The Mitochondrial Calcium Uniporter Matches Energetic Supply with Cardiac Workload during Stress and Modulates Permeability Transition
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Cardiac contractility is mediated by a variable flux in intracellular calcium (Ca(2+)), thought to be integrated into mitochondria via the mitochondrial calcium uniporter (MCU) channel to match energetic demand. Here, we examine a conditional, cardiomyocyte-specific, mutant mouse lacking Mcu, the pore-forming subunit of the MCU channel, in adulthood. Mcu(-/-) mice display no overt baseline phenotype and are protected against mCa(2+) overload in an in vivo myocardial ischemia-reperfusion injury model by preventing the activation of the mitochondrial permeability transition pore, decreasing infarct size, and preserving cardiac function. In addition, we find that Mcu(-/-) mice lack contractile responsiveness to acute β-adrenergic receptor stimulation and in parallel are unable to activate mitochondrial dehydrogenases and display reduced bioenergetic reserve capacity. These results support the hypothesis that MCU may be dispensable for homeostatic cardiac function but required to modulate Ca(2+)-dependent metabolism during acute stress.
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Adult mice subjected to cardiomyocyte-specific deletion of Mcu are protected against cardiac ischemia/reperfusion as consequence of MTP inhibition.
“Adult mice subjected to the cardiomyocyte-specific deletion of Mcu are protected against cardiac ischemia/reperfusion as a consequence of MTP inhibition [419].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [419]
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Control of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+
Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,120 · see citing works
Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280 · see citing works
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257 · see citing works
Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter
Baughman, J. M., Perocchi, F., Girgis, H. S., Plovanich, M. E., Belcher-Timme, C. A., Sancak, Y., Bao, X., Strittmatter, L., Goldberger, O., Bogorad, R., et al. (2011) · Nature · doi:10.1038/nature10234 · Cited by 1,926 · see citing works
A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
Stefani, D. D., Raffaello, A., Teardo, E., Szabò, I., & Rizzuto, R. (2011) · Nature · doi:10.1038/nature10230 · Cited by 1,431 · see citing works
The mitochondrial calcium uniporter is a highly selective ion channel
Kirichok, Y., Krapivinsky, G., & Clapham, D. E. (2004) · Nature · doi:10.1038/nature02246 · Cited by 1,409 · see citing works
Metabolite profiling identifies a key role for glycine in rapid cancer cell proliferation
Jain, M., Nilsson, R., Sharma, S., Madhusudhan, N., Kitami, T., Souza, A. L., Kafri, R., Kirschner, M. W., Clish, C. B., & Mootha, V. K. (2012) · Science · doi:10.1126/science.1218595 · Cited by 1,403 · see citing works
Self-citationCalcium cycling and signaling in cardiac myocytes.
Bers, D. (2008) · Annual Review of Physiology · doi:10.1146/annurev.physiol.70.113006.100455 · Cited by 1,386 · see citing works
Effect of Cyclosporine on Reperfusion Injury in Acute Myocardial Infarction
Piot, C. A., Croisille, P., Staat, P., Thibault, H., Rioufol, G., Mewton, N., Belghiti, R. E., Cung, T. T., Bonnefoy‐Cudraz, E., Angoulvant, D., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa071142 · Cited by 1,339 · see citing works
Elrod, J. W., Calvert, J. W., Morrison, J., Doeller, J. E., Kraus, D. W., Tao, L., Jiao, X., Scalia, R. G., Kiss, L., Szabó, C., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705891104 · Cited by 1,246 · see citing works
