NADH-generating substrates reduce peroxyl radical toxicity in RL-34 cells

• Autorzy: Antosiewicz J , Spodnik J.H. , Teranishi M. , Herman-Antosiewicz A. , Kurono C. , Soji T. , Wozniak M. , Borkowska A. , Wakabayashi T.
• Języki publikacji: EN

Abstrakty

EN

There is general agreement that oxidative stress may induce apoptotic and necrotic cell death. Recently it has been shown that NADH can be considered an important antioxidant as it reacts with peroxyl and alkoxyl radicals under in vitro conditions. Therefore, in the present study we hypothesized that an increase in intracellular NADH using specific substrates will protect RL-34 cells against cytotoxicity of 2’-azobis (2-amidinopropane) dihydrochloride (AAPH), which is a peroxyl radical generating compound. Cells treated for 24 hours with 6.0 mM AAPH were severely damaged: mitochondria were vacuolated, and the level of free radicals significantly increased. Both apoptotic and necrotic cells were detected (11.1% and 11.4%, respectively) even after 5 hours of treatment. Pretreatment of the cells with substrates which increase the intracellular level of NADH, such as lactate, beta-hydroxybutyrate, and ethanol, distinctly inhibited AAPH-induced reactive oxygen species (ROS) formation and cell death. On the other hand, acetoacetate (AcA), which decrease the intracellular level of NADH, had opposite effects. Interestingly, NADH-generating substrates augment, while AcA reduced superoxide radical formation induced by AAPH. These results may suggest that although NADH generating substrates may exert some deleterious effects within a cell by inducing reductive stress, they diminish alkoxyl or peroxyl radical cytotoxicity. The protection is associated with a decrease in ROS formation measured by dichlorofluorescein, but with an increase in superoxide radical formation. (Folia Morphol 2009; 68, 4: 247–255)

Słowa kluczowe

EN

2'-azobis [2-amidinopropane] dihydrochloride; oxidative stress; reactive oxygen species; ethanol; apoptosis; nicotinamide adenine dinucleotide; peroxyl; toxicity; free radical

• Wydawca: -
• Czasopismo: Folia Morphologica
• Rocznik: 2009
• Tom: 68
• Numer: 4
• Opis fizyczny: p.247-255,fig.,ref.

Twórcy

autor

Antosiewicz J

• Medical University of Gdansk, Debinki 1, 80-210 Gdansk, Poland

autor

Spodnik J.H.

autor

Teranishi M.

autor

Herman-Antosiewicz A.

autor

Kurono C.

autor

Soji T.

autor

Wozniak M.

autor

Borkowska A.

autor

Wakabayashi T.

