Effects of Epigallocatechin Gallate on Tert-Butyl Hydroperoxide-Induced Mitochondrial Dysfunction in Rat Liver Mitochondria and Hepatocytes

. 2016 ; 2016 () : 7573131. [epub] 20161215

Jazyk angličtina Země Spojené státy americké Médium print-electronic

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid28074116

Epigallocatechin gallate (EGCG) is a green tea antioxidant with adverse effects on rat liver mitochondria and hepatocytes at high doses. Here, we assessed whether low doses of EGCG would protect these systems from damage induced by tert-butyl hydroperoxide (tBHP). Rat liver mitochondria or permeabilized rat hepatocytes were pretreated with EGCG and then exposed to tBHP. Oxygen consumption, mitochondrial membrane potential (MMP), and mitochondrial retention capacity for calcium were measured. First, 50 μM EGCG or 0.25 mM tBHP alone increased State 4 Complex I-driven respiration, thus demonstrating uncoupling effects; tBHP also inhibited State 3 ADP-stimulated respiration. Then, the coexposure to 0.25 mM tBHP and 50 μM EGCG induced a trend of further decline in the respiratory control ratio beyond that observed upon tBHP exposure alone. EGCG had no effect on MMP and no effect, in concentrations up to 50 μM, on mitochondrial calcium retention capacity. tBHP led to a decline in both MMP and mitochondrial retention capacity for calcium; these effects were not changed by pretreatment with EGCG. In addition, EGCG dose-dependently enhanced hydrogen peroxide formation in a cell- and mitochondria-free medium. Conclusion. Moderate nontoxic doses of EGCG were not able to protect rat liver mitochondria and hepatocytes from tBHP-induced mitochondrial dysfunction.

Zobrazit více v PubMed

Yoshino K., Hara Y., Sano M., Tomita I. Antioxidative effects of black tea theaflavins and thearubigin on lipid peroxidation of liver homogenates induced by tert-butyl hydroperoxide. Biological and Pharmaceutical Bulletin. 1994;17(1):146–149. doi: 10.1248/bpb.17.146. PubMed DOI

Na H.-K., Surh Y.-J. Modulation of Nrf2-mediated antioxidant and detoxifying enzyme induction by the green tea polyphenol EGCG. Food and Chemical Toxicology. 2008;46(4):1271–1278. doi: 10.1016/j.fct.2007.10.006. PubMed DOI

Wang Y., Mei Y., Feng D., Xu L. (−)-Epigallocatechin-3-gallate protects mice from concanavalin A-induced hepatitis through suppressing immune-mediated liver injury. Clinical and Experimental Immunology. 2006;145(3):485–492. doi: 10.1111/j.1365-2249.2006.03137.x. PubMed DOI PMC

Sahin K., Tuzcu M., Gencoglu H., et al. Epigallocatechin-3-gallate activates Nrf2/HO-1 signaling pathway in cisplatin-induced nephrotoxicity in rats. Life Sciences. 2010;87(7-8):240–245. doi: 10.1016/j.lfs.2010.06.014. PubMed DOI

Tipoe G. L., Leung T. M., Liong E. C., Lau T. Y. H., Fung M. L., Nanji A. A. Epigallocatechin-3-gallate (EGCG) reduces liver inflammation, oxidative stress and fibrosis in carbon tetrachloride (CCl4)-induced liver injury in mice. Toxicology. 2010;273(1–3):45–52. doi: 10.1016/j.tox.2010.04.014. PubMed DOI

Lambert J. D., Elias R. J. The antioxidant and pro-oxidant activities of green tea polyphenols: a role in cancer prevention. Archives of Biochemistry and Biophysics. 2010;501(1):65–72. doi: 10.1016/j.abb.2010.06.013. PubMed DOI PMC

Romeo L., Intrieri M., D'Agata V., et al. The major green tea polyphenol, (-)-epigallocatechin-3-gallate, induces heme oxygenase in rat neurons and acts as an effective neuroprotective agent against oxidative stress. The Journal of the American College of Nutrition. 2009;28(supplement 4):492S–499S. doi: 10.1080/07315724.2009.10718116. PubMed DOI