Self-citationOrganelle isolation: functional mitochondria from mouse liver, muscle and cultured filroblasts
Frezza, C., Cipolat, S., & Scorrano, L. (2007) · Nature Protocols · doi:10.1038/nprot.2006.478 · Cited by 1,188 · see citing works
Quantitative flux analysis reveals folate-dependent NADPH production
Fan, J., Ye, J., Kamphorst, J. J., Shlomi, T., Thompson, C. B., & Rabinowitz, J. D. (2014) · Nature · doi:10.1038/nature13236 · Cited by 1,114 · see citing works
Regulation of mitochondrial dehydrogenases by calcium ions
Denton, R. M. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.01.005 · Cited by 885 · see citing works
NCLX is an essential component of mitochondrial Na + /Ca 2+ exchange
Palty, R., Silverman, W. F., Hershfinkel, M., Caporale, T., Sensi, S. L., Parnis, J., Nolte, C., Fishman, D., Shoshan‐Barmatz, V., Herrmann, S., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908099107 · Cited by 789 · see citing works
A Novel and Efficient Model of Coronary Artery Ligation and Myocardial Infarction in the Mouse
Gao, E., Lei, Y. H., Shang, X., Huang, Z. M., Zuo, L., Boucher, M., Fan, Q., Chuprun, J. K., Ma, X. L., & Koch, W. J. (2010) · Circulation Research · doi:10.1161/circresaha.110.223925 · Cited by 769 · see citing works
Self-citationMallilankaraman, K. B., Doonan, P. J., Cárdenas, C., Chandramoorthy, H. C. K., Müller, M., Miller, R., Hoffman, N. E., Gandhirajan, R. K., Molgó, J., Birnbaum, M. J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.011 · Cited by 661 · see citing works
Self-citationRole of Mitochondrial Ca2+ in the Regulation of Cellular Energetics
Glancy, B. C., & Balaban, R. S. (2012) · Biochemistry · doi:10.1021/bi2018909 · Cited by 649 · see citing works
Pan, X., Liu, J., Nguyen, T. T. M., Liu, C., Sun, J., Teng, Y., Fergusson, M. M., Rovira, I. I., Allen, M. D., Springer, D., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2868 · Cited by 645 · see citing works
Specific inhibition of mitochondrial Ca++ transport by ruthenium red
Moore, C. L. (1971) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(71)90102-1 · Cited by 617 · see citing works
Mitochondrial permeability transition in Ca2+-dependent apoptosis and necrosis
Rasola, A., & Bernardi, P. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.04.007 · Cited by 563 · see citing works
Genome-Wide RNAi Screen Identifies Letm1 as a Mitochondrial Ca 2+ /H + Antiporter
Jiang, D., Zhao, L., & Clapham, D. E. (2009) · Science · doi:10.1126/science.1175145 · Cited by 512 · see citing works
MICU1 Controls Both the Threshold and Cooperative Activation of the Mitochondrial Ca2+ Uniporter
Csordás, G., Golenár, T., Seifert, E. L., Kamer, K. J., Sancak, Y., Perocchi, F., Moffat, C., Weaver, D., de la Fuente, S., Bogorad, R. L., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.04.020 · Cited by 491 · see citing works
Oka, T., Maillet, M., Watt, A. J., Schwartz, R. J., Aronow, B. J., Duncan, S. A., & Molkentin, J. D. (2006) · Circulation Research · doi:10.1161/01.res.0000215985.18538.c4 · Cited by 424 · see citing works
Elrod, J. W., Wong, R., Mishra, S., Vagnozzi, R. J., Sakthievel, B., Goonasekera, S. A., Karch, J., Gabel, S., Farber, J., Force, T., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci43171 · Cited by 384 · see citing works
Self-citationWilliams, G. S. B., Boyman, L., Chikando, A. C., Khairallah, R. J., & Lederer, W. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300410110 · Cited by 362 · see citing works
