Induction of apoptosis in leukemic cells by the reversible microtubule- disrupting agent 2-methoxy-5-(2',3',4'-trimethoxyphenyl)-2,4,6- cycloheptatrien-1-one: Protection by bcl-2 and bcl-x(L) and cell cycle arrest

Cancer Research

Volumn 60, Issue 10, 2000, Pages 2651-2659

  Gajate, Consuelo ^a,b   Barasoain, Isabel ^c   Andreu, José M ^c   Mollinedo, Faustino ^a,b,d  

^a Centro de Investigacion del Cancer   (Spain)

^b University of Valladolid   (Spain)

^c CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

^d UNIVERSITY OF SALAMANCA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

2 METHOXY 5 (2',3',4' TRIMETHOXYPHENYL) 2,4,6 CYCLOHEPTATRIEN 1 ONE; 2 METHOXY 5 [3 (3,4,5 TRIMETHOXYPHENYL)PROPIONAMIDO] 2,4,6 CYCLOHEPTATRIEN 1 ONE; CASPASE; COLCHICINE; COLCHICINE DERIVATIVE; LUMICOLCHICINE; PROTEIN BCL 2; PROTEIN BCL X; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; CANCER CELL DESTRUCTION; CANCER GROWTH; CELL CYCLE G2 PHASE; CELL PROTECTION; CONCENTRATION RESPONSE; CONTROLLED STUDY; DOSE TIME EFFECT RELATION; DRUG MECHANISM; DRUG POTENCY; DRUG STRUCTURE; ENZYME ACTIVATION; HUMAN; HUMAN CELL; LEUKEMIA CELL; MICROTUBULE ASSEMBLY; MITOSIS INHIBITION; PRIORITY JOURNAL; PROTEIN INDUCTION; SIGNAL TRANSDUCTION;

ANISOLES; APOPTOSIS; BCL-X PROTEIN; CASPASES; CELL CYCLE; CELL DIVISION; COLCHICINE; CYCLOHEPTANES; ENZYME ACTIVATION; ENZYME INDUCTION; HL-60 CELLS; HUMANS; JNK MITOGEN-ACTIVATED PROTEIN KINASES; MICROTUBULES; MITOGEN-ACTIVATED PROTEIN KINASES; MITOSIS; MODELS, CHEMICAL; PROTO-ONCOGENE PROTEINS C-BCL-2;

EID: 0034657265     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (43)

