Cross-linking of dithiols by mitomycin C

Chemical Research in Toxicology

Volumn 23, Issue 8, 2010, Pages 1384-1392

  Paz, Manuel M ^a  

^a UNIVERSITY OF SANTIAGO DE COMPOSTELA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

1,3 PROPANEDITHIOL; AMINE; DITHIOL DERIVATIVE; DITHIOTHREITOL; MITOMYCIN C; MITOSENE DERIVATIVE; UNCLASSIFIED DRUG;

ALKYLATION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; CROSS LINKING; DIASTEREOISOMER; HUMAN; HUMAN CELL; NUCLEAR MAGNETIC RESONANCE; PROTON NUCLEAR MAGNETIC RESONANCE; RACEMIZATION; ULTRAVIOLET RADIATION;

CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CROSS-LINKING REAGENTS; MASS SPECTROMETRY; MITOMYCIN; MOLECULAR CONFORMATION; STEREOISOMERISM; SULFHYDRYL COMPOUNDS;

EID: 77955686271     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx100134h     Document Type: Article

References (39)

1. Paz, M. M. (2008) Antitumor Antibiotics, in Anticancer Therapeutics (Missailidis, S., Ed.) pp 112-115, John Wiley and Sons, Chichester, UK.
2. Teus, M. A., de Benito-Llopis, L., and Alió, J. L. (2009) Mitomycin C in corneal refractive surgery Surv. Ophthalmol. 54, 487-502
3. Iyer, V. N. and Szybalsk, W. (1964) Mitomycin and porfiromycin: chemical mechanism of activation and cross-linking of DNA Science 145, 55-58
4. Tomasz, M. (1995) Mitomycin C: small, fast and deadly (but very selective) Chem. Biol. 2, 575-579
5. Tomasz, M. and Lipman, R. (1981) Reductive metabolism and alkylating activity of mitomycin C induced by rat liver microsomes Biochemistry 20, 5056-5061
6. Paz, M. M. (2010) Reaction of reductively activated mitomycin C with aqueous bicarbonate: Isolation and characterization of an oxazolidinone derivative of cis-1-hydroxy-2,7-diaminomitosene Bioorg. Med. Chem. Lett. 20, 31-34
7. Sharma, M. and Tomasz, M. (1994) Conjugation of glutathione and other thiols with bioreductively activated mitomycin C. Effect of thiols on the reductive activation rate Chem. Res. Toxicol. 7, 390-400
8. Tomasz, M., Lipman, R., Chowdary, D., Pawlak, J., Verdine, G. L., and Nakanishi, K. (1987) Isolation and structure of a covalent cross-link adduct between mitomycin C and DNA Science 235, 1204-1208
9. Cummings, J., Spanswick, V. J., Tomasz, M., and Smyth, J. F. (1998) Enzymology of mitomycin C metabolic activation in tumour tissue: implications for enzyme-directed bioreductive drug development Biochem. Pharmacol. 56, 405-414
10. Celli, M. and Jaiswal, A. K. (2003) Role of GRP58 in mitomycin C-induced DNA cross-Linking Cancer Res. 63, 6016-6025
11. Adikesavan, A. K. and Jaiswal, A. K. (2007) Thioredoxin-like domains required for glucose regulatory protein 58 mediated reductive activation of mitomycin C leading to DNA cross-linking Mol. Cancer Ther. 6, 2719-2727
12. Paz, M. M. (2009) Reductive activation of mitomycin C by thiols: Kinetics, mechanism, and biological implications Chem. Res. Toxicol. 22, 1663-1668
13. Kontou, M., Adelfalk, C., Ramirez, M. H., Ruppitsch, W., Hirsch-Kauffmann, M., and Schweiger, M. (2002) Overexpressed thioredoxin compensates Fanconi anemia related chromosomal instability Oncogene 21, 2406-2412
14. Ruppitsch, W., Meisslitzer, C., Hirsch-Kauffmann, M., and Schweiger, M. (1998) Overexpression of thioredoxin in Fanconi anemia fibroblasts prevents the cytotoxic and DNA damaging effect of mitomycin C and diepoxybutane FEBS Lett. 422, 99-102
15. Yokomizo, A., Ono, M., Nanri, H., Makino, Y., Ohga, T., Wada, M., Okamoto, T., Yodoi, J., Kuwano, M., and Kohno, K. (1995) Cellular levels of thioredoxin associated with drug sensitivity to cisplatin, mitomycin C, doxorubicin, and etoposide Cancer Res. 55, 4293-4296
16. Hoey, B. M., Butler, J., and Swallow, A. J. (1988) Reductive activation of mitomycin C Biochemistry 27, 2608-2614
17. Schiltz, P. and Kohn, H. (1993) Studies on the reactivity of reductively activated mitomycin C J. Am. Chem. Soc. 115, 10510-10518
