Specific reaction of α,β-unsaturated carbonyl compounds such as 6-shogaol with sulfhydryl groups in tubulin leading to microtubule damage

FEBS Letters

Volumn 582, Issue 23-24, 2008, Pages 3531-3536

  Ishiguro, Kazuhiro ^a   Ando, Takafumi ^b   Watanabe, Osamu ^b   Goto, Hidemi ^b  

^a NAGOYA UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b NAGOYA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

, Unsaturated carbonyl compound; Cancer; Ginger; Microtubule; Tubulin

Indexed keywords

6 SHOGAOL; ALPHA,BETA CARBONYL DERIVATIVE; CARBONYL DERIVATIVE; CYSTEINE PROTEINASE; DITHIOTHREITOL; GLUTATHIONE; MERCAPTOETHANOL; PAPAIN; SHOGAOL; THIOL DERIVATIVE; TUBULIN; UNCLASSIFIED DRUG;

ARTICLE; CELL VIABILITY; CONTROLLED STUDY; DRUG MECHANISM; DRUG STRUCTURE; HUMAN; HUMAN CELL; MICROTUBULE; PRIORITY JOURNAL;

CATECHOLS; CELL LINE; CELL LINE, TUMOR; CYSTEINE; FATTY ALCOHOLS; HUMANS; MICROTUBULES; MOLECULAR STRUCTURE; TUBULIN;

ZINGIBER OFFICINALE;

EID: 53049095924     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.09.027     Document Type: Article

References (29)

