biochemistry , vol.17 , pp. 3900-3917
    • Detrich, H.W.1    Williams, R.C.2
  • 21
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 22
    • 0016927744 scopus 로고
    • Kinetics and mechanisms of conversion of methyl 1-(butylcarbamoyl)-2-benzimidazolecarbamate (benomyl) to methyl 2-benzimidazolecarbamate (MBC)
    • Calmon, J. P., and Sayag, D. R. (1976) Kinetics and mechanisms of conversion of methyl 1-(butylcarbamoyl)-2-benzimidazolecarbamate (benomyl) to methyl 2-benzimidazolecarbamate (MBC). J. Agric. Food Chem. 24, 311-314.
    • (1976) J. Agric. Food Chem , vol.24 , pp. 311-314
    • Calmon, J.P.1    Sayag, D.R.2
  • 23
    • 1242314220 scopus 로고    scopus 로고
    • Assessing N,N′-dibutylurea (DBU) formation in soils after application of n-butylisocyanate and benlate fungicides
    • Sassman, S. A., Lee, L. S., Bischoff, M., and Turco, R. F. (2004) Assessing N,N′-dibutylurea (DBU) formation in soils after application of n-butylisocyanate and benlate fungicides. J. Agric. Food Chem. 52, 747-754.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 747-754
    • Sassman, S.A.1    Lee, L.S.2    Bischoff, M.3    Turco, R.F.4
  • 24
    • 0031062307 scopus 로고    scopus 로고
    • The role of the benomyl metabolite carbendazim in benomyl-induced testicular toxicity
    • Lim, J., and Miller, M. G. (1997) The role of the benomyl metabolite carbendazim in benomyl-induced testicular toxicity. Toxicol. Appl. Pharmacol. 142, 401-410.
    • (1997) Toxicol. Appl. Pharmacol , vol.142 , pp. 401-410
    • Lim, J.1    Miller, M.G.2
  • 25
    • 1642464774 scopus 로고    scopus 로고
    • A benzimidazole fungicide, benomyl, and its metabolite, carbendazim, induce aromatase activity in a human ovarian granulose-like tumor cell line (KGN)
    • Morinaga, H., Yanase, T., Nomura, M., Okabe, T., Goto, K., Harada, N., and Nawata, H. (2004) A benzimidazole fungicide, benomyl, and its metabolite, carbendazim, induce aromatase activity in a human ovarian granulose-like tumor cell line (KGN). Endocrinology 145, 1860-1869.
    • (2004) Endocrinology , vol.145 , pp. 1860-1869
    • Morinaga, H.1    Yanase, T.2    Nomura, M.3    Okabe, T.4    Goto, K.5    Harada, N.6    Nawata, H.7
  • 26
    • 0021235143 scopus 로고
    • Binding to tubulin of the colchicine analog 2-methoxy-5-(2′,3′, 4′-trimethoxyphenyl)tropone. Thermodynamic and kinetic aspects
    • Bane, S., Puett, D., Macdonald, T. L., and Williams, R. C., Jr. (1984) Binding to tubulin of the colchicine analog 2-methoxy-5-(2′,3′, 4′-trimethoxyphenyl)tropone. Thermodynamic and kinetic aspects. J. Biol. Chem. 259, 7391-7398.
    • (1984) J. Biol. Chem , vol.259 , pp. 7391-7398
    • Bane, S.1    Puett, D.2    Macdonald, T.L.3    Williams Jr., R.C.4
  • 27
    • 0032499648 scopus 로고    scopus 로고
    • Role of the colchicine ring A and its methoxy groups in the binding to tubulin and microtubule inhibition
    • Andreu, J. M., Perez-Ramirez, B., Gorbunoff, M. J., Ayala, D., and Timasheff, S. N. (1998) Role of the colchicine ring A and its methoxy groups in the binding to tubulin and microtubule inhibition. Biochemistry 37, 8356-8368.
    • (1998) Biochemistry , vol.37 , pp. 8356-8368
    • Andreu, J.M.1    Perez-Ramirez, B.2    Gorbunoff, M.J.3    Ayala, D.4    Timasheff, S.N.5
  • 28
    • 37249020371 scopus 로고    scopus 로고
    • Anti-mitotic activity of colchicine and the structural basis for its interaction with tubulin
    • Bhattacharyya, B., Panda, D., Gupta, S., and Banerjee, M. (2008) Anti-mitotic activity of colchicine and the structural basis for its interaction with tubulin. Med. Res. Rev. 28, 155-183.
    • (2008) Med. Res. Rev , vol.28 , pp. 155-183
    • Bhattacharyya, B.1    Panda, D.2    Gupta, S.3    Banerjee, M.4
  • 29
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
    • Ravelli, R. B. G., Gigant, B., Curmi, P. A., Jourdain, I., Lachkar, S., Sobel, A., and Knossow, M. (2004) Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 428, 198-202.
    • (2004) Nature , vol.428 , pp. 198-202
    • Ravelli, R.B.G.1    Gigant, B.2    Curmi, P.A.3    Jourdain, I.4    Lachkar, S.5    Sobel, A.6    Knossow, M.7
  • 30
    • 0019856315 scopus 로고    scopus 로고
    • Detrich, H. W., III, Williams, R. C., Jr., Macdonald, T. L., Wilson, L., and Puett, D. (1981) Changes in the circular dichroic spectrum of colchicine associated with its binding to tubulin. Biochemistry 20, 5999-6005.
    • Detrich, H. W., III, Williams, R. C., Jr., Macdonald, T. L., Wilson, L., and Puett, D. (1981) Changes in the circular dichroic spectrum of colchicine associated with its binding to tubulin. Biochemistry 20, 5999-6005.
  • 31
    • 0024502909 scopus 로고
    • The binding of isocolchicine to tubulin. Mechanisms of ligand association with tubulin
    • Hastie, S. B., Williams, R. C., Jr., Puett, D., and Macdonald, T. L. (1989) The binding of isocolchicine to tubulin. Mechanisms of ligand association with tubulin. J. Biol. Chem. 264, 6682-6688.
    • (1989) J. Biol. Chem , vol.264 , pp. 6682-6688
    • Hastie, S.B.1    Williams Jr., R.C.2    Puett, D.3    Macdonald, T.L.4
  • 32
    • 0024421424 scopus 로고
    • Spectroscopic and kinetic features of allocolchicine binding to tubulin
    • Hastie, S. B. (1989) Spectroscopic and kinetic features of allocolchicine binding to tubulin. Biochemistry 28, 7753-7760.
    • (1989) Biochemistry , vol.28 , pp. 7753-7760
    • Hastie, S.B.1
  • 33
    • 0026559290 scopus 로고
    • A single amino-acid substitution in the β-tubulin gene of Neurospora confers both carbendazim resistance and diethofencarb sensitivity
    • Fujimura, M., Oeda, K., Inoue, H., and Kato, T. (1992) A single amino-acid substitution in the β-tubulin gene of Neurospora confers both carbendazim resistance and diethofencarb sensitivity. Curr. Genet. 21, 399-404.
    • (1992) Curr. Genet , vol.21 , pp. 399-404
    • Fujimura, M.1    Oeda, K.2    Inoue, H.3    Kato, T.4


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