Activation of prodeath Bcl-2 family proteins and mitochondrial apoptosis pathway by sanguinarine in immortalized human HaCaT keratinocytes

Clinical Cancer Research

Volumn 9, Issue 8, 2003, Pages 3176-3182

  Adhami, Vaqar Mustafa ^a   Aziz, Moammir Hasan ^a   Mukhtar, Hasan ^a   Ahmad, Nihal ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; ADENOSINE DIPHOSPHATE RIBOSE; CASPASE 3; CASPASE 7; CASPASE 8; CASPASE 9; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BID; SANGUINARINE;

APOPTOSIS; ARTICLE; ASSAY; CANCER CELL; CELL DEATH; CELL GROWTH; CELL IMMORTALIZATION; CELL PROLIFERATION; CELL VIABILITY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DRUG EFFECT; DRUG MECHANISM; ENZYME ACTIVITY; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN; HUMAN CELL; IMMUNOBLOTTING; KERATINOCYTE; MITOCHONDRION; PRIORITY JOURNAL; PROTEIN EXPRESSION; REGULATORY MECHANISM; SKIN CANCER; STATISTICAL SIGNIFICANCE;

ALKALOIDS; ANTIOXIDANTS; APOPTOSIS; BCL-2-ASSOCIATED X PROTEIN; BENZOPHENANTHRIDINES; CASPASE 3; CASPASE 7; CASPASE 8; CASPASE 9; CASPASES; CELL DIVISION; CELL LINE, TUMOR; CELL SURVIVAL; CYTOCHROMES C; CYTOSOL; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME INHIBITORS; ENZYME-LINKED IMMUNOSORBENT ASSAY; HUMANS; IMMUNOBLOTTING; ISOQUINOLINES; KERATINOCYTES; MITOCHONDRIA; MODELS, BIOLOGICAL; POLY(ADP-RIBOSE) POLYMERASES; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-BCL-2;

EID: 0043026772     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (36)