Kwong, J. Q., Lu, X., Correll, R. N., Schwanekamp, J. A., Vagnozzi, R. J., Sargent, M. A., York, A. J., Zhang, J. J., Bers, D. M., & Molkentin, J. D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.06.002 · Cited by 360 · see citing works
Chen, Y., Csordás, G., Jowdy, C. C., Schneider, T. G., Csordás, N., Wang, W., Liu, Y., Kohlhaas, M., Meiser, M., Bergem, S., et al. (2012) · Circulation Research · doi:10.1161/circresaha.112.266585 · Cited by 348 · see citing works
Death begets failure in the heart
Foo, R., Mani, K. M., & Kitsis, R. N. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24569 · Cited by 307 · see citing works
Curran, J. W., Hinton, M., Ríos, E., Bers, D., & Shannon, T. (2007) · Circulation Research · doi:10.1161/01.res.0000258172.74570.e6 · Cited by 281 · see citing works
Zhou, Y.-Y., Wang, S., Zhu, W., Chruscinski, A., Kobilka, B. K., Ziman, B. D., Wang, S., Lakatta, E. G., Cheng, H., & Xiao, R.-P. (2000) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2000.279.1.h429 · Cited by 280 · see citing works
Physiologic Functions of Cyclophilin D and the Mitochondrial Permeability Transition Pore
Elrod, J. W., & Molkentin, J. D. (2013) · Circulation Journal · doi:10.1253/circj.cj-13-0321 · Cited by 266 · see citing works
Self-citationIdentification of a Ryanodine Receptor in Rat Heart Mitochondria
Beutner, G., Sharma, V. K., Giovannucci, D. R., Yule, D. I., & Sheu, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101486200 · Cited by 246 · see citing works
Activity of the mitochondrial calcium uniporter varies greatly between tissues
Fieni, F., Lee, S. B., Jan, Y. N., & Kirichok, Y. (2012) · Nature Communications · doi:10.1038/ncomms2325 · Cited by 231 · see citing works
Mitochondrial Ca 2+ uptake contributes to buffering cytoplasmic Ca 2+ peaks in cardiomyocytes
Drago, I., Stefani, D. D., Rizzuto, R., & Pozzan, T. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210718109 · Cited by 218 · see citing works
Mitochondrial calcium and the regulation of metabolism in the heart
Williams, G. S. B., Boyman, L., & Lederer, W. J. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.10.019 · Cited by 194 · see citing works
MCU encodes the pore conducting mitochondrial calcium currents
Chaudhuri, D., Sancak, Y., Mootha, V. K., & Clapham, D. E. (2013) · eLife · doi:10.7554/elife.00704 · Cited by 181 · see citing works
Evolutionary Diversity of the Mitochondrial Calcium Uniporter
Bick, A. G., Calvo, S. E., & Mootha, V. K. (2012) · Science · doi:10.1126/science.1214977 · Cited by 158 · see citing works
The mitochondrial uniporter controls fight or flight heart rate increases
Wu, Y., Rasmussen, T. P., Koval, O. M., Joiner, M.-L. A., Hall, D. D., Chen, B., Luczak, E. D., Wang, Q., Rokita, A. G., Wehrens, X. H. T., et al. (2015) · Nature Communications · doi:10.1038/ncomms7081 · Cited by 147 · see citing works
Michels, G., Khan, I., Endres-Becker, J., Rottlaender, D., Herzig, S., Ruhparwar, A., Wahlers, T., & Hoppe, U. C. (2009) · Circulation · doi:10.1161/circulationaha.108.835389 · Cited by 138 · see citing works
Isolation of a soluble Ca2+ binding glycoprotein from ox liver mitochondria
Sottocasa, G. L., Sandri, G., Panfili, E., de BERNARD, B., Gazzotti, P., Vasington, F. D., & Carafoli, E. (1972) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(72)90564-5 · Cited by 126 · see citing works
McCormack, J. G., & ENGLAND, P. J. (1983) · Biochemical Journal · doi:10.1042/bj2140581 · Cited by 123 · see citing works
Brandes, R. P., & Bers, D. M. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75194-1 · Cited by 113 · see citing works
Palmieri, E. M., Spera, I., Menga, A., Infantino, V., Porcelli, V., Iacobazzi, V., Pierri, C. L., Hooper, D. C., Palmieri, F., & Castegna, A. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.04.009 · Cited by 102 · see citing works
