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Calcium, ATP, and ROS: a mitochondrial love-hate triangle
Abstract
The mitochondrion is at the core of cellular energy metabolism, being the site of most ATP generation. Calcium is a key regulator of mitochondrial function and acts at several levels within the organelle to stimulate ATP synthesis. However, the dysregulation of mitochondrial Ca(2+) homeostasis is now recognized to play a key role in several pathologies. For example, mitochondrial matrix Ca(2+) overload can lead to enhanced generation of reactive oxygen species, triggering of the permeability transition pore, and cytochrome c release, leading to apoptosis. Despite progress regarding the independent roles of both Ca(2+) and mitochondrial dysfunction in disease, the molecular mechanisms by which Ca(2+) can elicit mitochondrial dysfunction remain elusive. This review highlights the delicate balance between the positive and negative effects of Ca(2+) and the signaling events that perturb this balance. Overall, a "two-hit" hypothesis is developed, in which Ca(2+) plus another pathological stimulus can bring about mitochondrial dysfunction.
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“Peroxides produced by mitochondria can create nonenzymatic shunts in the TCA cycle (56, 121).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [56]
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“In turn, an increased Ca 2ϩ load in the mitochondrial matrix has been linked to increased ROS production and increased permeability transition pore opening, leading to apoptosis (40,45).”
From Simvastatin Effects on Skeletal Muscle (2013) · cites this paper as [45]
Citations
Cites
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Green, D. R., & Reed, J. C. (1998) · Science · doi:10.1126/science.281.5381.1309 · Cited by 9,051
Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084
Nitric oxide synthases: structure, function and inhibition
ALDERTON, W. K., COOPER, C. E., & KNOWLES, R. G. (2001) · Biochemical Journal · doi:10.1042/bj3570593 · Cited by 4,110
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
The mitochondrial permeability transition pore and its role in cell death
CROMPTON, M. (1999) · Biochemical Journal · doi:10.1042/bj3410233 · Cited by 2,432
Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178
Nitric oxide mediates glutamate neurotoxicity in primary cortical cultures.
Dawson, V. L., Dawson, T. M., London, E. D., Bredt, D. S., & Snyder, S. H. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.14.6368 · Cited by 2,174
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Gupta, S., Bhatia, V., Wen, J.-J., Wu, Y., Huang, M.-H., & Garg, N. J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.08.008 · Cited by 120
Wojtovich, A. P., & Brookes, P. S. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.025 · Cited by 119
Self-citationValvassori, S. S., Rezin, G. T., Ferreira, C. L., Moretti, M., Gonçalves, C. L., Cardoso, M. R., STRECK, E. L., Kapczinski, F. P., & Quevedo, J. (2010) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2010.02.009 · Cited by 121
Targeting post-mitochondrial effectors of apoptosis for neuroprotection
Galluzzi, L., Morselli, E., Kepp, O., & Kroemer, G. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.09.006 · Cited by 123
Mehta, A. K., & Shaha, C. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.01.024 · Cited by 119
Pathophysiological mechanisms in acute pancreatitis: Current understanding
Singh, P., & Garg, P. K. (2016) · Indian Journal of Gastroenterology · doi:10.1007/s12664-016-0647-y · Cited by 118
CGI1746 targets σ1R to modulate ferroptosis through mitochondria-associated membranes
Zhang, Z., Zhou, H., Gu, W., Wei, Y., Mou, S., Wang, Y., Zhang, J., & Zhong, Q. (2024) · Nature Chemical Biology · doi:10.1038/s41589-023-01512-1 · Cited by 126
Mitochondria: A target for bacteria
Lobet, E., Letesson, J., & Arnould, T. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.02.007 · Cited by 117
Espino, J., Bejarano, I., Redondo, P. C., Rosado, J. A., Barriga, C., Reiter, R. J., Pariente, J. A., & Rodríguez, A. B. (2010) · The Journal of Membrane Biology · doi:10.1007/s00232-010-9230-0 · Cited by 115
The role of calcium in VDAC1 oligomerization and mitochondria-mediated apoptosis
Keinan, N., Pahima, H. T., Ben-Hail, D., & Shoshan‐Barmatz, V. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.03.017 · Cited by 116
Aldakkak, M., Camara, A. K. S., Heisner, J. S., Yang, M., & Stowe, D. F. (2011) · Pharmacological Research · doi:10.1016/j.phrs.2011.06.018 · Cited by 116
Decreased Neuronal Death in Na+/H+Exchanger Isoform 1-Null Mice afterIn VitroandIn VivoIschemia
Luo, J., Chen, H., Kintner, D. B., Shull, G. E., & Sun, D. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3271-05.2005 · Cited by 115
