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Antioxidants and Phase 2 Enzymes in Cardiomyocytes: Chemical Inducibility and Chemoprotection Against Oxidant and Simulated Ischemia-Reperfusion Injury
Abstract
The increasing recognition of the role for oxidative stress in cardiac disorders has led to extensive investigation on the protection by exogenous antioxidants against oxidative cardiac injury. On the other hand, another strategy for protecting against oxidative cardiac injury may be through upregulation of the endogenous antioxidants and phase 2 enzymes in the myocardium by chemical inducers. However, our current understanding of the chemical inducibility of cardiac cellular antioxidants and phase 2 enzymes is very limited. In this study, using rat cardiac H9c2 cells we have characterized the concentration- and time-dependent induction of cellular antioxidants and phase 2 enzymes by 3H-1,2-dithiole-3-thione (D3T), and the resultant chemoprotective effects on oxidative cardiac cell injury. Incubation of H9c2 cells with D3T resulted in a marked concentration- and time-dependent induction of a number of cellular antioxidants and phase 2 enzymes, including catalase, reduced glutathione (GSH), GSH peroxidase, glutathione reductase (GR), GSH S-transferase (GST), and NAD(P)H:quinone oxidoreductase-1 (NQO1). D3T treatment of H9c2 cells also caused an increase in mRNA expression of catalase, gamma-glutamylcysteine ligase catalytic subunit, GR, GSTA1, M1 and P1, and NQO1. Moreover, both mRNA and protein expression of Nrf2 were induced in D3T-treated cells. D3T pretreatment led to a marked protection against H9c2 cell injury elicited by various oxidants and simulated ischemia-reperfusion. D3T pretreatment also resulted in decreased intracellular accumulation of reactive oxygen in H9c2 cells after exposure to the oxidants as well as simulated ischemia-reperfusion. This study demonstrates that a series of endogenous antioxidants and phase 2 enzymes in H9c2 cells can be induced by D3T in a concentration- and time-dependent fashion, and that the D3T-upregulated cellular defenses are accompanied by a markedly increased resistance to oxidative cardiac cell injury.
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Nrf2 protects cardiomyocytes from ROS-induced damage through the expression of antioxidant enzymes.
“Nrf2 has been shown to protect cardiomyocytes from ROS-induced damage through the expression of antioxidant enzymes [150,151]”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [150]
Citations
Cites
Aebi, H. (1984) · Methods in Enzymology · doi:10.1016/s0076-6879(84)05016-3 · Cited by 25,696
[12] Assays of glutathione peroxidase
Flohé, L., & Günzler, W. A. (1984) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(84)05015-1 · Cited by 4,954
Hayes, J. D., Flanagan, J. U., & Jowsey, I. R. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.095857 · Cited by 3,565
Role of Oxidative Modifications in Atherosclerosis
Stocker, R., & Keaney, J. F. (2004) · Physiological Reviews · doi:10.1152/physrev.00047.2003 · Cited by 2,646
Nrf2–Keap1 defines a physiologically important stress response mechanism
Motohashi, H., & Yamamoto, M. (2004) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2004.09.003 · Cited by 1,725
Cuzzocrea, S., Riley, D. P., Caputi, A. P., & Salvemini, D. (2001) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01484-4 · Cited by 1,087
An assay for superoxide dismutase activity in mammalian tissue homogenates
Spitz, D. R., & Oberley, L. W. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90192-9 · Cited by 751
Benson, A. M., Hunkeler, M. J., & Talalay, P. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.9.5216 · Cited by 750
Ross, D., Kepa, J. K., Winski, S. L., Beall, H. D., Anwar, A., & Siegel, D. M. (2000) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(00)00199-x · Cited by 621
Role of reactive aldehyde in cardiovascular diseases
Uchida, K. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00226-4 · Cited by 606
Kwak, M.-K., Itoh, K., Yamamoto, M. P., & Kensler, T. W. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.9.2883-2892.2002 · Cited by 597
Wheeler, C. R., Salzman, J. A., Elsayed, N. M., Omaye, S. T., & Korte, D. W. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90668-y · Cited by 548