Mitochondrial calcium channels
Hoppe, U. C. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.04.017 · Cited by 95 · see citing works
Unitt, J. F., McCormack, J. G., Reid, D. G., MacLachlan, L. K., & ENGLAND, P. J. (1989) · Biochemical Journal · doi:10.1042/bj2620293 · Cited by 87 · see citing works
Involvement of the mitochondrial calcium uniporter in cardioprotection by ischemic preconditioning
Zhang, S., Gao, Q. F., Cao, C., Bruce, I. C., & Xia, Q. (2005) · Life Sciences · doi:10.1016/j.lfs.2005.05.076 · Cited by 66 · see citing works
Zhou, Y., Wang, S. Q., Zhu, W. Z., Chruscinski, A. J., Kobilka, B. K., Ziman, B. D., Wang, S., Lakatta, E. G., Cheng, H., & Xiao, R. (2000) · Cited by 58 · see citing works
Zhao, Q., Wang, S., Li, Y., Wang, P., Li, S., Guo, Y., & Yao, R. (2013) · Molecular Medicine Reports · doi:10.3892/mmr.2013.1321 · Cited by 54 · see citing works
Musgrove, E. A., Šarčević, B., & Sutherland, R. L. (1996) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19960301)60:3 · Cited by 37 · see citing works
Yang, L., Luo, H., Vinay, P., & Wu, J. (1996) · PubMed · doi:10.1002/(sici)1097-4644(19960301)60:3%3c400::aid-jcb11%3e3.0.co;2-o · Cited by 16 · see citing works
Howell, W. H., & DUKE, W. W. (1906) · The Journal of Physiology · doi:10.1113/jphysiol.1906.sp001186 · Cited by 12 · see citing works
Huang, Y. C., & Colman, R. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505828200 · Cited by 11 · see citing works
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Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works
Self-citationThe machineries, regulation and cellular functions of mitochondrial calcium
Giorgi, C., Marchi, S., & Pinton, P. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0052-8 · Cited by 941 · see citing works
Mitochondrial dysfunction in pathophysiology of heart failure
Zhou, B., & Tian, R. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120849 · Cited by 934 · see citing works
Calcium Signaling and Reactive Oxygen Species in Mitochondria
Bertero, E., & Maack, C. (2018) · Circulation Research · doi:10.1161/circresaha.118.310082 · Cited by 616 · see citing works
Mitochondria at the neuronal presynapse in health and disease
Devine, M. J., & Kittler, J. T. (2018) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.170 · Cited by 615 · see citing works
Molecular mechanisms and consequences of mitochondrial permeability transition
Bonora, M., Giorgi, C., & Pinton, P. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00433-y · Cited by 549 · see citing works
Raffaello, A., Mammucari, C., Gherardi, G., & Rizzuto, R. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.09.001 · Cited by 542 · see citing works
Bernardi, P., Gerle, C., Halestrap, A. P., Jonas, E. A., Karch, J. M., Mnatsakanyan, N., Pavlov, E. V., Sheu, S., & Soukas, A. A. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01187-0 · Cited by 482 · see citing works
Mitochondrial Function, Biology, and Role in Disease
Murphy, E., Ardehali, H., Balaban, R. S., DiLisa, F., Dorn, G. W., Kitsis, R. N., Otsu, K., Ping, P., Rizzuto, R., Sack, M. N., et al. (2016) · Circulation Research · doi:10.1161/res.0000000000000104 · Cited by 459 · see citing works
Role of Mitochondrial Calcium and the Permeability Transition Pore in Regulating Cell Death
Bauer, T. M., & Murphy, E. (2020) · Circulation Research · doi:10.1161/circresaha.119.316306 · Cited by 441 · see citing works
Enjoy the Trip: Calcium in Mitochondria Back and Forth
