Disulfiram is a potent inhibitor of proteases of the caspase family

Chemical Research in Toxicology

Volumn 10, Issue 12, 1997, Pages 1319-1324

  Nobel, C Stefan I ^a   Kimland, Monica ^a   Nicholson, Donald W ^b   Orrenius, Sten ^a   Slater, Andrew F G ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b MERCK FROSST CENTRE FOR THERAPEUTIC RESEARCH   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

DIETHYLDITHIOCARBAMIC ACID; DISULFIDE; DISULFIRAM; DITHIOTHREITOL; FAS ANTIGEN; GLUTATHIONE DISULFIDE; INTERLEUKIN 1BETA CONVERTING ENZYME; PROTEIN S 100; PROTEINASE INHIBITOR; THIOL GROUP;

ARTICLE; CONTROLLED STUDY; CYTOSOL; ENZYME ACTIVITY; ENZYME DEGRADATION; HUMAN; HUMAN CELL; LEUKEMIA CELL LINE; PROTEIN FAMILY; PROTEINASE INHIBITION;

ALCOHOL DETERRENTS; BLOTTING, WESTERN; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; DISULFIRAM; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLUTATHIONE; GLUTATHIONE DISULFIDE; HUMANS; JURKAT CELLS; KINETICS;

EID: 0031445356     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx970131m     Document Type: Article

References (41)

