Cytosolic heat shock proteins and heme oxygenase-1 are preferentially induced in response to specific and localized intramitochondrial damage by tetrafluoroethylcysteine

Biochemical Pharmacology

Volumn 72, Issue 1, 2006, Pages 80-90

  Ho, Han K ^a   Jia, Yankai ^a   Coe, Kevin J ^a   Gao, Qiuxia ^a   Doneanu, Catalin E ^a   Hu, Zhonghua ^b   Bammler, Theo K ^a   Beyer, Richard P ^a   Fausto, Nelson ^a   Bruschi, Sam A ^a   Nelson, Sidney D ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b AMGEN INC   (United States)

Author keywords

Cytotoxicity; Heat shock proteins; Heme oxygenase; Microarray; Mitochondrial dysfunction; Tetrafluoroethylcysteine

Indexed keywords

CYSTEINE DERIVATIVE; DIQUAT; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 105; HEAT SHOCK PROTEIN 25; HEAT SHOCK PROTEIN 32; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEME OXYGENASE 1; PARACETAMOL; ROTENONE; TETRAFLUOROETHYLCYSTEINE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL LINE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; IMMUNOREACTIVITY; LIVER CELL; MICROARRAY ANALYSIS; MITOCHONDRION; MOUSE; MOUSE STRAIN; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; STATISTICAL SIGNIFICANCE;

CELL LINE; CELL SURVIVAL; CYSTEINE; CYTOSOL; DIMERIZATION; GENE EXPRESSION; GENE SILENCING; HEAT-SHOCK PROTEINS; HEME OXYGENASE-1; HEPATOCYTES; HYDROCARBONS, FLUORINATED; MITOCHONDRIA, LIVER; PROTEIN ARRAY ANALYSIS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RNA, MESSENGER; RNA, SMALL INTERFERING; TRANSFECTION; UP-REGULATION;

EID: 33646940104     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2006.03.019     Document Type: Article

References (42)