Stefani, D. D., Rizzuto, R., & Pozzan, T. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034216 · Cited by 424 · see citing works
Mitochondrial calcium exchange in physiology and disease
Garbincius, J. F., & Elrod, J. W. (2021) · Physiological Reviews · doi:10.1152/physrev.00041.2020 · Cited by 413 · see citing works
Self-citationThe mitochondrial Na+/Ca2+ exchanger is essential for Ca2+ homeostasis and viability
Luongo, T. S., Lambert, J. P., Gross, P., Nwokedi, M., Lombardi, A. A., Shanmughapriya, S., Carpenter, A. C., Kolmetzky, D., Gao, E., van Berlo, J. H., et al. (2017) · Nature · doi:10.1038/nature22082 · Cited by 396 · see citing works
Self-citationKwong, J. Q., Lu, X., Correll, R. N., Schwanekamp, J. A., Vagnozzi, R. J., Sargent, M. A., York, A. J., Zhang, J. J., Bers, D. M., & Molkentin, J. D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.06.002 · Cited by 360 · see citing works
Jadiya, P., Kolmetzky, D. W., Tomar, D., Di Meco, A., Lombardi, A. A., Lambert, J. P., Luongo, T. S., Ludtmann, M. H., Praticò, D., & Elrod, J. W. (2019) · Nature Communications · doi:10.1038/s41467-019-11813-6 · Cited by 323 · see citing works
Self-citationRegulation of Mitochondrial ATP Production: Ca2+ Signaling and Quality Control
Boyman, L., Karbowski, M., & Lederer, W. J. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.10.007 · Cited by 309 · see citing works
Targeting mitochondria for cardiovascular disorders: therapeutic potential and obstacles
Bonora, M., Wieckowski, M. R., Sinclair, D. A., Kroemer, G., Pinton, P., & Galluzzi, L. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0074-0 · Cited by 299 · see citing works
Calcium Dynamics as a Machine for Decoding Signals
Giorgi, C., Danese, A., Missiroli, S., Patergnani, S., & Pinton, P. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.01.002 · Cited by 282 · see citing works
Stein, C. S., Jadiya, P., Zhang, X., McLendon, J. M., Abouassaly, G. M., Witmer, N. H., Anderson, E. J., Elrod, J. W., & Boudreau, R. L. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.002 · Cited by 271 · see citing works
Self-citationRovere, R. M. L. L., Roest, G., Bultynck, G., & Parys, J. B. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.04.005 · Cited by 256 · see citing works
Calcium Transport and Signaling in Mitochondria
Bravo, R., Parra, V., López‐Crisosto, C., Díaz, P., Quest, A. F. G., & Lavandero, S. (2017) · Comprehensive physiology · doi:10.1002/cphy.c160013 · Cited by 249 · see citing works
Crosstalk between calcium and reactive oxygen species signaling in cancer
Hempel, N., & Trebak, M. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.01.007 · Cited by 243 · see citing works
Xiao, M., Zhong, H., Xia, L., Tao, Y., & Yin, H. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.363 · Cited by 242 · see citing works
Na(+) controls hypoxic signalling by the mitochondrial respiratory chain
Hernansanz-Agustín, P., Choya-Foces, C., Carregal-Romero, S., Ramos, E., Oliva, T., Villa-Piña, T., Moreno, L., Izquierdo-Álvarez, A., Cabrera-García, J. D., Cortés, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2551-y · Cited by 238 · see citing works
Self-citationPathak, T., & Trebak, M. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.07.001 · Cited by 223 · see citing works
MICU1 Serves as a Molecular Gatekeeper to Prevent In Vivo Mitochondrial Calcium Overload
Liu, J. C., Liu, J., Holmström, K. M., Menazza, S., Parks, R. J., Fergusson, M. M., Yu, Z., Springer, D., Halsey, C., Liu, C., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.011 · Cited by 222 · see citing works
Mitochondrial Ca2+ and regulation of the permeability transition pore
