Free radical reactions might contribute to severe alpha amanitin hepatotoxicity - A hypothesis

Medical Hypotheses

Volumn 69, Issue 2, 2007, Pages 361-367

  Zheleva, Antoaneta ^a   Tolekova, Anna ^a   Zhelev, Momchil ^b   Uzunova, Veselina ^a   Platikanova, Magdalena ^a   Gadzheva, Vesselina ^a  

^a TRAKIA UNIVERSITY   (Bulgaria)

^b Hospital of Mental Diseases   (Bulgaria)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMANITIN; ANTIOXIDANT; BETA AMANITIN; CATALASE; DNA DIRECTED RNA POLYMERASE III; FREE RADICAL; HYDROGEN PEROXIDE; LACTOPEROXIDASE; REACTIVE OXYGEN METABOLITE; RNA POLYMERASE II; SCAVENGER; SILIBININ; SUPEROXIDE; SUPEROXIDE DISMUTASE;

AMANITA PHALLOIDES; ARTICLE; CORRELATION ANALYSIS; DISEASE SEVERITY; ENZYME ACTIVITY; EUKARYOTIC CELL; HOMOGENATE; HUMAN; IC 50; LD 50; LIPID PEROXIDATION; LIVER CELL; LIVER TOXICITY; MEMBRANE STABILIZATION; MEMBRANE STRUCTURE; MOLECULAR INTERACTION; NONHUMAN; OXIDATION; OXIDATIVE STRESS; POISONOUS MUSHROOM; PRIORITY JOURNAL; STATISTICAL SIGNIFICANCE; ULTRAVIOLET SPECTROSCOPY;

AMANITINS; ANIMALS; CATALASE; ENZYME ACTIVATION; FREE RADICALS; LETHAL DOSE 50; LIVER; MALE; MICE; SUPEROXIDE DISMUTASE;

AMANITA PHALLOIDES; BASIDIOMYCOTA; EUKARYOTA; MUS;

EID: 34249286658     PISSN: 03069877     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mehy.2006.10.066     Document Type: Article

References (36)