Bibliografia

• 1. Antosiewicz J, Herman-Antosiewicz A, Marynowski SW, Singh SV (2006) c-Jun NH(2)-terminal kinase signaling axis regulates diallyl trisulfide-induced generation of reactive oxygen species and cell cycle arrest in human prostate cancer cells. Cancer Res, 66: 5379–5386.
• 2. Antosiewicz J, Nishizawa Y, Liu X, Usukura J, Wakabayashi T (1994) Suppression of the hydrazine-induced formation of megamitochondria in the rat liver by alpha-tocopherol. Exp Mol Pathol, 60: 173–187.
• 3. Bodaness RS, Chan PC (1977) Singlet oxygen as a mediator in the hematoporphyrin-catalyzed photooxidation of NADPH to NADP+ in deuterium oxide. J Biol Chem, 252: 8554–8560.
• 4. Buege JA, Aust SD (1978) Microsomal lipid peroxidation. Methods Enzymol, 52: 302–310.
• 5. Chan PC, Bielski BH (1974) Enzyme-catalyzed free radical reactions with nicotinamide adenine nucleotides. II. Lactate dehydrogenase-catalyzed oxidation of reduced nicotinamide adenine dinucleotide by superoxide radicals generated by xanthine oxidase. J Biol Chem, 249: 1317–1319.
• 6. Chan PC, Bielski BH (1975) Lactate dehydrogenase-catalyzed stereospecific hydrogen atom transfer from reduced nicotinamide adenine dinucleotide to dicarboxylate radicals. J Biol Chem, 250: 7266–7271.
• 7. Forni LG, Willson RL (1986) Thiyl and phenoxyl free radicals and NADH. Direct observation of one-electron oxidation. Biochem J, 240: 897–903.
• 8. Hausladen A, Fridovich I (1994) Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not. J Biol Chem, 269: 29405–29408.
• 9. Kamata H, Honda S, Maeda S, Chang L, Hirata H, Karin M (2005) Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell, 120: 649–661.
• 10. Karbowski M, Kurono C, Wozniak M, Ostrowski M, Teranishi M, Nishizawa Y, Usukura J, Soji T, Wakabayashi T (1999) Free radical-induced megamitochondria formation and apoptosis. Free Radic Biol Med, 26: 396–409.
• 11. Khan S, O’Brien PJ (1995) Modulating hypoxia-induced hepatocyte injury by affecting intracellular redox state. Biochim Biophys Acta,1269:153–161.
• 12. Kirsch M, de Groot H (1999) Reaction of peroxynitrite with reduced nicotinamide nucleotides, the formation of hydrogen peroxide. J Biol Chem, 274: 24664–24670.
• 13. Kirsch M, De Groot H (2001) NAD(P)H, a directly operating antioxidant? Faseb J, 15: 1569–1574.
• 14. Kuo WY, Tang TK (1998) Effects of G6PD overexpression in NIH3T3 cells treated with tert-butyl hydroperoxide or paraquat. Free Radic Biol Med, 24: 1130–1138.
• 15. Lee YJ, Kim JH, Chen J, Song JJ (2002) Enhancement of metabolic oxidative stress-induced cytotoxicity by the thioredoxin inhibitor 1-methylpropyl 2-imidazolyl disulfide is mediated through the ASK1-SEK1-JNK1 pathway. Mol Pharmacol, 62: 1409–1417.
• 16. Li X, Zhang R, Luo D, Park SJ, Wang Q, Kim Y, Min W (2005) Tumor necrosis factor alpha-induced desumoylation and cytoplasmic translocation of homeodomaininteracting protein kinase 1 are critical for apoptosis signal-regulating kinase 1-JNK/p38 activation. J Biol Chem, 280: 15061–15070.
• 17. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem, 193: 265–275.
• 18. Niki E (1990) Free radical initiators as source of wateror lipid-soluble peroxyl radicals. Methods Enzymol, 186: 100–108.
• 19. Nishida M, Schey KL, Takagahara S, Kontani K, Katada T, Urano Y, Nagano T, Nagao T, Kurose H (2002) Activation mechanism of Gi and Go by reactive oxygen species. J Biol Chem, 277: 9036–9042.
• 20. Olek RA, Ziolkowski W, Kaczor JJ, Greci L, Popinigis J, Antosiewicz J (2004) Antioxidant activity of NADH and its analogue — an in vitro study. J Biochem Mol Biol, 37: 416–421.
• 21. Petrat F, Pindiur S, Kirsch M, de Groot H (2003) NAD(P)H, a primary target of 1O2 in mitochondria of intact cells. J Biol Chem, 278: 3298–3307.
• 22. Ursini F, Zamburlini A, Cazzolato G, Maiorino M, Bon GB, Sevanian A (1998) Postprandial plasma lipid hydroperoxides: a possible link between diet and atherosclerosis. Free Radic Biol Med, 25: 250–252.
• 23. Ventura JJ, Kennedy NJ, Lamb JA, Flavell RA, Davis RJ (2003) c-Jun NH(2)-terminal kinase is essential for the regulation of AP-1 by tumor necrosis factor. Mol Cell Biol, 23: 2871–2882.
• 24. Watabe S, Wada S, Saito S, Matsunaga S, Fusetani N, Ozaki H, Karaki H (1996) Cellular changes of rat embryonic fibroblasts by an actin-polymerization inhibitor, bistheonellide A, from a marine sponge. Cell Struct Funct, 21: 199–212.
• 25. Xiao D, Herman-Antosiewicz A, Antosiewicz J, Xiao H, Brisson M, Lazo JS, Singh SV (2005) Diallyl trisulfideinduced G(2)-M phase cell cycle arrest in human prostate cancer cells is caused by reactive oxygen species-dependent destruction and hyperphosphorylation of Cdc 25 C. Oncogene, 24: 6256–6268.
• 26. Zerez CR, Lee SJ, Tanaka KR (1987) Spectrophotometric determination of oxidized and reduced pyridine nucleotides in erythrocytes using a single extraction procedure. Anal Biochem, 164: 367–373.