Hescheler, J., Meyer, R., Plant, S., Krautwurst, D., Rosenthal, W., & Schultz, G. (1991) · Circulation Research · doi:10.1161/01.res.69.6.1476 · Cited by 523
Glutathione Peroxidase Protects against Peroxynitrite-mediated Oxidations
Sies, H., Sharov, V. S., Klotz, L., & Briviba, K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.44.27812 · Cited by 488
NAD(P)H:Quinone Oxidoreductase 1: Role as a Superoxide Scavenger
Siegel, D. M., Gustafson, D. L., Dehn, D. L., Han, J. Y., Boonchoong, P., Berliner, L. J., & Ross, D. (2004) · Molecular Pharmacology · doi:10.1124/mol.65.5.1238 · Cited by 455
Oxidative stress and cardiac disease
Lefer, D. J., & Granger, D. N. (2000) · The American Journal of Medicine · doi:10.1016/s0002-9343(00)00467-8 · Cited by 449
Antioxidant Vitamin Supplements and Cardiovascular Disease
Kris‐Etherton, P. M., Lichtenstein, A. H., Howard, B. V., Steinberg, D. H., & Witztum, J. L. (2004) · Circulation · doi:10.1161/01.cir.0000137822.39831.f1 · Cited by 409
Role of Glutathione S-Transferases in Protection against Lipid Peroxidation
Yang, Y., Cheng, J., Singhal, S. S., Saini, M. K., Pandya, U., Awasthi, S., & Awasthi, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100551200 · Cited by 312
Role of phase 2 enzyme induction in chemoprotection by dithiolethiones
Kwak, M.-K., Egner, P. A., Dolan, P. M., Ramos‐Gómez, M., Groopman, J. D., Itoh, K., Yamamoto, M. P., & Kensler, T. W. (2001) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(01)00190-7 · Cited by 241
Oxidative pathways in cardiovascular disease: roles, mechanisms, and therapeutic implications
Wattanapitayakul, S. K. (2001) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(00)00114-5 · Cited by 239
Cao, Z., & Li, Y. (2004) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2004.02.031 · Cited by 229
Self-citationChemical Carcinogenesis and Mutagenesis I
Cooper, C. S., & Grover, P. L. (1990) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-74775-5 · Cited by 227
Forgione, M. A., Cap, A., Liao, R., Moldovan, N. I., Eberhardt, R. T., Lim, C. C., Jones, J., Goldschmidt-Clermont, P. J., & Loscalzo, J. (2002) · Circulation · doi:10.1161/01.cir.0000026820.87824.6a · Cited by 200
Glutathione-Related Antioxidant Defenses in Human Atherosclerotic Plaques
Lapenna, D., de Gioia, S., Ciofani, G., Mezzetti, A., Ucchino, S., Calafiore, A. M., Napolitano, A. M., Ilio, C. D., & Cuccurullo, F. (1998) · Circulation · doi:10.1161/01.cir.97.19.1930 · Cited by 197
Turner, N. A., Xia, F., Azhar, G., Zhang, X., Liu, L., & Wei, J. Y. (1998) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1998.0743 · Cited by 193
Evaluation of the role of xanthine oxidase in myocardial reperfusion injury.
Thompson-Gorman, S. L., & Zweier, J. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39200-2 · Cited by 168
Self-citationMolavi, B., & Mehta, J. L. (2004) · Current Opinion in Cardiology · doi:10.1097/01.hco.0000133657.77024.bd · Cited by 160
Marchioli, R. (1999) · Pharmacological Research · doi:10.1006/phrs.1999.0480 · Cited by 130
Site-Specific Antiatherogenic Effect of Probucol in Apolipoprotein E–Deficient Mice
Witting, P. K., Pettersson, K. S., Letters, J., & Stocker, R. (2000) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.20.8.e26 · Cited by 92
Glutathione S-transferase overexpression protects against anthracycline-induced H9C2 cell death
L’Ecuyer, T. J., Allebban, Z., Thomas, R., & Heide, R. V. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00778.2003 · Cited by 74
Regulation of Necrosis of H9c2 Myogenic Cells upon Transient Energy Deprivation
Yaglom, J. A., Ekhterae, D., Gabai, V. L., & Sherman, M. Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306903200 · Cited by 71
Cao, Z. (2003) · Atherosclerosis · doi:10.1016/s0021-9150(02)00331-3 · Cited by 71
Self-citationCao, Z., Tsang, M., Hai, Z., & Li, Y. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.09.110 · Cited by 56
Self-citationClinical Toxicology: Principles and Mechanisms
Barile, F. A. (2003) · Thammasat University Digital Collections · Cited by 55
Xie, C. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00553-6 · Cited by 55
Zhu, H., Li, Y., & Trush, M. A. (1995) · Journal of Toxicology and Environmental Health · doi:10.1080/15287399509532028 · Cited by 36
Self-citationAnthracycline-induced cardiac injury using a cardiac cell line: potential for gene therapy studies.