1. Jordan, M. A., and Wilson, L. Microtubule and actin filaments: dynamic targets for cancer chemotherapy. Curr. Opin. Cell Biol., 10: 123-130, 1998.
2. Manfredi, J. J., and Horwitz, S. B. Taxol: an antimitotic agent with a new mechanism of action. Pharmacol. Ther., 25: 83-125, 1984.
3. Rowinsky, E. K., and Donehower, R. C. Paclitaxel (Taxol). N. Engl. J. Med., 332: 1004-1014, 1995.
4. Bhalla, K., Ibrado, A. M., Tourkina, E., Tang, C. Q., Mahoney, M. E., and Huang, Y. Taxol induces internucleosomal DNA fragmentation associated with programmed cell death in human myeloid leukemia cells. Leukemia (Baltimore), 7: 563-568, 1993.
5. 1 phase by interference with spindle formation without affecting other microtubule functions during anaphase and telophase. Cancer Res., 54: 4355-4361, 1994.
6. Horwitz, S. B. Mechanism of action of Taxol. Trends Pharmacol. Sci., 13: 134-136, 1992.
7. Hastie, S. B. Interaction of colchicine with tubulin. Pharmacol. Ther., 51: 377-401, 1991.
8. Andreu, J. M., and Timasheff, S. N. Interaction of tubulin with single ring analogues of colchicine. Biochemistry, 21: 534-543, 1982.
9. Martin, S. J., and Cotter, T. G. Disruption of microtubules induces an endogenous suicide pathway in human leukaemia HL-60 cells. Cell Tissue Kinet., 23: 545-559, 1990.
10. Bonfoco, E., Ceccatelli, S., Manzo, L., and Nicotera, P. Colchicine induces apoptosis in cerebellar granule cells. Exp. Cell Res., 218: 189-200, 1995.
11. De Vincenzo, R., Scambia, G., Ferlini, C., Distefano, M., Filippini, P., Riva, A., Bombardelli, E., Pocar, D., Gelmi, M. L., Panici, P. B., and Mancuso, S. Antiproliferative activity of colchicine analogues on MDR-positive and MDR-negative human cancer cell lines. Anticancer Drug Des., 13: 19-33, 1998.
12. Fakih, M., Yagoda, A., Reploge, T., Lehr, J. E., and Pienta, K. J. Inhibition of prostate cancer growth by estramustine and colchicine. Prostate. 26: 310-315, 1995.
13. Sun, L., Hamel, E., Lin, C. M., Hastie, S. B., Pyluch, A., and Lee, K. H. Antitumor agents. 141. Synthesis and biological evaluation of novel thiocolchicine analogs: N-acyl, N-aroyl, and N-(substituted benzyl)deacetylthiocolchicines as potent cytotoxic and antimitotic compounds. J. Med. Chem., 36: 1474-1479, 1993.
14. Shearwin, K. E., and Timasheff, S. N. Effect of colchicine analogues or the dissociation of αβ tubulin into subunits: the locus of colchicine binding. Biochemistry, 33: 894-901, 1994.
15. Menendez, M., Rivas, G., Diaz, J. F., and Andreu, J. M. Control of the structural stability of the tubulin dimer by one high affinity bound magnesium ion at nucleotide N-site. J. Biol. Chem., 273: 167-176, 1998.
16. Perez-Ramirez, B., Andreu, J. M., Gorbunoff, M. J., and Timasheff, S. N. Stoichiometric and substoichiometric inhibition of tubulin self-assembly by colchicine analogues. Biochemistry, 35: 3277-3285, 1996.
17. Perez-Ramirez, B., Gorbunoff, M. J., and Timasheff, S. N. Linkages in tubulin-colchicine functions: the role of the ring C (C′) oxygens and ring B in the controls. Biochemistry, 37: 1646-1661, 1998.
18. Andreu, J. M., Perez-Ramirez, B., Gorbunoff, M. J., Ayala, D., and Timasheff, S. N. Role of the colchicine ring A and its methoxy groups in the binding to tubulin and microtubule inhibition. Biochemistry, 37: 8356-8368, 1998.
19. Fitzgerald, T. J. Molecular features of colchicine associated with antimitotic activity and inhibition of tubulin polymerization. Biochem. Pharmacol., 25: 1383-1387, 1976.
20. Andreu, J. M., Gorbunoff, M. J., Lee, J. C., and Timasheff, S. N. Interaction of tubulin with bifunctional colchicine analogues: an equilibrium study. Biochemistry, 23: 1742-1752, 1984.
21. Bane, S., Puetl, D., MacDonald, T. L., and Williams, R. C. Binding to tubulin of the colchicine analog 2-methoxy-5-(2′,3′,4′-trimelhoxyphenyl)tropone: thermodynamic and kinetic aspects. J. Biol. Chem., 259: 7391-7398, 1984.
22. Engelborghs, Y., and Fitzgerald, T. J. A fluorescence stopped flow study of the competition and displacement kinetics of podophyllotoxin and the colchicine analog 2-methoxy-5-(2′,3′,4′-trimethoxyphenyl)tropone on tubulin. J. Biol. Chem., 262: 5204-5209, 1987.
23. Díez, J. C., Avila, J., Nieto, J. M., and Andreu, J. M. Reversible inhibition of microtubules and cell growth by the bicyclic colchicine analogue MTC. Cell Motil. Cytoskeleton, 7: 178-186, 1987.
