A forskolin derivative, FSK88, induces apoptosis in human gastric cancer BGC823 cells through caspase activation involving regulation of Bcl-2 family gene expression, dissipation of mitochondrial membrane potential and cytochrome c release

Cell Biology International

Volumn 30, Issue 11, 2006, Pages 940-946

  Li, Zhonghai ^a,b   Wang, Jingze ^a  

^a INSTITUTE OF ZOOLOGY   (China)

^b CHINESE NATIONAL HUMAN GENOME CENTER AT SHANGHAI   (China)

Author keywords

Apoptosis; Bcl 2; Caspases; Cytochrome c; FSK88

Indexed keywords

ANTINEOPLASTIC AGENT; BENZYLOXYCARBONYLASPARTYLGLUTAMYLVALYLASPARTYL FLUOROMETHYL KETONE; CASPASE 3; CASPASE 3 INHIBITOR; CYTOCHROME C; FORSKOLIN DERIVATIVE; FSK 88; PROTEIN BAD; PROTEIN BAX; PROTEIN BCL 2; UNCLASSIFIED DRUG;

ANTINEOPLASTIC ACTIVITY; APOPTOSIS; ARTICLE; CANCER CELL CULTURE; CELL SECRETION; CONTROLLED STUDY; DOSE RESPONSE; DOWN REGULATION; ENZYME ACTIVATION; GENE CONTROL; GENE EXPRESSION; HUMAN; HUMAN CELL; MEMBRANE POTENTIAL; MITOCHONDRIAL MEMBRANE; NUCLEOTIDE SEQUENCE; STOMACH CANCER; UPREGULATION;

APOPTOSIS; CASPASE 3; CELL SURVIVAL; CYTOCHROMES C; DNA FRAGMENTATION; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME ACTIVATION; ENZYME INHIBITORS; FORSKOLIN; GENE EXPRESSION REGULATION, NEOPLASTIC; HL-60 CELLS; HUMANS; MEMBRANE POTENTIALS; MITOCHONDRIA; MITOCHONDRIAL MEMBRANES; PROTO-ONCOGENE PROTEINS C-BCL-2; RNA, MESSENGER; STOMACH NEOPLASMS; TIME FACTORS;

PLECTRANTHUS BARBATUS;

EID: 33750332011     PISSN: 10656995     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cellbi.2006.06.015     Document Type: Article

References (40)