Kucera O., Mezera V., Moravcova A., et al. In vitro toxicity of epigallocatechin gallate in rat liver mitochondria and hepatocytes. Oxidative Medicine and Cellular Longevity. 2015;2015:10. doi: 10.1155/2015/476180.476180 PubMed DOI PMC

Brand M. D., Affourtit C., Esteves T. C., et al. Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins. Free Radical Biology and Medicine. 2004;37(6):755–767. doi: 10.1016/j.freeradbiomed.2004.05.034. PubMed DOI

Mookerjee S. A., Divakaruni A. S., Jastroch M., Brand M. D. Mitochondrial uncoupling and lifespan. Mechanisms of Ageing and Development. 2010;131(7-8):463–472. doi: 10.1016/j.mad.2010.03.010. PubMed DOI PMC

Galati G., Lin A., Sultan A. M., O'Brien P. J. Cellular and in vivo hepatotoxicity caused by green tea phenolic acids and catechins. Free Radical Biology and Medicine. 2006;40(4):570–580. doi: 10.1016/j.freeradbiomed.2005.09.014. PubMed DOI

Schmidt M., Schmitz H.-J., Baumgart A., et al. Toxicity of green tea extracts and their constituents in rat hepatocytes in primary culture. Food and Chemical Toxicology. 2005;43(2):307–314. doi: 10.1016/j.fct.2004.11.001. PubMed DOI

Mezera V., Kucera O., Moravcova A., Peterova E., Cervinkova Z. The effect of epigallocatechin gallate on hepatocytes isolated from normal and partially hepatectomized rats. Canadian Journal of Physiology and Pharmacology. 2014;92(6):512–517. doi: 10.1139/cjpp-2014-0069. PubMed DOI

Li W., Nie S., Yu Q., Xie M. Y. (-)-epigallocatechin-3-gallate induces apoptosis of human hepatoma cells by mitochondrial pathways related to reactive oxygen species. Journal of Agricultural and Food Chemistry. 2009;57(15):6685–6691. doi: 10.1021/jf901396f. PubMed DOI

Serrano J. C. E., Gonzalo-Benito H., Jové M., et al. Dietary intake of green tea polyphenols regulates insulin sensitivity with an increase in AMP-activated protein kinase α content and changes in mitochondrial respiratory complexes. Molecular Nutrition and Food Research. 2013;57(3):459–470. doi: 10.1002/mnfr.201200513. PubMed DOI

Meng Q., Velalar C. N., Ruan R. Regulating the age-related oxidative damage, mitochondrial integrity, and antioxidative enzyme activity in Fischer 344 rats by supplementation of the antioxidant epigallocatechin-3-gallate. Rejuvenation Research. 2008;11(3):649–660. doi: 10.1089/rej.2007.0645. PubMed DOI

Liu J., Tang Y., Feng Z., Liu J., Liu J., Long J. (−)-Epigallocatechin-3-gallate attenuated myocardial mitochondrial dysfunction and autophagy in diabetic Goto-Kakizaki rats. Free Radical Research. 2014;48(8):898–906. doi: 10.3109/10715762.2014.920955. PubMed DOI

Miltonprabu S., Thangapandiyan S. Epigallocatechin gallate potentially attenuates Fluoride induced oxidative stress mediated cardiotoxicity and dyslipidemia in rats. Journal of Trace Elements in Medicine and Biology. 2015;29:321–335. doi: 10.1016/j.jtemb.2014.08.015. PubMed DOI

Crispo J. A. G., Ansell D. R., Piche M., et al. Protective effects of polyphenolic compounds on oxidative stress-induced cytotoxicity in PC12 cells. Canadian Journal of Physiology and Pharmacology. 2010;88(4):429–438. doi: 10.1139/Y09-137. PubMed DOI

Nakagawa T., Yokozawa T. Direct scavenging of nitric oxide and superoxide by green tea. Food and Chemical Toxicology. 2002;40(12):1745–1750. doi: 10.1016/S0278-6915(02)00169-2. PubMed DOI