Hurst, S., Hoek, J. B., & Sheu, S. (2016) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-016-9672-x · Cited by 220 · see citing works
MCUR1 Is a Scaffold Factor for the MCU Complex Function and Promotes Mitochondrial Bioenergetics
Tomar, D., Dong, Z., Shanmughapriya, S., Koch, D. A., Thomas, T. P., Hoffman, N. E., Timbalia, S. A., Goldman, S. J., Breves, S. L., Corbally, D. P., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.050 · Cited by 210 · see citing works
Self-citationMICU1 regulation of mitochondrial Ca2+ uptake dictates survival and tissue regeneration
Antony, A. N., Paillard, M., Moffat, C., Juskeviciute, E., Correnti, J., Bolon, B., Rubin, E., Csordás, G., Seifert, E. L., Hoek, J. B., et al. (2016) · Nature Communications · doi:10.1038/ncomms10955 · Cited by 206 · see citing works
Davidson, S. M., Adameová, A., Barile, L., Cabrera-Fuentes, H. A., Lazou, A., Pagliaro, P., Stensløkken, K., García‐Dorado, D., & (CA16225), T. E. C. A. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15127 · Cited by 206 · see citing works
Paillard, M., Csordás, G., Szanda, G., Golenár, T., Debattisti, V., Bartók, Á., Wang, N., Moffat, C., Seifert, E. L., Spät, A., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.032 · Cited by 194 · see citing works
Crosstalk between Calcium and ROS in Pathophysiological Conditions
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Sarcoplasmic reticulum–mitochondria communication in cardiovascular pathophysiology
López‐Crisosto, C., Pennanen, C., Vásquez-Trincado, C., Morales, P. E., Bravo, R., Quest, A. F. G., Chiong, M., & Lavandero, S. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2017.23 · Cited by 183 · see citing works
Mitochondrial calcium uptake in organ physiology: from molecular mechanism to animal models
Mammucari, C., Raffaello, A., Reane, D. V., Gherardi, G., Mario, A. D., & Rizzuto, R. (2018) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-018-2123-2 · Cited by 179 · see citing works
Molecular nature and physiological role of the mitochondrial calcium uniporter channel
Alevriadou, B. R., Patel, A., Noble, M., Ghosh, S., Gohil, V. M., Stathopulos, P. B., & Madesh, M. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00502.2020 · Cited by 174 · see citing works
Self-citationThe Toxicity and Polymorphism of β-Amyloid Oligomers
Huang, Y., & Liu, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124477 · Cited by 168 · see citing works
Lombardi, A. A., Gibb, A., Arif, E., Kolmetzky, D. W., Tomar, D., Luongo, T. S., Jadiya, P., Murray, E. K., Lorkiewicz, P. K., Hajnóczky, G., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12103-x · Cited by 161 · see citing works
Self-citationWoods, J. J., Nemani, N., Shanmughapriya, S., Kumar, A., Zhang, M., Nathan, S. R., Thomas, M., Carvalho, E. J., Karthik, R., Srikantan, S., et al. (2019) · ACS Central Science · doi:10.1021/acscentsci.8b00773 · Cited by 161 · see citing works
Self-citationFerdinandy, P., Andreadou, I., Baxter, G. F., Bøtker, H. E., Davidson, S. M., Dobrev, D., Gersh, B. J., Heusch, G., Lecour, S., Ruiz‐Meana, M., et al. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000348 · Cited by 162 · see citing works
The role of succinate and ROS in reperfusion injury – A critical appraisal
Andrienko, T., Pasdois, P., Pereira, G. C., Ovens, M. J., & Halestrap, A. P. (2017) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2017.06.016 · Cited by 158 · see citing works
ER–Mitochondria Microdomains in Cardiac Ischemia–Reperfusion Injury: A Fresh Perspective
Zhou, H., Wang, S., Hu, S., Chen, Y., & Ren, J. T. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00755 · Cited by 157 · see citing works