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Zhao, X., Li, G.-Z., Liu, Y., Chai, L., Chen, J., Zhang, Y., Du, Z., Lu, Y., & Yang, B. (2008) · British Journal of Pharmacology · doi:10.1038/bjp.2008.81 · Cited by 116
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Chaurasia, M., Bhatt, A. N., Das, A., Dwarakanath, B. S. R., & Sharma, K. (2016) · Free Radical Research · doi:10.3109/10715762.2015.1129534 · Cited by 119
Miyake, T., Nakamura, S., Zhao, M., So, K., Inoue, K., Numata, T., Takahashi, N., Shirakawa, H., Mori, Y., Nakagawa, T., et al. (2016) · Nature Communications · doi:10.1038/ncomms12840 · Cited by 119
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Shkryl, V. M., Martins, A. S., Ullrich, N. D., Nowycky, M. C., Niggli, E., & Shirokova, N. (2009) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0670-2 · Cited by 120
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Pickrell, A. M., Fukui, H., Wang, X., Pinto, M., & Moraes, C. T. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6223-10.2011 · Cited by 114
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Quintanilla, R. A., Jin, Y. N., von Bernhardi, R., & Johnson, G. V. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-45 · Cited by 108
Tian, J., Wang, Y., Lu, Z., Sun, C., Zhang, M., Zhu, A., & Peng, X. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6b03546 · Cited by 114
Xue, J., Li, R., Zhao, X., Ma, C., Lv, X., Liu, L., & Liu, P. (2018) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2018.02.003 · Cited by 114
Exercise-induced rhabdomyolysis mechanisms and prevention: A literature review
Kim, J., Lee, J., Kim, S., Ryu, H. Y., Cha, K. S., & Sung, D. J. (2015) · Journal of sport and health science/Journal of Sport and Health Science · doi:10.1016/j.jshs.2015.01.012 · Cited by 113
Streptomycin reduces stretch-induced membrane permeability in muscles from mdx mice
Whitehead, N. P., Streamer, M., Lusambili, L. I., Sachs, F., & Allen, D. G. (2006) · Neuromuscular Disorders · doi:10.1016/j.nmd.2006.07.024 · Cited by 112
Miyake, T., Shirakawa, H., Nakagawa, T., & Kaneko, S. (2015) · Glia · doi:10.1002/glia.22854 · Cited by 118
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Dedkova, E. N., & Blatter, L. A. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.08.030 · Cited by 118
Zhang, D., Liu, J.-S., Tang, M.-K., Yiu, A., Cao, H., Jiang, L., Chan, J. Y., Tian, H., Fung, K., & Ye, W. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.06.045 · Cited by 112
Nagy, E., Andersson, D. C., Caidahl, K., Eriksson, M. J., Eriksson, P. O., Franco‐Cereceda, A., Hansson, G. K., & Bäck, M. (2011) · Circulation · doi:10.1161/circulationaha.110.966846 · Cited by 112
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Cillero‐Pastor, B., Caramés, B., Lires-Deán, M., Vaamonde‐García, C., Blanco, F. J., & López-Armada, M. J. (2008) · Arthritis & Rheumatism · doi:10.1002/art.23644 · Cited by 113
Maltecca, F., Magnoni, R., Cerri, F., Cox, G. A., Quattrini, A., & Casari, G. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1532-09.2009 · Cited by 113
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Fried, L. P. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a025916 · Cited by 116
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Wang, Y., Yu, H., Zhang, J., Gao, J., Ge, X., & Lou, G. (2015) · BMC Cancer · doi:10.1186/s12885-015-1706-y · Cited by 110
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Hong, Q., Qi, K., Feng, Z., Huang, Z., Cui, S., Wang, L., Fu, B., Ding, R., Yang, J., Chen, X., et al. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.01.003 · Cited by 110
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Boncompagni, S., Rossi, A. E., Micaroni, M., Hamilton, S. L., Dirksen, R. T., Franzini‐Armstrong, C., & Protasi, F. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911496106 · Cited by 110
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Chalmers, S., & McCarron, J. G. (2007) · Journal of Cell Science · doi:10.1242/jcs.014522 · Cited by 109
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Kook, S.-Y., Jeong, H., Kang, M. J., Park, R., Hj, S., Han, S.-H., Son, S. M., Song, H., Baik, S., Moon, M., et al. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.67 · Cited by 110
Madesh, M., Hawkins, B. J., Milovanova, T. N., Bhanumathy, C. D., Joseph, S. K., RamachandraRao, S. P., Sharma, K., Kurosaki, T., & Fisher, A. B. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505022 · Cited by 111
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Xiong, S., George, S., Ji, Z., Lin, S., Yu, H., Damoiseaux, R. D., France, B., Ng, K. W., & Loo, S. C. J. (2012) · Archives of Toxicology · doi:10.1007/s00204-012-0912-5 · Cited by 109