1. Wieland Th. Peptides of poisonous Amanita mushrooms. In: Rich A. (Ed). Springer Series in Molecular Biology (1986), Springer-Verlag, New York
2. Beaudreuil S., Sharobeem R., Maitre F., Karsenti D., Grezard O., and Pierre D. Biopsy proven Amanita phalloides renal toxicity. Presse Med 27 28 (1998) 1434
3. Fiume L., and Stirpe F. Decreased RNA content in mouse liver nuclei after intoxication with alpha amanitin. Biochim Biophys Acta 123 (1966) 643-647
4. Seifart T., and Sekeris C.E. Alpha-amanitin, a specific inhibitor of transcription by mammalian RNA polymerase. Z Naturforsch B34 (1969) 1538-1542
5. Little M.C., and Preston J.F. Sensitivity of carrot cell cultures and RNA polymerase II to amatoxins. Evidence for the inactivation of 6′-hydroxyl-amatoxins. Plant Physiol 77 (1985) 443-449
6. Cadenas E., Simic M.G., and Sies H. Antioxidant activity of 5-hydroxytryptophan, 5-hydroxyindole, and DOPA against microsomal lipid peroxidation and its dependence on vitamin E. Free Rad Res Commun 6 1 (1989) 11-17
7. Zheleva A, Benov L, Zhelev Z. Effect of amatoxins on lipid peroxidation in model membranes. In: International conference on regulation of free radical reactions, 13-16 September, Varna, Bulgaria; 1989. 188.
8. Zheleva A., Benov L., and Zhelev Zh. Amanitin-induced toxicity may involve free radicals. Toxicon 28 2 (1990) 169
9. Ratty A.K., Sunamoto J., and Das N.P. Interaction of flavonoids with 1, 1-diphenyl-2-picrylhydrazyl free radical, liposomal membranes and soybean lipoxygenase-1. Biochem Pharmacol 37 6 (1988) 989-995
10. Zheleva A., Michelot D., Zhelev Z., Carpenter B., and Dobreva Z. Reactivity of the tryptathionin moiety of alpha-amanitin and implication in the toxic process. Toxicon 32 4 (1994) 410
11. Ghibaudi E.M., Laurenti E., Beltramo P., and Ferrari R.P. Can estrogenic radicals, generated by lactoperoxidase, be involved in the molecular mechanism of breast carcinogenesis?. Redox Rep 5 4 (2000) 229-235
12. Giles G.I., Tasker K.M., and Jacob C. Hypothesis: the role of reactive sulfur species in oxidative stress. Free Rad Biol Med 31 10 (2001) 1279-1283
13. Zhelev A.M., Michelot D., and Zhelev Zh.D. Sensitivity of alpha amanitin to oxidation by a lactoperoxidase-hydrogen peroxide system. Toxicon 38 8 (2000) 1055-1063
14. Southorn P.A., and Powis G. Free radicals in medicine. I. Chemical nature and biologic reactions. Mayo Clin Proc 63 (1988) 381-408
15. Fink-Gremmels J., Jalin A., and Blom M.J. Toxicity and metabolism of ochratoxin A. Nat Toxins 3 4 (1995) 214-220
16. Liu J., Yang C.F., Lee B.L., Shen H.M., Ang S.G., and Ong C.N. Effect of Salvia miltiorrhiza on alphatoxin B1-induced oxidative stress in cultured rat hepatocytes. Free Rad Res 31 6 (1999) 559-568
17. Diez-Fernandez C., Zaragoza A., Alvarez A., and Cascales M. Cocaine-cytotoxicity in hepatocyte cultures from Phenobarbital-induced rats: involvement of reactive oxygen species and expression of antioxidant defense systems. Biochem Pharmacol 58 (1999) 797-805
18. Esterbauer H., Gebicki J., Puhl H., and Jurgens G. The role of lipid peroxidation and antioxidants in oxidative modification on LDL. Free Rad Biol Med 13 (1992) 341-390
19. Mates J.M., Perez-Gomez C., and Nunez de Castro I. Antioxidant enzymes and human diseases. Clin Biochem 32 (1999) 595-603
20. Patterson R.A., and Leake D.S. Human serum, cysteine and histidine inhibit the oxidation of low density lipoprotein less at acidic pH. Febs Lett 434 (1998) 317-321
21. Prasad T., and Kundu M.S. Serum IgG and IgM responses to sheep red blood cells (SRBC) in weaned calves fedmilh supplemented with Zn and Cu. Nutrition 11 (1995) 712-715
22. Morikofer-Zwez S., Cantz M., Kaufmann H., von Wartburg J.P., and Aebi H. Heterogeneity of erythrocyte catalase. Correlations between sulfhydryl group content, chromatographic and electrophoretic properties. Eur J Biochem 11 1 (1969) 49-57
23. Deisseroth A., and Dounce A.L. Catalase: physical and chemical properties, mechanism of catalysis and physiological role. Physiol Rev 50 (1970) 319-375
24. Zheleva A., and Popova S. Antioxidant properties of Amanita phalloides mushroom toxins. Trakia J Sci 2 3 (2004) 28-30
25. Zheleva A., Gadjeva V., and Zhelev M. Free radical formation might contribute to the severe amatoxin hepatotoxicity. Trakia J Sci 1 3 (2003) 42-45
26. Wagner V.H., Diesel P., and Sietz M. Zur chemie und analytik von silymarin, aus Silybum marianum gaertn. Arzneim-Forsch 24 (1974) 466-471
27. Wellington K., and Jarvis B. Silymarin: a review of its clinical properties in the management of hepatic disorders. Biodrugs 15 7 (2001) 465-489
28. Gyorgy I., Antus S., Blazovics A., and Foldiak G. Substituent effects in the free radical reactions of silybin: radiation-induced oxidation of the flavonoid at neutral pH. Int J Radiat Biol 61 5 (1992) 603-609
29. Enjalbert F., Rapior S., Nouguier-Soule J., Guillon S., Amouroux N., and Cabot C. Treatment of amatoxins poisoning: 20-year retrospective analysis. J Toxicol-Clin Toxic 40 6 (2002) 715-757
30. Sun Y., Oberley L.W., and Li Y. A simple method for clinical assay of superoxide dismutase. Clin Nephrol 53 (1988) S9-S17
31. Johanson L.H., and Borg H.L.A. A spectrophotometric method for determination of catalase activity in small tissue sample. Anal Biochem 174 (1988) 331-336
32. Plaser Z.A., Cushman L.L., and Janson B.C. Estimation of product of lipid peroxidation (malonyl dialdehyde) in biochemical systems. Anal Biochem 16 (1966) 359-364
33. Spilkova J., and Dusek J. Natural substances with antioxidant activity. Ceska Slov Farm 45 6 (1996) 296-301
34. 2 Oxidoreductase. Reviews on structure and function of catalases. In: Biomolecules at Kenyon, 1997. www.callutheran.edu/Academic_Programs/Departments/BioDev/omm/catalase.
35. EI-Bahay C., Gerber E., Horbach M., Tran-Thi Q.H., Rohrdanz E., and Kahl R. Influence of tumor necrosis factor-alpha and silybin on the cytotoxic action of alpha-amanitin in rat hepatocyte culture. Toxicol Appl Pharmacol 158 3 (1999) 253-260
36. Sakagami H., and Satoh K. Prooxidant action of two antioxidants: ascorbic acid and gallic acid. Anticancer Res 17 1A (1997) 221-224