1. Agarwal K.C., and Parks Jr. R.E. Forskolin: a potential antimetastatic agent. Int J Cancer 32 (1983) 801-804
2. Bamias A., and Pavlidis N. Systemic chemotherapy in gastric cancer: where do we stand today?. Oncologist 3 (1998) 171-177
3. Chao D.T., and Stanley J. Bcl-2 family: regulators of cell death. Annu Rev Immunol 16 (1998) 395-419
4. Emaus R.K., Grunwald R., and Lemasters J.J. Rhodamine 123 as a probe of transmembrane potential in isolated rat-liver mitochondria: spectral and metabolic properties. Biochim Biophys Acta 850 3 (1986) 436-448
5. Ferreira C.G., Epping M., Kruyt F.A.E., and Giaccone G. Apoptosis: target of cancer therapy. Clin Cancer Res 8 (2002) 2024-2034
6. Feschenko M.S., Stevenson E., Nairn A.C., and Sweadner K.J. A novel cAMP-stimulated pathway in protein phosphatase 2A activation. J Pharmacol Exp Ther 302 (2002) 111-118
7. Green G.R., and Reed J.C. Mitochondria and apoptosis. Science 281 (1998) 1309-1312
8. Gutzkow K.B., Naderi S., and Blomhoff H.K. Forskolin-mediated G1 arrest in acute lymphoblastic leukaemia cells: phosphorylated pRB sequesters E2Fs. J Cell Sci 115 (2002) 1073-1082
9. Hampton M.B., and Orrenius S. Dual regulation of caspase activity by hydrogen peroxide: implications for apoptosis. FEBS Lett 414 (1997) 552-556
10. Hengartner M.O. The biochemistry of apoptosis. Nature 407 (2000) 770-776
11. Hohenberger P., and Gretschel S. Gastric cancer. Lancet 362 (2003) 305-315
12. Kasibhatlal S., and Tseng B. Why target apoptosis in cancer treatment?. Mol Cancer Ther 2 (2003) 573-580
13. Kluck R.M., Wetzel E.B., Green D.R., and Newmeyer D. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275 (1997) 1132-1136
14. Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmed M., Alnemri E.S., et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91 (1997) 479-489
15. Lowe S.W., and Lin A.W. Apoptosis in cancer. Carcinogenesis 21 (2000) 485-495
16. Lu W.L., Pan K.F., Zhang L., Lin D.X., Miao X.P., and You W.C. Genetic polymorphisms of interleukin (IL)-1B, IL-1RN, IL-8, IL-10 and tumor necrosis factor and risk of gastric cancer in a Chinese population. Carcinogenesis 26 3 (2005) 631-636
17. Marchetti P., Castedo M., and Susin S.A. Mitochondrial permeability transition is central coordinating event of apoptosis. J Exp Med 184 (1996) 1155-1160
18. Michael C., Victoria D.G.M., Mari N., Guo W., Stanley K., Scott A.A., et al. Mitochondria primed by death signals determines cellular addiction to antiapoptotic Bcl-2 family members. Cancer Cell 9 5 (2006) 351-365
19. Moon E.Y., and Lerner A. PDE4 inhibitors activate a mitochondrial apoptotic pathway in chronic lymphocytic leukemia cells that is regulated by protein phosphatase 2A. Blood 101 (2003) 4122-4130
20. Mosmann T. Rapid colorimetric assay for cellular growth and survivals: application to proliferation and cytotoxicity assays. J Immunol Methods 65 (1983) 55-63
21. Narita M., Shimizu S., Ito T., Chittenden T., Lutz R.J., Matsuda H., et al. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc Natl Acad Sci USA 95 (1998) 14681-14686
22. Neviani P., Santhanam R., Trotta R., Notari M., Blaser B.W., Liu S., et al. The tumor suppressor PP2A is functionally inactivated in blast crisis CML through the inhibitory activity of the BCR/ABL regulated SET protein. Cancer Cell 8 (2005) 355-368
23. Ortiz M.A., Lopez-Hernandez F.J., Bayon Y., Pfahl M., and Piedrafita F.J. Retinoid-related molecules induce cytochrome c release and apoptosis through activation of c-Jun NH2-terminal kinase/p38 mitogen-activated protein kinases. Cancer Res 61 (2001) 8504-8512
24. Palmeira C.M., Moreno A.J.M., Madeira V.M.C., and Wallace K.B. Continuous monitoring of mitochondrial membrane potential in hepatocyte cell suspensions. J Pharmacol Toxicol Methods 35 1 (1996) 35-43
25. Reed J.C. Cytochrome c: can't live with it-can't live without it. Cell 91 (1997) 559-562
26. Reed J.C. Bcl-2 family proteins. Oncogene 17 (1998) 3225-3236
27. Rosse T., Olivier R., Monney L., Rager M., Conus S., Fellay I., et al. Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c. Nature 391 (1998) 496-499
28. Schendel S.L., Xie Z., Montal M.O., Matsuyama S., Montal M., and Reed J. Channel formation by antiapoptotic protein Bcl-2. Proc Natl Acad Sci USA 94 (1997) 5113-5118
29. Slee E.A., Harte M.T., Kluck R.M., Wolf B.B., Casiano C.A., Newmeyer D.D., et al. Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8 and -10 in a caspase-9-dependent manner. J Cell Biol 144 (1999) 281-292
30. Taetle R., and Li-en S. Further studies on mechanisms of abnormal prostaglandin response by chronic myelogenous leukaemia granulocyte/macrophage progenitors. Leuk Res 8 (1984) 833-842
31. Tamm I., Dorken B., and Hartmann G. Antisense therapy in oncology: new hope for an old idea?. Lancet 358 (2001) 489-497
32. Tamm I., Schriever F., and Dorken B. Apoptosis: implications of basic research for clinical oncology. Lancet Oncol 2 (2001) 33-42
33. Tanabe H., Eguchi Y., Shimizu S., Martinou J.C., and Tsujimoto Y. Death-signaling cascade in mouse cerebellar granule neurons. Eur J Neurosci 10 (1998) 1403-1411
34. Thompson G.B., van Heerden J.A., and Sarr M.G. Adenocarcinoma of the stomach: are we making progress?. Lancet 342 (1993) 713-718
35. Tsujimoto Y. Cell death regulation by the Bcl-2 protein family in the mitochondria. J Cell Physiol 19 (2003) 158-167
36. Vaux D.L., and Korsmeyer S.J. Cell death in development. Cell 96 (1999) 245-254
37. Verma Y.K., Gangenahalli G.U., Singh V.K., Gupta P., Chandra R., Sharma R.K., et al. Cell death regulation by B-cell lymphoma protein. Apoptosis 11 4 (2006) 459-471
38. Wang J.Z., Tan W.Q., and Zhao Q. Effect of RFP134 on membrane lipid fluidity in UMR106 cells. Dev Reprod Biol 1 (1999) 23-27
39. Yang J., Liu X.S., Bhalla K., Kim C.N., Ibrado A.M., Cai J.Y., et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 275 (1997) 1129-1132
40. Zhou H., Hanzel W.J., Liu X., Lutschg A., and Wang X. Apf-1, a human protein homologous to C. elegans CED-4, participates cytochrome c-dependent activation of caspase-3. Cell 90 (1997) 405-413