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Rharass, T., Lemcke, H., Lantow, M., Kuznetsov, S. A., Weiss, D. G., & Panáková, D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.573519 · Cited by 112
Saks, V. A., Guzun, R., Timohhina, N., Tepp, K., Varikmaa, M., Monge, C., Béraud, N., Käämbre, T., Kuznetsov, A. V., Kadaja, L., et al. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.011 · Cited by 111
Heidari, R., Behnamrad, S., Khodami, Z., Ommati, M. M., Azarpira, N., & Vazin, A. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.10.093 · Cited by 108
RetractedAldakkak, M., Stowe, D. F., Chen, Q., Lesnefsky, E. J., & Camara, A. K. S. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.08.008 · Cited by 111
Pignochino, Y., Dell’Aglio, C., Basiricò, M., Capozzi, F., Soster, M., Marchiò, S., Bruno, S., Gammaitoni, L., Sangiolo, D., Torchiaro, E., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-2293 · Cited by 107
Cai, Y., Kong, H., Pan, Y., Jiang, L., Pan, X.-X., Hu, L., Qian, Y., Jiang, C., & Liu, W. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0520-z · Cited by 107
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Vultur, A., Gibhardt, C. S., Stanisz, H., & Bogeski, I. (2018) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-018-2162-8 · Cited by 107
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Florenzano, F., Viscomi, M. T., Mercaldo, V., Longone, P., Bernardi, G., Bagni, C., Molinari, M., & Carrive, P. (2006) · The Journal of Comparative Neurology · doi:10.1002/cne.21013 · Cited by 104
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de Oliveira, J., Hort, M. A., Moreira, E. L. G., Glaser, V., Ribeiro‐do‐Valle, R. M., Prediger, R. D., Farina, M., Latini, A., & Bem, A. F. D. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.09.009 · Cited by 107
Feng, X., Xia, Q., Yuan, L., Yang, X., & Wang, K. (2010) · NeuroToxicology · doi:10.1016/j.neuro.2010.04.003 · Cited by 104
Heinen, A., Aldakkak, M., Stowe, D. F., Rhodes, S. S., Riess, M. L., Varadarajan, S. G., & Camara, A. K. S. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00198.2007 · Cited by 103
Orr, A. L., Kim, C., Jimenez-Morales, D., Newton, B. W., Johnson, J. R., Krogan, N. J., Swaney, D. L., & Mahley, R. W. (2019) · Journal of Alzheimer's Disease · doi:10.3233/jad-181184 · Cited by 103
Huang, H., Liao, J., Zheng, X., Chen, Y., & Ren, H. (2019) · Water Research · doi:10.1016/j.watres.2019.04.046 · Cited by 103
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Cao, X., Zhao, S.-S., Liu, D., Wang, Z., Niu, L.-L., Hou, L., & Wang, C. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2011.01.010 · Cited by 104
Xiao, Y., Karam, C. N., Yi, J., Zhang, L., Li, X., Yoon, D., Wang, H., Dhakal, K. R., Ramlow, P., Yu, T., et al. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.09.008 · Cited by 101
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Silva, B., Oliveira, P. J., Dias, A. C. P., & Malva, J. O. (2008) · Neurotoxicity Research · doi:10.1007/bf03033510 · Cited by 101
Zuo, Z., Zhu, Y., Bai, Y., & Wang, Y. (2011) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2011.11.003 · Cited by 101
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Chu, X., Jiang, X., Liu, Y., Zhai, S., Jiang, Y., Chen, Y., Wu, J., Ya, W., Wu, Y., Tao, X., et al. (2021) · Advanced Functional Materials · doi:10.1002/adfm.202008507 · Cited by 99
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Metadata
- Authors
- Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S.
- Affiliations
- University of Rochester Medicine (US)
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 2004-10
- Volume
- 287
- Issue
- 4
- Pages
- C817-C833
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- OpenAlex
- W2068048197
- Cited by
- 2,575
- References
- 227
- Citations by year
- 2026: 72 · 2025: 112 · 2024: 126 · 2023: 138 · 2022: 144 · 2021: 177 · 2020: 162 · 2019: 134 · 2018: 125 · 2017: 125 · 2016: 122 · 2015: 125 · 2014: 124 · 2013: 129 · 2012: 124
- FWCI
- 5.61
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Cell Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Medical Center, University of Rochester
- National Heart, Lung, and Blood Institute (HL 33333, R01HL033333, HL-71158-01, R01HL071158)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-061991, R01DK061991)
- National Institute of Neurological Disorders and Stroke (NS-37710, R01NS037710)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial calcium homeostasis, ATP production, reactive oxygen species, mitochondrial dysfunction, mitochondrial permeability transition pore, cytochrome c release, apoptosis, two-hit hypothesis, mitochondrial bioenergetics, calcium signaling
- MeSH terms
- Adenosine Triphosphate, Calcium, Energy Metabolism, Ion Channels, Mitochondria, Signal Transduction, Reactive Oxygen Species
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