1. Jemal, A., Thomas, A., Murray, T., and Thun, M. Cancer statistics, 2002. CA - Cancer J. Clin., 52: 23-47, 2002.
2. Hail, N., Jr., and Lotan, R. Examining the role of mitochondrial respiration in vanilloid-induced apoptosis. J. Natl. Cancer Inst. (Bethesda), 94: 1281-1292, 2002.
3. Chaturvedi, M. M., Kumar, A., Darnay, B. G., Chainy, G. B. N., Agarwal, S., and Aggarwal, B. B. Sanguinarine (pseudochelerythrine) is a potent inhibitor of NF-κB activation, IκBα phosphorylation, and degradation. J. Biol. Chem., 272: 30129-30134, 1997.
4. Walterova, D., Ulrichova, J., Valka, I., Vicar, J., Vavreckova, C., Taborska, E., Harjrader, R. J., Meyer, D. L., Cerna, H., and Simanek, V. Benzo[c]phenanthridine alkaloids sanguinarine and chelerythrine: biological activities and dental care applications. Acta Univ. Palacki. Olomuc. Fac. Med., 139: 7-16, 1995.
5. Mandel, I. D. Chemotherapeutic agents for controlling plaque and gingivitis. J. Clin. Periodontol., 15: 488-498, 1988.
6. Mandel, I. D. Antimicrobial mouthrinses: overview and update. J. Am. Dent. Assoc., 125 (Suppl. 2): 2S-10S, 1994.
7. Ahmad, N., Gupta, S., Husain, M. M., Heiskanen, K. M., and Mukhtar, H. Differential antiproliferative and apoptotic response of sanguinarine for cancer cells versus normal cells. Clin. Cancer Res., 6: 1524-1528, 2000.
8. Makin, G. Targeting apoptosis in cancer chemotherapy. Expert. Opin. Ther. Targets, 6: 73-84, 2002.
9. Johnstone, R. W., Ruefli, A. A., and Lowe, S. W. Apoptosis: a link between cancer genetics and chemotherapy. Cell, 108: 153-164, 2002.
10. Ehlert, J. E., and Kubbutat, M. H. Apoptosis and its relevance in cancer therapy. Onkologie, 24: 433-440, 2001.
11. Penn, L. Z. Apoptosis modulators as cancer therapeutics. Curr. Opin. Investig. Drugs, 2: 684-692, 2001.
12. Sjostrom, J., and Bergh, J. How apoptosis is regulated, and what goes wrong in cancer. BMJ, 322: 1538-1539, 2001.
13. Herr, I., and Debatin, K. M. Cellular stress response and apoptosis in cancer therapy. Blood, 98: 2603-2614, 2001.
14. Petak, I., and Houghton, J. A. Shared pathways: death receptors and cytotoxic drugs in cancer therapy. Pathol. Oncol. Res., 7: 95-106, 2001.
15. Daniel, P. T. Dissecting the pathways to death. Leukemia (Baltimore), 14: 2035-2044, 2000.
16. Allen, R. T., Cluck, M. W., and Agrawal, D. K. Mechanisms controlling cellular suicide: role of Bcl-2 and caspases. Cell Mol. Life Sci., 54: 427-445, 1998.
17. Cory, S., and Adams, J. M. The Bcl2 family: regulators of the cellular life-or-death switch. Nat. Rev. Cancer, 2: 647-656, 2002.
18. Adams, J. M., and Cory, S. Life-or-death decisions by the Bcl-2 protein family. Trends Biochem. Sci., 26: 61-66, 2001.
19. Wang, X. The expanding role of mitochondria in apoptosis. Genes Dev., 15: 2922-2933, 2001.
20. Szewczyk, A., and Wojtczak, L. Mitochondria as a pharmacological target. Pharmacol. Rev., 54: 101-127, 2002.
21. Fusenig, N. E., and Boukamp, P. Multiple stages and genetic alterations in immortalization, malignant transformation, and tumor progression of human skin keratinocytes. Mol. Carcinog., 23: 144-158, 1998.
22. Budihardjo, I., Oliver, H., Lutter, M., Luo, X., and Wang, X. Biochemical pathways of caspase activation during apoptosis. Annu. Rev. Cell Dev. Biol., 15: 269-290, 1999.
23. Cecconi, F., and Gruss, P. Apaf1 in developmental apoptosis and cancer: how many ways to die? Cell Mol. Life Sci., 58: 1688-1697, 2001.
24. Hu, C. M., Cheng, H. W., Cheng, Y. W., and Kang, J. J. Induction of skeletal muscle contracture and calcium release from isolated sarcoplasmic reticulum vesicles by sanguinarine. Br. J. Pharmacol., 130: 299-306, 2000.
25. Sen, A., and Maiti, M. Interaction of sanguinarine with double stranded RNA structures. Indian J. Biochem. Biophys., 39: 106-112, 2002.
26. Munro, I. C., Delzell, E. S., Nestmann, E. R., and Lynch, B. S. Viadent usage and oral leukoplakia: a spurious association. Regul. Toxicol. Pharmacol., 30: 182-196, 1999.
27. Vaux, D. L., Cory, S., and Adams, J. M. Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells. Nature (Lond.), 335: 440-442, 1988.
28. Cory, S., Vaux D. L., Strasser, A., Harris, A. W., and Adams J. M. Insights from Bcl-2 and Myc: malignancy involves abrogation of apoptosis as well as sustained proliferation. Cancer Res., 59: 1685s-1692s, 1999.
29. Chinnaiyan, A. M., Orth, K., O'Rourke, K., Duan, H., Poirier, G. G., and Dixit, V. M. Molecular ordering of the cell death pathway, Bcl-2 and Bcl-xL function upstream of the CED-3-like apoptotic proteases. J. Biol. Chem., 271: 4573-4576, 1996.
30. Oltvai, Z. N., Milliman, C. L., and Korsmeyer, S. J. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell, 74: 609-619, 1993.
31. Srivastava, M., Ahmad, N., Gupta, S., and Mukhtar, H. Involvement of Bcl-2 and Bax in photodynamic therapy-mediated apoptosis. Anti-sense Bcl-2 oligonucleotide sensitizes RIF 1 cells to photodynamic therapy apoptosis. J. Biol. Chem., 276: 15481-15488, 2001.
32. Kuida, K. Caspase-9. Int. J. Biochem. Cell Biol., 32: 121-124, 2000.
33. Cain, K., Bratton, S. B., and Cohen, G. M. The Apaf-1 apoptosome: a large caspase-activating complex. Biochimie, 84: 203-214, 2002.
34. Weerasinghe, P., Hallock, S., Tang, S. C., and Liepins, A. Role of Bcl-2 family proteins and caspase-3 in sanguinarine-induced bimodal cell death. Cell Biol. Toxicol., 17: 371-381, 2001.
35. Weerasinghe, P., Hallock, S., Tang, S. C. and Liepins, A. Sanguinarine induces bimodal cell death in K562 but not in high Bcl-2-expressing JM1 cells. Pathol. Res. Pract., 197: 717-726, 2001.
36. Weerasinghe, P., Hallock, S., and Liepins, A. Bax, Bcl-2, and NF-κB expression in sanguinarine induced bimodal cell death. Exp. Mol. Pathol., 71: 89-98, 2001.