24. Mollinedo, F., Nieto, J. M., and Andreu, J. M. Cytoplasmic microtubules in human neutrophil degranulation: reversible inhibition by the colchicine analogue 2-methoxy-5-(2′,3′,4′-trimethoxyphenyl)-2,4,6-cycloheptatrien- 1-one. Mol. Pharmacol., 36: 547-555, 1989.
25. L. Cancer Res., 57: 1320-1328, 1997.
26. de Ines, C., Leynadier, D., Barasoain, I., Peyrot, V., Garcia, P., Briand, C., Rener, G. A., and Temple, C., Jr. Inhibition of microtubules and cell cycle arrest by a new 1-deaza-7,8-dihydropteridine antitumor drug, CI 980, and its chiral isomer, NSC 613863. Cancer Res., 54: 75-84, 1994.
27. Mollinedo, F., Santos-Beneit, A. M., and Gajate, C. The human leukemia cell line HL-60 as a cell culture model to study neutrophil functions and inflammatory cell responses. In: M. Clynes (ed.). Animal Cell Culture Techniques, pp. 264-297. Heidelberg, Germany: Springer-Verlag, 1998.
28. Pérez-Sala, D., Collado-Escobar, D., and Mollinedo, F. Intracellular alkalinization suppresses lovastatin-induced apoptosis in HL-60 cells through the inactivation of a pH-dependent endonuclease. J. Biol. Chem., 270: 6235-6242, 1995.
29. Mollinedo, F., Gajate, C., and Modolell, M. The ether lipid 1-octadecyl-2-methyl-rac-glycero-3-phosphocholine induces expression of fos and jun proto-oncogenes and activates AP-I transcription factor in human leukaemic cells. Biochem. J., 302: 325-329, 1994.
30. Mollinedo, F., and Naranjo, J. R. Uncoupled changes in the expression of the jun family members during myeloid cell differentiation. Eur. J. Biochem., 200: 483-486, 1991.
31. Hibi, M., Lin, A., Smeal, T., Minden, A., and Karin, M. Identification of an oncoprotein-and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes Dev., 7: 2135-2148, 1993.
32. 2-terminal kinase activation and c-Jun in the induction of apoptosis by the ether phospholipid 1-O-octadecyl-2-O-methyl-rac-glycero-3-phospnocholine. Mol. Pharmacol., 53: 602-612, 1998.
33. Ham, J., Babij, C., Whitfield, J., Pfarr, C. M., Lallemand, D., Yaniv, Y., and Rubin, L. L. A c-Jun dominant negative mutant protects sympathetic neurons against programmed cell death. Neuron, 14: 927-939, 1995.
34. Chen, Y-R., Wang, X., Templeton, D., Davis, R. J., and Tan, T-H. The role of c-Jun N-terminal kinase (JNK) in apoptosis induced by ultraviolet C and gamma radiation. Duration of JNK activation may determine cell death and proliferation. J. Biol. Chem., 271: 31929-31936, 1996.
35. Verheij, M., Bose, R., Lin, X. H., Yao, B., Jarvis, W. D., Grant, S., Birrer, M. J., Szabo, E., Zon, L. I., Kyriakis, J. M., Haimovitz-Friedman, A., Fuks, Z., and Kolesnick, R. N. Requirement for ceramide-initiated SAPK/JNK signaling in stress-induced apoptosis. Nature (Lond.), 380: 75-79, 1996.
36. Yang, D. D., Kuan, C. Y., Whitmarsh, A. J., Rincon, M., Zheng, T. S., Davis, R. J., Rakic, P., and Flavell, R. A. Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene. Nature (Lond.), 389: 865-870, 1997.
37. Kuan, C. Y., Yang, D. D., Samanta Roy, D. R., Davis, R. J., Rakic, P., and Flavell, R. A. The Jnk1 and Jnk2 protein kinases are required for regional specific apoptosis during early brain development. Neuron, 22: 667-676, 1999.
38. Tang, C., Willingham, M. C., Reed, J. C., Miyashita, T., Ray, S., Ponnathpur, V., Huang, Y., Mahoney, M. E., Bullock, G., and Bhalla, K. High levels of p26Bcl-2 oncoprotein retard Taxol-induced apoptosis in human pre-B leukemia cells. Leukemia (Baltimore), 8: 1960-1969, 1994.
39. L overexpression inhibits progression of molecular events leading to paclitaxel-induced apoptosis of human acute myeloid leukemia HL-60 cells. Cancer Res., 57: 1109-1115, 1997.
40. Adams, J. M., and Cory, S. The Bcl-2 protein family: arbiters of cell survival. Science (Washington DC), 281: 1322-1326, 1998.
41. Wang, T-H., Wang, H-S., Ichijo, H., Giannakakou, P., Foster, J. S., Fojo, T., and Wimalasena, J. Microtubule-interfering agents activate c-Jun N-terminal kinase/ stress-activated protein kinase through both ras and apoptosis signal-regulating kinase pathways. J. Biol. Chem., 273: 4928-4936, 1998.
42. Wolf, D., and Rotter, V. Major deletions in the gene encoding p53 tumor antigen cause lack of p53 expression in HL60 cells. Proc. Natl. Acad. Sci. USA, 82: 790-794, 1985.
43. 2/M arrest and apoptosis. Nat. Med., 2: 72-79, 1996.