1. Nicholson, D. W. (1996) ICE/CED3-like proteases as therapeutic targets for the control of inappropriate apoptosis. Nature Biotech. 14, 297-301.
2. Nicholson, D. W., Ali, A., Thornberry, N. A., Vaillancourt, J. P., Ding, C. K., Gallant, M., Gareau, Y., Griffin, P. R., Labelle, M., Lazebnik, Y. A., Munday, N. A., Raju, S. R., Smulson, M. E., Yamin, T.-T., Yu, V. L., and Miller, D. K. (1995) Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 376, 37-43.
3. Jacobson, M. D., Weil, M., and Raff, M. C. (1996) Role of ced-3/ ICE-family proteases in staurosporine-induced programmed cell death. J. Cell. Biol. 133, 1041-1051.
4. Alnemri, E. S., Livingston, D. J., Nicholson, D. W., Salvesen, G., Thornberry, N. A., Wong, W. W., and Yuan, J. (1996) Human ICE/ CED-3 protease nomenclature. Cell 87, 171.
5. Srinivasula, S. M., Fernandes-Alnemri, T., Zangrilli, J., Robertson, N., Armstrong, R. C., Wang, L., Trapani, J. A., Tomaselli, K. J., Litwack, G., and Alnemri, E. S. (1996) The ced-3/Interleukin 1β converting enzyme-like homologue Mch6 and the lamin-cleaving enzyme Mch2a are substrates for the apoptotic mediator CPP32. J. Biol. Chem. 271, 27099-27106.
6. Srinivasula, S. M., Ahmad, M., Fernandes-Alnemri, T., Litwack, G., and Alnemri, E. S. (1996) Molecular ordering of the Fasapoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases. Proc. Natl. Acad. Sci. U.S.A. 93, 14486-14491.
7. Orth, K., O'Rourke, K., Salvesen, G. S., and Dixit, V. M. (1996) Molecular ordering of apoptotic mammalian CED-3/ICE-Iike proteases. J. Biol. Chem. 271, 20977-20980.
8. Kuida, K., Zheng, T. S., Na, S., Kuan, C., Yang, D., Karasuyama, H-, Rakic, P., and Flavell, R. A. (1996) Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature 384, 368-372.
9. Schlegel, J., Peters, I., Orrenius, S., Miller, D. K., Thornberry, N. A., Yamin, T.-T., and Nicholson, D. W. (1996) CPP32/apopain is a key interleukin-1β converting enzyme-like protease involved in Fas-mediated apoptosis. J. Biol. Chem. 271, 1841-1844.
10. L. J. Biol. Chem. 271, 17601-17604.
11. Cerretti, D. P., Kozlosky, C. J., Mosley, B., Nelson, N., Van, N. K., Greenstreet, T. A., March, C. J., Kronheim, S. R., Druck, T., Cannizzaro, L. A., et al. (1992) Molecular cloning of the interleukin-1β converting enzyme. Science 256, 97-100.
12. Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J., Elliston, K. O., Ayala, J. M., Casano, F. J., Chin, J., Ding, G. J.-F., Egger, L. A., Gaffney, E. P., Limjuco, G., Palyha, O. C., Raju, S. M., Rolando, A. M., Salley, J. P., Yamin, T.-T., Lee, T. D., Shively, J. E., MacCross, M., Mumford, R. A., Schmidt, J. A., and Tocci, M. J. (1992) A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes. Nature 356, 768-774.
13. Thornberry, N. A. (1994) Interleukin-1β converting enzyme. Methods Enzymol. 244, 615-631.
14. Kuida, K., Lippke, J. A., Ku, G., Harding, M. W., Livingston, D. J., Su, M. S.-S., and Flavell, R. A. (1995) Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme. Science 267, 2000-2003.
15. Li, P., Allen, H., Banerjee, S., Franklin, S., Herzog, L., Johnston, C., McDowell, J., Paskind, M., Rodman, L., Salfeld, J., et al. (1995) Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1 beta and resistant to endotoxic shock. Cell 80, 401-411.
16. Dinarello, C. A., and Thompson, R. C. (1991) Blocking IL-1: interleukin 1 receptor antagonist in vivo and in vitro. Immunol. Today 12, 404-410.
17. Yuan, J., Shaham, S., Ledoux, S., Ellis, H. M., and Horvitz, H. R. (1993) The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell 75, 641-652.
18. Miura, M., Zhu, H., Rotello, R. J., Hartwig, E. A., and Yuan, J. (1993) Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homologue of the C. elegans cell death gene ced-3. Cell 75, 653-660.
19. Los, M., Van de Craen, M., Penning, L. C., Schenk, H., Westendorp, M., Baeuerle, P. A., Droge, W., and Schulze-Osthoff, K. (1995) Requirement of an ICE/CED-3 protease for Fas/APO-1-mediated apoptosis. Nature 375, 81-83.
20. Enari, M., Hug, H., and Nagata, S. (1995) Involvement of an ICE-like protease in Fas-mediated apoptosis. Nature 375, 78-81.
21. Gilbert, H. F. (1990) Molecular and cellular aspects of thioldisulfide exchange. Adv. Enzymol. Relat. Areas Mol. Biol. 63, 69-172.
22. Wilson, K. P., Black, J.-A. F., Thomson, J. A., Kim, E. E., Griffith, J. P., Navia, M. A., Murcko, M. A., Chambers, S. P., Aldape, R. A., Raybuck, S. A., and Livingston, D. J. (1994) Structure and mechanism of interleukin-1β converting enzyme. Nature 370, 270-275.
23. Johansson, B. (1992) A review of the pharmacokinetics and pharmacodynamics of disulfiram and its metabolites. Acta Psychiatr. Scand. 86, 15-26.
24. Vallari, R. C., and Pietruszko, R. (1982) Human aldehyde dehydrogenase: Mechanism of inhibition by disulfiram. Science 216, 637-639.
25. Sanny, C. G., and Weiner, H. (1987) Inactivation of horse liver mitochondrial aldehyde dehydrogenase by disulfiram. Evidence that disulfiram is not an active-site-directed reagent. Biochem. J. 242, 499-503.
26. m mitochondrial aldehyde dehydrogenase. Biochem. Pharmacol. 49, 693-700.
27. Neims, A. H., Coffey, D. S., and Hellerman, L. (1966) Interaction between tetraethylthiuram disulfide and the sulfhydryl groups of D-amino acid oxidase and of hemoglobin. J. Biol. Chem. 241, 5941-5948.
28. Nobel, C. S. I., Burgess, D. H., Zhivotovsky, B., Burkitt, M. J., Orrenius, S., and Slater, A. F. G. (1997) Mechanism of dithiocarbamate inhibition of apoptosis: Thiol oxidation by dithiocarbamate disulfides directly inhibits processing of the caspase-3 proenzyme. Chem. Res. Toxicol. 10, 636-643.
29. Liu, X., Kim, N. C., Yang, J., Jemmerson, R., and Wang, X. (1996) Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c. Cell 86, 147-157.
30. Slater, A. F. G., Nobel, C. S. I, Maellaro, E., Bustamante, J., Kimland, M., and Orrenius, S. (1995) Nitrone spin traps and a nitroxide antioxidant inhibit a common pathway of thymocyte apoptosis. Biochem. J. 306, 771-778.
31. Cotgreave, I. A., and Moldéus, P. (1986) Methodologies for the application of monobromobimane to the simultaneous analysis of soluble and protein thiol components of biological systems. J. Biochem. Biophys. Methods 13, 231-249.
32. Tsou, C. L. (1988) Kinetics of substrate reaction during irreversible modification of enzyme activity. Adv. Enzymol. Relat. Areas Mol. Biol. 61, 381-436.
33. Morrison, J. F., and of Walsh, C. T. (1988) The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. Relat. Areas Mol. Biol. 61, 201-301.
34. Faiman, M. D., Artman, L., and Haya, K. (1980) Disulfiram distribution and elimination in the rat after oral and intraperitoneal administration. Alcoholism 4, 412-419.
35. Rotonda, J., Nicholson, D. W., Fazil, K. M., Gallant, M., Gareau, Y., Labelle, M., Peterson, E. P., Rasper, D. M., Ruel, R., Vaillancourt, J. P., Thornberry, N. A., and Becker, J. W. (1996) The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. Nature Struct. Biol. 3, 619-625.
36. Thorn, G. D., and Ludwig, R. A. (1962) The dithiocarbamates and related compounds, Elsevier Publishing Co., Amsterdam.
37. Dimmeler, S., Haendeler, J., Nehls, M., and Zeiher, A. M. (1997) Suppression of apoptosis by nitric oxide via inhibition of interleukin-1-beta-converting enzyme (ice)-like and cysteine protease protein (cpp)-32-like proteases. J. Exp. Med. 185, 601-607.
38. Elskens, M. T., and Penninckx, M. J. (1995) In vitro inactivation of yeast glutathione reductase by tetramethylthiuram disulphide. Eur. J. Biochem. 231, 667-672.
39. Babson, J. R., and Reed, D. J. (1978) Inactivation of glutathione reductase by 2-chloroethyl nitrosourea-derived isocyanates. Biochem. Biophys. Res. Commun. 83, 754-762.
40. Maellaro, E., Delbello, B., and Comporti, M. (1996) Protection by ascorbate against apoptosis of thymocytes-implications of ascorbate-induced nonlethal oxidative stress and poly(adp-ribosyl)ation. Exp. Cell Res. 226, 105-113.
41. Clement, M. V., and Stamenkovic, I. (1996) Superoxide anion is a natural inhibitor of fas-mediated cell death. EMBO J. 15, 216-225.