Nakagawa H., Hasumi K., Woo J.-T., Nagai K., Wachi M. Generation of hydrogen peroxide primarily contributes to the induction of Fe(II)-dependent apoptosis in Jurkat cells by (−)-epigallocatechin gallate. Carcinogenesis. 2004;25(9):1567–1574. doi: 10.1093/carcin/bgh168. PubMed DOI

Long L. H., Clement M. V., Halliwell B. Artifacts in cell culture: Rapid generation of hydrogen peroxide on addition of (−)-epigallocatechin, (−)-epigallocatechin gallate, (+)-catechin, and quercetin to commonly used cell culture media. Biochemical and Biophysical Research Communications. 2000;273(1):50–53. doi: 10.1006/bbrc.2000.2895. PubMed DOI

Chance B., Sies H., Boveris A. Hydroperoxide metabolism in mammalian organs. Physiological Reviews. 1979;59(3):527–605. PubMed

Sies H., Moss K. M. A role of mitochondrial glutathione peroxidase in modulating mitochondrial oxidations in liver. European Journal of Biochemistry. 1978;84(2):377–383. doi: 10.1111/j.1432-1033.1978.tb12178.x. PubMed DOI

Endlicher R., Křiváková P., Rauchová H., Nůsková H., Červinková Z., Drahota Z. Peroxidative damage of mitochondrial respiration is substrate-dependent. Physiological Research. 2009;58(5):685–692. PubMed

Drahota Z., Křiváková P., Červinková Z., et al. Tert-butyl hydroperoxide selectively inhibits mitochondrial respiratory-chain enzymes in isolated rat hepatocytes. Physiological Research. 2005;54(1):67–72. PubMed

Melov S., Coskun P., Patel M., et al. Mitochondrial disease in superoxide dismutase 2 mutant mice. Proceedings of the National Academy of Sciences of the United States of America. 1999;96(3):846–851. doi: 10.1073/pnas.96.3.846. PubMed DOI PMC

Murakami C., Hirakawa Y., Inui H., Nakano Y., Yoshida H. Effect of tea catechins on cellular lipid peroxidation and cytotoxicity in HepG2 cells. Bioscience, Biotechnology and Biochemistry. 2002;66(7):1559–1562. doi: 10.1271/bbb.66.1559. PubMed DOI

Fernández-Iglesias A., Quesada H., Díaz S., et al. DHA sensitizes FaO cells to tert-BHP-induced oxidative effects. Protective role of EGCG. Food and Chemical Toxicology. 2013;62:750–757. doi: 10.1016/j.fct.2013.10.013. PubMed DOI

Braud L., Peyre L., de-Sousa G., Armand M., Rahmani R., Maixent J.-M. Effect of brewing duration on the antioxidant and hepatoprotective abilities of tea phenolic and alkaloid compounds in a t-BHP oxidative stress-induced rat hepatocyte model. Molecules. 2015;20(8):14985–15002. doi: 10.3390/molecules200814985. PubMed DOI PMC

Červinková Z., Křiváková P., Lábajová A., et al. Mechanisms participating in oxidative damage of isolated rat hepatocytes. Archives of Toxicology. 2009;83(4):363–372. doi: 10.1007/s00204-008-0385-8. PubMed DOI

Bustamante E., Soper J. W., Pedersen P. L. A high-yield preparative method for isolation of rat liver mitochondria. Analytical Biochemistry. 1977;80(2):401–408. doi: 10.1016/0003-2697(77)90661-3. PubMed DOI

Drahota Z., Palenickova E., Endlicher R., et al. Biguanides inhibit complex I, II and IV of rat liver mitochondria and modify their functional properties. Physiological Research. 2014;63(1):1–11. PubMed

Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry. 1976;72(1-2):248–254. doi: 10.1016/0003-2697(76)90527-3. PubMed DOI

Kuznetsov A. V., Schneeberger S., Seiler R., et al. Mitochondrial defects and heterogeneous cytochrome c release after cardiac cold ischemia and reperfusion. American Journal of Physiology—Heart and Circulatory Physiology. 2004;286(5):H1633–H1641. doi: 10.1152/ajpheart.00701.2003. PubMed DOI

