Gene expression profiles of necrosis and apoptosis induced by 5-fluoro-2′-deoxyuridine

Genomics

Volumn 92, Issue 1, 2008, Pages 9-17

  Sato, Akira ^a   Hiramoto, Akiko ^a   Uchikubo, Yusuke ^a   Miyazaki, Eriko ^a   Satake, Akito ^a   Naito, Tomoharu ^a   Hiraoka, Osamu ^b   Miyake, Tsuyoshi ^c   Kim, Hye Sook ^a   Wataya, Yusuke ^a  

^a OKAYAMA UNIVERSITY   (Japan)

^b SHUJITSU UNIVERSITY   (Japan)

^c INDUSTRIAL TECHNOLOGY CENTER OF OKAYAMA PREFECTURE   (Japan)

Author keywords

5 Fluoro 2 deoxyuridine; Apoptosis; Cell death; Gene expression profile; Microarray analysis; Necrosis

Indexed keywords

COMPLEMENTARY DNA; FLOXURIDINE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 90; NUCLEOTIDE; THYMIDYLATE SYNTHASE;

ANIMAL CELL; ANTINEOPLASTIC ACTIVITY; APOPTOSIS; ARTICLE; CANCER CELL CULTURE; CELL CLONE; CELL DEATH; CONTROLLED STUDY; CULTURE MEDIUM; DNA MICROARRAY; DRUG EFFECT; DRUG MECHANISM; ENZYME INHIBITION; GENE EXPRESSION PROFILING; GENE IDENTIFICATION; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; UNINDEXED SEQUENCE;

ANIMALS; ANTIMETABOLITES, ANTINEOPLASTIC; APOPTOSIS; CELL LINE, TUMOR; CYTOCHROMES C; FLOXURIDINE; GENE EXPRESSION PROFILING; HSP90 HEAT-SHOCK PROTEINS; MICE; MITOCHONDRIA; NECROSIS; OLIGONUCLEOTIDE ARRAY SEQUENCE ANALYSIS;

EID: 45249120588     PISSN: 08887543     EISSN: 10898646     Source Type: Journal    
DOI: 10.1016/j.ygeno.2008.02.002     Document Type: Article

References (46)