1. Halestrap A.P., Doran E., Gillespie J.P., and O'Toole A. Mitochondria and cell death. Biochem Soc Trans 28 (2000) 170-177
2. Hengartner M.O. The biochemistry of apoptosis. Nature 407 (2000) 770-776
3. Duchen M.R. Roles of mitochondria in health and disease. Diabetes 53 (2004) S96-S102
4. Krahenbuhl S. Mitochondria: important target for drug toxicity?. J Hepatol 34 (2001) 334-336
5. Anders M.W., and Dekant W. Glutathione-dependent bioactivation of haloalkenes. Annu Rev Pharmacol Toxicol 38 (1998) 501-537
6. IARC. Tetrafluoroethylene. IARC Monogr Eval Carcinog Risks Hum1999;71:1143. http://www-cie.iarc.fr/htdocs/monographs/vol71/048-tetrafluo.html.
7. James E.A., Gygi S.P., Adams M.L., Pierce R.H., Fausto N., Aebersold R.H., et al. Mitochondrial aconitase modification, functional inhibition, and evidence for a supramolecular complex of the TCA cycle by the renal toxicant S-(1,1,2,2-tetrafluoroethyl)-l-cysteine. Biochemistry 41 (2002) 6789-6797
8. Keller D.A., Kennedy Jr. G.L., Ross P.E., Kelly D.P., and Elliott G.S. Toxicity of tetrafluoroethylene and S-(1,1,2,2-tetrafluoroethyl)-l-cysteine in rats and mice. Toxicol Sci 56 (2000) 414-423
9. Lock E.A., and Ishmael J. The nephrotoxicity and hepatotoxicity of 1,1,2,2-tetrafluoroethyl-l-cysteine in the rat. Arch Toxicol 72 (1998) 347-354
10. Cooper A.J., and Pinto J.T. Aminotransferase, l-amino acid oxidase and beta-lyase reactions involving l-cysteine S-conjugates found in allium extracts relevance to biological activity?. Biochem Pharmacol 69 (2005) 209-220
11. Odum J., and Green T. The metabolism and nephrotoxicity of tetrafluoroethylene in the rat. Toxicol Appl Pharmacol 76 (1984) 306-318
12. Cooper A.J., Bruschi S.A., and Anders M.W. Toxic, halogenated cysteine S-conjugates and targeting of mitochondrial enzymes of energy metabolism. Biochem Pharmacol 64 (2002) 553-564
13. Bruschi S.A., West K.A., Crabb J.W., Gupta R.S., and Stevens J.L. Mitochondrial HSP60 (P1 protein) and a HSP70-like protein (mortalin) are major targets for modification during S-(1,1,2,2-tetrafluoroethyl)-l-cysteine-induced nephrotoxicity. J Biol Chem 268 (1993) 23157-23161
14. Wu J.C., Merlino G., Cveklova K., Mosinger Jr. B., and Fausto N. Autonomous growth in serum-free medium and production of hepatocellular carcinomas by differentiated hepatocyte lines that overexpress transforming growth factor alpha 1. Cancer Res 54 (1994) 5964-5973
15. Ho H.K., White C.C., Fernandez C., Fausto N., Kavanagh T.J., Nelson S.D., et al. Nrf2 activation involves an oxidative-stress independent pathway in tetrafluoroethylcysteine-induced cytotoxicity. Toxicol Sci 86 (2005) 354-364
16. Ho H.K., Hu Z.H., Tzung S.P., Hockenbery D.M., Fausto N., Nelson S.D., et al. BCL-xL overexpression effectively protects against tetrafluoroethylcysteine-induced intramitochondrial damage and cell death. Biochem Pharmacol 69 (2005) 147-157
17. Pierce R.H., Franklin C.C., Campbell J.S., Tonge R.P., Chen W., Fausto N., et al. Cell culture model for acetaminophen-induced hepatocyte death in vivo. Biochem Pharmacol 64 (2002) 413-424
18. Bolstad B.M., Irizarry R.A., Astrand M., and Speed T.P. A comparison of normalization methods for high density oligonucleotide array data based on variance and bias. Bioinformatics 19 (2003) 185-193
19. Single B., Leist M., and Nicotera P. Simultaneous release of adenylate kinase and cytochrome c in cell death. Cell Death Differ 5 (1998) 1001-1003
20. Dietze E.C., Schafer A., Omichinski J.G., and Nelson S.D. Inactivation of glyceraldehyde-3-phosphate dehydrogenase by a reactive metabolite of acetaminophen and mass spectral characterization of an arylated active site peptide. Chem Res Toxicol 10 (1997) 1097-1103
21. Shevchenko A., Wilm M., Vorm O., and Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 68 (1996) 850-858
22. Plumb J.A., Milroy R., and Kaye S.B. Effects of the pH dependence of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-tetrazolium bromide-formazan absorption on chemosensitivity determined by a novel tetrazolium-based assay. Cancer Res 49 (1989) 4435-4440
23. De Maio A. Heat shock proteins: facts, thoughts, and dreams. Shock 11 (1999) 1-12
24. Kregel K.C. Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance. J Appl Physiol 92 (2002) 2177-2186
25. Ritossa F. Discovery of the heat shock response. Cell Stress Chaperones 1 (1996) 97-98
26. Sammut I.A., and Harrison J.C. Cardiac mitochondrial complex activity is enhanced by heat shock proteins. Clin Exp Pharmacol Physiol 30 (2003) 110-115
27. Maniratanachote R., Minami K., Katoh M., Nakajima M., and Yokoi T. Chaperone proteins involved in troglitazone-induced toxicity in human hepatoma cell lines. Toxicol Sci 83 (2005) 293-302
28. Schafler A.E., Kirmanoglou K., Pecher P., Hannekum A., and Schumacher B. Overexpression of heat shock protein 60/10 in myocardium of patients with chronic atrial fibrillation. Ann Thorac Surg 74 (2002) 767-770
29. Asmellash S., Stevens J.L., and Ichimura T. Modulating the endoplasmic reticulum stress response with trans-4,5-dihydroxy-1,2-dithiane prevents chemically induced renal injury in vivo. Toxicol Sci 88 (2005) 576-584
30. Garrido C., Gurbuxani S., Ravagnan L., and Kroemer G. Heat shock proteins: endogenous modulators of apoptotic cell death. Biochem Biophys Res Commun 286 (2001) 433-442
31. Mosser D.D., Caron A.W., Bourget L., Denis-Larose C., and Massie B. Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol Cell Biol 17 (1997) 5317-5327
32. Beere H.M., Wolf B.B., Cain K., Mosser D.D., Mahboubi A., Kuwana T., et al. Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol 2 (2000) 469-475
33. Gotoh T., Terada K., Oyadomari S., and Mori M. hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Cell Death Differ 11 (2004) 390-402
34. Ravagnan L., Roumier T., and Kroemer G. Mitochondria, the killer organelles and their weapons. J Cell Physiol 192 (2002) 131-137
35. Zhou H., Kato A., Yasuda H., Odamaki M., Itoh H., and Hishida A. The induction of heat shock protein-72 attenuates cisplatin-induced acute renal failure in rats. Pflugers Arch 446 (2003) 116-124
36. Zavialov A.V., Gaestel M., Korpela T., and Zav'yalov V.P. Thiol/disulfide exchange between small heat shock protein 25 and glutathione. Biochim Biophys Acta 1388 (1998) 123-132
37. Arrigo A.P. Hsp27: novel regulator of intracellular redox state. IUBMB Life 52 (2001) 303-307
38. Diaz-Latoud C., Buache E., Javouhey E., and Arrigo A.P. Substitution of the unique cysteine residue of murine Hsp25 interferes with the protective activity of this stress protein through inhibition of dimer formation. Antioxid Redox Signal 7 (2005) 436-445
39. Ehrnsperger M. Molecular chaperones in the life cycle of proteins (1997), Marcel Dekker, New York
40. Downs C.A., Jones L.R., and Heckathorn S.A. Evidence for a novel set of small heat-shock proteins that associates with the mitochondria of murine PC12 cells and protects NADH:ubiquinone oxidoreductase from heat and oxidative stress. Arch Biochem Biophys 365 (1999) 344-350
41. He L., and Lemasters J.J. Heat shock suppresses the permeability transition in rat liver mitochondria. J Biol Chem 278 (2003) 16755-16760
42. Samali A., Robertson J.D., Peterson E., Manero F., van Zeijl L., Paul C., et al. Hsp27 protects mitochondria of thermotolerant cells against apoptotic stimuli. Cell Stress Chaperones 6 (2001) 49-58