Kučera O., Endlicher R., Roušar T., et al. The effect of tert-butyl hydroperoxide-induced oxidative stress on lean and steatotic rat hepatocytes in vitro . Oxidative Medicine and Cellular Longevity. 2014;2014:12. doi: 10.1155/2014/752506.752506 PubMed DOI PMC

Staňková P., Kučera O., Lotková H., Roušar T., Endlicher R., Červinková Z. The toxic effect of thioacetamide on rat liver in vitro. Toxicology in Vitro. 2010;24(8):2097–2103. doi: 10.1016/j.tiv.2010.06.011. PubMed DOI

Åkerman K. E. O., Wikström M. K. F. Safranine as a probe of the mitochondrial membrane potential. FEBS Letters. 1976;68(2):191–197. doi: 10.1016/0014-5793(76)80434-6. PubMed DOI

Drahota Z., Endlicher R., Staňková P., Rychtrmoc D., Milerová M., Červinková Z. Characterization of calcium, phosphate and peroxide interactions in activation of mitochondrial swelling using derivative of the swelling curves. Journal of Bioenergetics and Biomembranes. 2012;44(3):309–315. doi: 10.1007/s10863-012-9443-2. PubMed DOI

Ichas F., Jouaville L. S., Mazat J.-P. Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals. Cell. 1997;89(7):1145–1153. doi: 10.1016/S0092-8674(00)80301-3. PubMed DOI

Fontaine E., Eriksson O., Ichas F., Bernardi P. Regulation of the permeability transition pore in skeletal muscle mitochondria. Modulation by electron flow through the respiratory chain complex I. The Journal of Biological Chemistry. 1998;273(20):12662–12668. doi: 10.1074/jbc.273.20.12662. PubMed DOI

Krumschnabel G., Fontana-Ayoub M., Sumbalova Z., et al. Simultaneous high-resolution measurement of mitochondrial respiration and hydrogen peroxide production. Methods in Molecular Biology. 2015;1264:245–261. doi: 10.1007/978-1-4939-2257-4_22. PubMed DOI

Serrano J., Jové M., Boada J., Bellmunt M. J., Pamplona R., Portero-Otín M. Dietary antioxidants interfere with Amplex Red-coupled-fluorescence assays. Biochemical and Biophysical Research Communications. 2009;388(2):443–449. doi: 10.1016/j.bbrc.2009.08.041. PubMed DOI

Brand M. D., Nicholls D. G. Assessing mitochondrial dysfunction in cells. Biochemical Journal. 2011;435(2):297–312. doi: 10.1042/BJ20110162. PubMed DOI PMC

Orr A. L., Ashok D., Sarantos M. R., Shi T., Hughes R. E., Brand M. D. Inhibitors of ROS production by the ubiquinone-binding site of mitochondrial complex i identified by chemical screening. Free Radical Biology and Medicine. 2013;65:1047–1059. doi: 10.1016/j.freeradbiomed.2013.08.170. PubMed DOI PMC

Weng Z., Zhou P., Salminen W. F., et al. Green tea epigallocatechin gallate binds to and inhibits respiratory complexes in swelling but not normal rat hepatic mitochondria. Biochemical and Biophysical Research Communications. 2014;443(3):1097–1104. doi: 10.1016/j.bbrc.2013.12.110. PubMed DOI

Gnaiger E. Capacity of oxidative phosphorylation in human skeletal muscle: new perspectives of mitochondrial physiology. International Journal of Biochemistry and Cell Biology. 2009;41(10):1837–1845. doi: 10.1016/j.biocel.2009.03.013. PubMed DOI

Hepple R. T. Mitochondrial involvement and impact in aging skeletal muscle. Frontiers in Aging Neuroscience. 2014;6, article no. 211 doi: 10.3389/fnagi.2014.00211. PubMed DOI PMC

Najít záznam

Citační ukazatele

Nahrávání dat ...

Možnosti archivace

Nahrávání dat ...