Dia, M., Gomez, L., Thibault, H., Tessier, N., Léon, C., Chouabe, C., Ducreux, S., Gallo-Bona, N., Tubbs, E., Bendridi, N., et al. (2020) · Basic Research in Cardiology · doi:10.1007/s00395-020-00835-7 · Cited by 151 · see citing works
Lambert, J. P., Luongo, T. S., Tomar, D., Jadiya, P., Gao, E., Zhang, X., Lucchese, A. M., Kolmetzky, D. W., Shah, N. S., & Elrod, J. W. (2019) · Circulation · doi:10.1161/circulationaha.118.037968 · Cited by 148 · see citing works
Self-citationGuan, L., Che, Z., Meng, X., Yu, Y. Q., Li, M., Yu, Z., Shi, H., Yang, D., & Yu, M. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14662 · Cited by 146 · see citing works
Voltage-energized calcium-sensitive ATP production by mitochondria
Wescott, A. P., Kao, J. P. Y., Lederer, W. J., & Boyman, L. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0126-8 · Cited by 144 · see citing works
Novel targets for mitochondrial medicine
Wang, W., Karamanlidis, G., & Tian, R. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aac7410 · Cited by 138 · see citing works
Heusch, G., Andreadou, I., Bell, R., Bertero, E., Bøtker, H. E., Davidson, S. M., Downey, J. M., Eaton, P., Ferdinandy, P., Gersh, B. J., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102894 · Cited by 140 · see citing works
Mitochondrial Function and Dysfunction in Dilated Cardiomyopathy
Ramaccini, D., Montoya-Uribe, V., Aan, F. J., Modesti, L., Potes, Y., Wieckowski, M. R., Krga, I., Glibetić, M., Pinton, P., Giorgi, C., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.624216 · Cited by 136 · see citing works
Physiopathology of the Permeability Transition Pore: Molecular Mechanisms in Human Pathology
Bonora, M., Patergnani, S., Ramaccini, D., Morciano, G., Pedriali, G., Kahsay, A., Bouhamida, E., Giorgi, C., Wieckowski, M., & Pinton, P. (2020) · Biomolecules · doi:10.3390/biom10070998 · Cited by 135 · see citing works
Mitochondrial calcium imbalance in Parkinson’s disease
Ludtmann, M. H. R., & Abramov, A. Y. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.08.044 · Cited by 133 · see citing works
Calcium signaling as a mediator of cell energy demand and a trigger to cell death
Bhosale, G., Sharpe, J. A., Sundier, S. Y., & Duchen, M. R. (2015) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12885 · Cited by 132 · see citing works
The mitochondrial permeability transition pore in AD 2016: An update
Biasutto, L., Azzolini, M., Szabó, I., & Zoratti, M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.02.012 · Cited by 128 · see citing works
Mitochondrial Regulation of the Hippocampal Firing Rate Set Point and Seizure Susceptibility
Styr, B., Gonen, N., Zarhin, D., Ruggiero, A., Atsmon, R., Gazit, N., Braun, G., Frère, S. G. A., Vertkin, I., Shapira, I., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.03.045 · Cited by 126 · see citing works
The Mitochondrial Voltage-Dependent Anion Channel 1, Ca2+ Transport, Apoptosis, and Their Regulation
Shoshan‐Barmatz, V., De, S., & Meir, A. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00060 · Cited by 122 · see citing works
Mitochondrial Ca2+ Signaling in Health, Disease and Therapy
Modesti, L., Danese, A., Vitto, V. A. M., Ramaccini, D., Aguiari, G., Gafà, R., Lanza, G., Giorgi, C., & Pinton, P. (2021) · Cells · doi:10.3390/cells10061317 · Cited by 119 · see citing works
Mitochondrial calcium and reactive oxygen species in cardiovascular disease
Murphy, E., & Liu, J. C. (2022) · Cardiovascular Research · doi:10.1093/cvr/cvac134 · Cited by 120 · see citing works
The EF-Hand Ca2+ Binding Protein MICU Choreographs Mitochondrial Ca2+ Dynamics in Arabidopsis