L'ecuyer, T., Horenstein, M., Thomas, R. L., & Heide, R. V. (2001) · Molecular Genetics and Metabolism · doi:10.1006/mgme.2001.3243 · Cited by 36
New understanding in cardiotoxicity.
Yj, K. (2003) · PubMed · Cited by 21
Cao, Z., & Li, Y. (2004) · Cardiovascular Toxicology · doi:10.1385/ct:4:4:339 · Cited by 19
Self-citation
Flagged first, then by citations
Research works printed but not linked: 2
- Kang YJ, 2003, Curr Opin Drug Discov Devel, 6, 110
- L'ecuyer T, 2004, Am J Physiol, 286, H2057
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Oxidative stress in health and disease: The therapeutic potential of Nrf2 activation
Hybertson, B. M., Gao, B., Bose, S. K., & McCord, J. M. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.10.006 · Cited by 1,046
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Tengattini, S., Reiter, R. J., Tan, D., Terrón, M. P., Rodella, L. F., & Rezzani, R. (2007) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2007.00518.x · Cited by 340
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Nrf2 and Cardiovascular Defense
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Angeloni, C., Leoncini, E., Malaguti, M., Angelini, S., Hrelia, P., & Hrelia, S. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf900549c · Cited by 117
Sulforaphane prevents age‐associated cardiac and muscular dysfunction through Nrf2 signaling
Bose, C., Alves, I., Singh, P., Palade, P., Carvalho, E., Børsheim, E., Jun, S., Cheema, A. K., Boerma, M., Awasthi, S., et al. (2020) · Aging Cell · doi:10.1111/acel.13261 · Cited by 113
Zhai, X., Chen, X., Shi, J., Shi, D., Ye, Z., Liu, W., Li, M., Wang, Q., Kang, Z., Bi, H., et al. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.004 · Cited by 101
Zhu, H., Jia, Z., Strobl, J. S., Ehrich, M. F., Misra, H. P., & Li, Y. (2008) · Cardiovascular Toxicology · doi:10.1007/s12012-008-9020-4 · Cited by 89
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Metadata
- Authors
- Cao, Z., Zhu, H., Zhang, L., Zhao, X., Zweier, J. L., & Li, Y.
- Affiliations
- The Ohio State University Wexner Medical Center (US)
- Second Military Medical University (CN)
- Corresponding author
- Li, Yunbo
- Venue
- Experimental Biology and Medicine
- Publisher
- Frontiers Media SA
- Published
- 2006-09
- Volume
- 231
- Issue
- 8
- Pages
- 1353-1364
- ISSN
- 0071-3384 (ISSN-L)
- 1535-3702
- 1535-3699
- OpenAlex
- W2338214197
- Cited by
- 56
- References
- 39
- Citations by year
- 2024: 1 · 2022: 3 · 2021: 3 · 2020: 2 · 2019: 4 · 2018: 2 · 2017: 4 · 2016: 3 · 2015: 2 · 2014: 2 · 2013: 7 · 2012: 1
- FWCI
- 2.04
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Experimental Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL-38324, R01HL063744, HL 65608, P01HL065608, HL 63744, R01HL071190, HL71190)
- National Cancer Institute (R15CA091895, CA91895)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Ischemia and Reperfusion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- 3H-1,2-dithiole-3-thione, chemical induction, phase II enzymes, endogenous antioxidants, cardioprotection, oxidative stress, ischemia-reperfusion injury, Nrf2, catalase, glutathione, glutathione S-transferase, NQO1, glutathione reductase, H9c2 cells, reactive oxygen species, chemoprotection
- MeSH terms
- Animals, Antioxidants, Catalase, Cell Line, Glutathione, Glutathione Peroxidase, Glutathione Reductase, Glutathione Transferase, RNA, Messenger, Superoxide Dismutase, Thiones, Blotting, Western, Reperfusion Injury, NAD(P)H Dehydrogenase (Quinone), Oxidants, Oxidative Stress, Reverse Transcriptase Polymerase Chain Reaction, Myocytes, Cardiac, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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