1. Caviston J.P., and Holzbaur E.L. Microtubule motors at the intersection of trafficking and transport. Trend Cell Biol. 16 (2006) 530-537
2. Mollinedo F., and Gajate C. Microtubules, microtubule-interfering agents and apoptosis. Apoptosis 8 (2003) 413-450
3. Galluzzi L., Maiuri M.C., Vitale I., Zischka H., Castedo M., Zitvogel L., and Kroemer G. Cell death modalities: classification and pathophysiological implications. Cell Death Differ. 14 (2007) 1237-1243
4. Waterman-Storer C.M., and Salmon E. Positive feedback interactions between microtubule and actin dynamics during cell motility. Curr. Opin. Cell Biol. 11 (1999) 61-67
5. Bijman M.N., Van Nieuw Amerongen G.P., Laurens N., van Hinsbergh V.W., and Boven E. Microtubule-targeting agents inhibit angiogenesis at subtoxic concentrations, a process associated with inhibition of Rac1 and Cdc42 activity and changes in the endothelial cytoskeleton. Mol. Cancer Ther. 5 (2006) 2348-2357
6. Altmann K.H., and Gertsch J. Anticancer drugs from nature-natural products as a unique source of new microtubule-stabilizing agents. Nat. Prod. Rep. 24 (2007) 327-357
7. Bent S., and Ko R. Commonly used herbal medicines in the United States: a review. Am. J. Med. 116 (2004) 478-485
8. Bhattarai S., Tran V.H., and Duke C.C. Stability of [6]-gingerol and [6]-shogaol in simulated gastric and intestinal fluids. J. Pharm. Biomed. Anal. 45 (2007) 648-653
9. Ishiguro K., Ando T., Maeda O., Ohmiya N., Niwa Y., Kadomatsu K., and Goto H. Ginger ingredients reduce viability of gastric cancer cells via distinct mechanisms. Biochem. Biophys. Res. Commun. 362 (2007) 218-223
10. D'Amato R.J., Lin C.M., Flynn E., Folkman J., and Hamel E. 2-Methoxyestradiol, an endogenous mammalian metabolite, inhibits tubulin polymerization by interacting at the colchicine site. Proc. Natl. Acad. Sci. USA 91 (1994) 3964-3968
11. Ellman G.L. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82 (1959) 70-77
12. Roychowdhury M., Sarkar N., Manna T., Bhattacharyya S., Sarkar T., Basusarkar P., Roy S., and Bhattacharyya B. Sulfhydryls of tubulin. A probe to detect conformational changes of tubulin. Eur. J. Biochem. 267 (2000) 3469-3476
13. Britto P.J., Knipling L., McPhie P., and Wolff J. Thiol-disulphide interchange in tubulin: kinetics and the effect on polymerization. Biochem. J. 389 (2005) 549-558
14. Lipnick R.L. Outliers: their origin and use in the classification of molecular mechanisms of toxicity. Sci. Total Environ. 109-110 (1991) 131-153
15. Luduena R.F., and Roach M.C. Tubulin sulfhydryl groups as probes and targets for antimitotic and antimicrotubule agents. Pharmacol. Ther. 49 (1991) 133-152
16. Olivero A., Miglietta A., Gadoni E., and Gabriel L. 4-Hydroxynonenal interacts with tubulin by reacting with its functional -SH groups. Cell Biochem. Funct. 8 (1990) 99-105
17. Cushman M., Mohanakrishnan A.K., Hollingshead M., and Hamel E. The effect of exchanging various substituents at the 2-position of 2-methoxyestradiol on cytotoxicity in human cancer cell cultures and inhibition of tubulin polymerization. J. Med. Chem. 45 (2002) 4748-4754
18. Edsall A.B., Mohanakrishnan A.K., Yang D., Fanwick P.E., Hamel E., Hanson A.D., Agoston G.E., and Cushman M. Effects of altering the electronics of 2-methoxyestradiol on cell proliferation, on cytotoxicity in human cancer cell cultures, and on tubulin polymerization. J. Med. Chem. 47 (2004) 5126-5139
19. Nguyen T.L., McGrath C., Hermone A.R., Burnett J.C., Zaharevitz D.W., Day B.W., Wipf P., Hamel E., and Gussio R. A common pharmacophore for a diverse set of colchicine site inhibitors using a structure-based approach. J. Med. Chem. 48 (2005) 6107-6116
20. Kim do Y., Kim K.H., Kim N.D., Lee K.Y., Han C.K., Yoon J.H., Moon S.K., Lee S.S., and Seong B.L. Design and biological evaluation of novel tubulin inhibitors as antimitotic agents using a pharmacophore binding model with tubulin. J. Med. Chem. 49 (2006) 5664-5670
21. Lawrence N.J., Patterson R.P., Ooi L.L., Cook D., and Ducki S. Effects of alpha-substitutions on structure and biological activity of anticancer chalcones. Bioorg. Med. Chem. Lett. 16 (2006) 5844-5848
22. Kingston D.G., Bane S., and Snyder J.P. The taxol pharmacophore and the T-taxol bridging principle. Cell Cycle 4 (2005) 279-289
23. Cragg G.M., and Newman D.J. A tale of two tumor targets: topoisomerase I and tubulin. The Wall and Wani contribution to cancer chemotherapy. J. Nat. Prod. 67 (2004) 232-244
24. Netto L.E., de Oliveira M.A., Monteiro G., Demasi A.P., Cussiol J.R., Discola K.F., Demasi M., Silva G.M., Alves S.V., Faria V.G., and Horta B.B. Reactive cysteine in proteins: protein folding, antioxidant defense, redox signaling and more. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 146 (2007) 180-193
25. Xian M., Chen X., Liu Z., Wang K., and Wang P.G. Inhibition of papain by S-nitrosothiols. Formation of mixed disulfides. J. Biol. Chem. 275 (2000) 20467-20473
26. Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
27. Wu G., Fang Y.Z., Yang S., Lupton J.R., and Turner N.D. Glutathione metabolism and its implications for health. J. Nutr. 134 (2004) 489-492
28. Gupta S., Banerjee M., Poddar A., Banerjee A., Basu G., Roy D., and Bhattacharyya B. Biphasic kinetics of the colchicine-tubulin interaction: role of amino acids surrounding the A ring of bound colchicine molecule. Biochemistry 44 (2005) 10181-10188
29. Snyder J.P., Nettles J.H., Cornett B., Downing K.H., and Nogales E. The binding conformation of Taxol in beta-tubulin: a model based on electron crystallographic density. Proc. Natl. Acad. Sci. USA 98 (2001) 5312-5316