1. Heidelberger C. Fluorinated pyrimidines. Prog. Nucleic Acid Res. Mol. Biol. 4 (1965) 1-50
2. Danenberg P.V. Thymidylate synthetase-a target enzyme in cancer chemotherapy. Biochim. Biophys. Acta 473 (1977) 73-92
3. Mayer C.E. The pharmacology of the fluoropyrimidines. Pharmacol. Rev. 33 (1980) 1-15
4. Santi D.V. Perspectives on the design and biochemical pharmacology of inhibitors of thymidylate synthetase. J. Med. Chem. 23 (1980) 103-111
5. Heidelberger C., Danenberg P.V., and Moran R.G. Fluorinated pyrimidines and their nucleosides. Adv. Enzymol. Relat. Areas Mol. Biol. 54 (1983) 58-119
6. In: Santi D.V., Danenberg P.V., Blakley R.L., and Benkovic S.J. (Eds). Folates and Pterins vol. 1 (1984), Wiley, New York 345-398
7. Yoshioka A., et al. Deoxyribonucleoside triphosphate imbalance. 5-Fluorodeoxyuridine-induced DNA double strand breaks in mouse FM3A cells and the mechanism of cell death. J. Biol. Chem. 262 (1987) 8235-8241
8. Fiers W., Beyaert R., Declercq W., and Vandenabeele P. More than one way to die: apoptosis, necrosis and reactive oxygen damage. Oncogene 18 (1999) 7719-7730
9. Kerr J.F., Wyllie A.H., and Currie A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26 (1972) 239-257
10. Wyllie A.H., Kerr J.F., and Currie A.R. Cell death: the significance of apoptosis. Int. Rev. Cytol. 68 (1980) 251-306
11. Denecker G., Vercammen D., Declercq W., and Vandenabeele P. Apoptotic and necrotic cell death induced by death domain receptors. Cell. Mol. Life Sci. 58 (2001) 356-370
12. Kakutani T., et al. Different modes of cell death induced by 5-fluoro-2′-deoxyuridine in two clones of the mouse mammary tumor FM3A cell line. Biochem. Biophys. Res. Commun. 247 (1998) 773-779
13. Rutherford S.L., and Lindquist S. Hsp90 as a capacitor for morphological evolution. Nature 396 (1998) 336-342
14. Scheibel T. J. Buchner. The Hsp90 complex-a super-chaperone machine as a novel drug target. Biochem. Pharmacol. 56 (1998) 675-682
15. Lewis J., et al. Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP) and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J. Biol. Chem. 275 (2000) 10519-10526
16. Vanden Berghe T., Kalai M., Van Loo G., Declercq W., and Vandenabeele P. Disruption of HSP90 function reverts tumor necrosis factor-induced necrosis to apoptosis. J. Biol. Chem. 278 (2003) 5622-5629
17. Zhao C., and Wang E. Heat shock protein 90 suppresses tumor necrosis factor alpha induced apoptosis by preventing the cleavage of Bid in NIH3T3 fibroblasts. Cell. Signal. 16 (2004) 313-321
18. Vanden Berghe T., et al. Differential signaling to apoptotic and necrotic cell death by Fas-associated death domain protein FADD. J. Biol. Chem. 279 (2004) 7925-7933
19. Powers M.V., and Workman P. Targeting of multiple signalling pathways by heat shock protein 90 molecular chaperone inhibitors. Endocr. Relat. Cancer 13 (2006) S125-S135
20. Tsujimoto Y. Cell death regulation by the Bcl-2 protein family in the mitochondria. J. Cell. Physiol. 195 (2003) 158-167
21. Green D.R., and Kroemer G. The pathophysiology of mitochondrial cell death. Science 305 (2004) 626-629
22. Nakagawa T., et al. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434 (2005) 652-658
23. Gogvadze V., and Orrenius S. Mitochondrial regulation of apoptotic cell death. Chem. Biol. Interact. 163 (2006) 4-14
24. Desagher S., and Martinou J.C. Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10 (2000) 369-377
25. Acehan D., et al. Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation. Mol. Cell 9 (2002) 423-432.
26. Kulms D., and Schwarz T. Independent contribution of three different pathways to ultraviolet-B-induced apoptosis. Biochem. Pharmacol. 64 (2002) 837-841
27. Verma Y.K., et al. Cell death regulation by B-cell lymphoma protein. Apoptosis 11 (2006) 459-471
28. Nur-E-Kamal A., et al. Nuclear translocation of cytochrome c during apoptosis. J. Biol. Chem. 279 (2004) 24911-24914
29. Panaretou B., et al. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol. Cell 10 (2002) 1307-1318
30. Lotz G.P., Lin H., Harst A., and Obermann W.M. Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J. Biol. Chem. 278 (2003) 17228-17235
31. Meyer P., et al. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J. 23 (2004) 1402-1410
32. Siligardi G., et al. Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J. Biol. Chem. 279 (2004) 51989-51998
33. Obermann W.M., Sondermann H., Russo A.A., Pavletich N.P., and Hartl F.U. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J. Cell Biol. 143 (1998) 901-910
34. Panaretou B., et al. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17 (1999) 4829-4836
35. Grenert J.P., Johnson B.D., and Toft D.O. The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes. J. Biol. Chem. 274 (1999) 17525-17533
36. Connell P., et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell Biol. 3 (2001) 93-96
37. Pearl L.H., and Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75 (2006) 271-294
38. Prodromou C., et al. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90 (1997) 65-75
39. Stebbins C.E., et al. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89 (1997) 239-250
40. Kitchens M.E., Forsthoefel A.M., Rafique Z., Spencer H.T., and Berger F.G. Ligand-mediated induction of thymidylate synthase occurs by enzyme stabilization. Implications for autoregulation of translation. J. Biol. Chem. 274 (1999) 12544-12547
41. Fischer J.A., Muller-Weeks S., and Caradonna S.J. Fluorodeoxyuridine modulates cellular expression of the DNA base excision repair enzyme uracil-DNA glycosylase. Cancer Res. 66 (2006) 8829-8837
42. Kerr M.K., Martin M., and Churchill G.A. Analysis of variance for gene expression microarray data. J. Comput. Biol. 7 (2000) 819-837
43. Kerr M.K., and Churchill G.A. Statistical design and the analysis of gene expression microarray data. Genet. Res. 77 (2001) 123-128
44. Bender R., and Lange S. Adjusting for multiple testing-when and how?. J. Clin. Epidemiol. 54 (2001) 343-349
45. Eisen M.B., Spellman P.T., Brown P.O., and Botstein D. Cluster analysis and display of genome-wide expression patterns. Proc. Natl. Acad. Sci. USA 95 (1998) 14863-14868
46. Matsui K., et al. Cutting edge: role of TANK-binding kinase 1 and inducible IkB kinase in IFN responses against viruses in innate immune cells. J. Immunol. 177 (2006) 5785-5789