18. Kohn, H., Zein, N., Lin, X. Q., Ding, J.-Q., and Kadish, K. M. (1987) Mechanistic studies on the mode of reaction of mitomycin C under catalytic and electrochemical reductive conditions J. Am. Chem. Soc. 109, 1833-1840
19. 4 for the reductive activation of mitomycin C J. Am. Chem. Soc. 115, 10497-10509
20. Tomasz, M., Jung, M., Verdine, G., and Nakanishi, K. (1984) Circular dichroism spectroscopy as a probe for the stereochemistry of aziridine cleavage reactions of mitomycin C. Application to adducts ofmitomycin with DNA constituents J. Am. Chem. Soc. 106, 7367-7370
21. He, Q.-Y., Maruenda, H., and Tomasz, M. (1994) Novel bioreductive activation mechanism of mitomycin C derivatives bearing a disulfide substituent in their quinone J. Am. Chem. Soc. 116, 9349-9350
22. Sharma, M. and Tomasz, M. (1994) Effects of glutathione on alkylation and cross-linking of DNA by mitomycin C. Isolation of a ternary glutathione-mitomycin-DNA adduct Chem. Res. Toxicol. 6, 390-400
23. Peterson, D. M. and Fisher, J. (1986) Autocatalytic quinone methide formation from mitomycin C Biochemistry 25, 4077-4084
24. Schiltz, P. and Kohn, H. (1992) Sodium dithionite-mediated mitomycin C reductive activation processes Tetrahedron Lett. 33, 4709-4712
25. Kallis, G. B. and Holmgren, A. (1980) Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli J. Biol. Chem. 255, 10261-10265
26. Zhong, L., Arnér, E. S. J., and Holmgren, A. (2000) Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence Proc. Natl. Acad. Sci. U.S.A. 97, 5854-5859
27. Arnér, E. S. J., Nakamura, H., Sasada, T., Yodoi, J., Holmgren, A., Spyrou, G., Fang, J., Lu, J., and Holmgren, A. (2001) Analysis of the inhibition of mammalian thioredoxin, thioredoxin reductase, and glutaredoxin by cis-diamminedichloroplatinum (II) and its major metabolite, the glutathione-platinum complex Free Radical Biol. Med. 31, 1170-1178
28. Fang, J. and Holmgren, A. (2006) Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo J. Am. Chem. Soc. 128, 1879-1885
29. Saravanamuthu, A., Vickers, T. J., Bond, C. S., Peterson, M. R., Hunter, W. N., and Fairlamb, A. H. J. (2004) Two interacting binding sites for quinacrine derivatives in the active site of trypanothione reductase: a template for drug design J. Biol. Chem. 279, 29493-29500
30. Fang, J., Lu, J., and Holmgren, A. (2005) Thioredoxin reductase is irreversibly modified by curcumin: a novel molecular mechanism for its anticancer activity J. Biol. Chem. 280, 25284-90
31. Esterbauer, H. (1970) Kinetik der reaktion von sulfhydrylverbindungen mit α,β-ungesättigten aldehyden in wäβrigem system Monatsh. Chem. 101, 782-810
32. Holmgren, A. (1995) Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide Structure 3, 239-243
33. Tereshko, V., Minasov, G., and Egli, M. (1999) The Dickerson-Drew B-DNA dodecamer revisited at atomic resolution J. Am. Chem. Soc. 121, 470-471
34. Sastry, M., Fiala, R., Lipman, R., Tomasz, M., and Patel, D. J. (1995) Solution structure of the monoalkylated mitomycin C-DNA complex J. Mol. Biol. 247, 338-359
35. Ramadan, D., Cline, D. J., Bai, S., Thorpe, C., and Schneider, J. P. (2007) Effects of As(III) binding on beta-hairpin structure J. Am. Chem. Soc. 129, 2981-2988
36. Aposhian, H. V. and Aposhian, M. M. (2006) Arsenic toxicology: five questions Chem. Res. Toxicol. 19, 1-15
37. Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., and Talalay, P. (2002) Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants Proc. Natl. Acad. Sci. U.S.A. 99, 11908-11913
38. Hawkins, H. C., de Nardi, M., and Freedman, R. B. (1991) Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase Biochem. J. 275, 341-348
39. Liebler, D. C. (2008) Protein damage by reactive electrophiles: targets and consequences Chem. Res. Toxicol. 21, 117-128