Wagner, S., Behera, S., Bortoli, S. D., Logan, D. C., Fuchs, P., Carraretto, L., Teardo, E., Cendron, L., Nietzel, T., Füßl, M., et al. (2015) · The Plant Cell · doi:10.1105/tpc.15.00509 · Cited by 117 · see citing works
Molecular regulation of MCU: Implications in physiology and disease
Nemani, N., Shanmughapriya, S., & Madesh, M. (2018) · Cell Calcium · doi:10.1016/j.ceca.2018.06.006 · Cited by 116 · see citing works
Self-citationElevated MCU Expression by CaMKIIδB Limits Pathological Cardiac Remodeling
Wang, P., Xu, S., Xu, J., Xin, Y., Lu, Y., Zhang, H., Zhou, B., Xu, H., Sheu, S.-S., Tian, R., et al. (2022) · Circulation · doi:10.1161/circulationaha.121.055841 · Cited by 111 · see citing works
The Role of Impaired Mitochondrial Dynamics in MFN2-Mediated Pathology
Zaman, M., & Shutt, T. E. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.858286 · Cited by 113 · see citing works
The Mitochondrial Ca2+ Uptake and the Fine-Tuning of Aerobic Metabolism
Gherardi, G., Monticelli, H., Rizzuto, R., & Mammucari, C. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.554904 · Cited by 109 · see citing works
CaMKII is a nodal signal for multiple programmed cell death pathways in heart
Feng, N., & Anderson, M. E. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.12.007 · Cited by 107 · see citing works
Wang, Z., Liu, D., Varin, A., Nicolas, V, Courilleau, D., Mateo, P., Caubere, C., Rouet, P., Gomez, A.-M., Vandecasteele, G., et al. (2016) · Cell Death & Disease · doi:10.1038/cddis.2016.106 · Cited by 106 · see citing works
Mitochondrial pathways to cardiac recovery: TFAM
Kunkel, G. H., Chaturvedi, P., & Tyagi, S. C. (2016) · Heart Failure Reviews · doi:10.1007/s10741-016-9561-8 · Cited by 105 · see citing works
Mitochondrial calcium cycling in neuronal function and neurodegeneration
Walters, G. C., & Usachev, Y. M. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1094356 · Cited by 105 · see citing works
Santin, Y., Fazal, L., Sainte–Marie, Y., Sicard, P., Maggiorani, D., Tortosa, F., Yücel, Y. Y., Teyssedre, L., Rouquette, J., Marcellin, M., et al. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0470-y · Cited by 103 · see citing works
Suárez, J., Cividini, F., Scott, B. T., Lehmann, K. A., Díaz-Juárez, J. A., Diemer, T., Dai, A., Suárez, J., Jain, M., & DILLMANN, W. H. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002066 · Cited by 103 · see citing works
Self-citationDS16570511 is a small-molecule inhibitor of the mitochondrial calcium uniporter
Kon, N., Murakoshi, M., Isobe, A., Kagechika, K., Miyoshi, N., & Nagayama, T. (2017) · Cell Death Discovery · doi:10.1038/cddiscovery.2017.45 · Cited by 101 · see citing works
Tomar, D., Jaña, F., Dong, Z., Quinn, W. J., Jadiya, P., Breves, S. L., Daw, C. C., Srikantan, S., Shanmughapriya, S., Nemani, N., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.107 · Cited by 95 · see citing works
Self-citationMitochondrial energetics and calcium coupling in the heart
Kohlhaas, M., Nickel, A. G., & Maack, C. (2017) · The Journal of Physiology · doi:10.1113/jp273609 · Cited by 98 · see citing works
Rueda, C. B., Llorente‐Folch, I., Traba, J., Amigo, I., González‐Sánchez, P., Contreras, L., Juaristi, I., Martínez-Valero, P., Pardo, B., del Arco, A., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.04.003 · Cited by 95 · see citing works
Mitochondrial calcium in cardiac ischemia/reperfusion injury and cardioprotection
Bertero, E., Popoiu, T.-A., & Maack, C. (2024) · Basic Research in Cardiology · doi:10.1007/s00395-024-01060-2 · Cited by 94 · see citing works
Ablation of the stress protease OMA1 protects against heart failure in mice
Acín‐Pérez, R., Lechuga‐Vieco, A. V., Muñoz, M. D. M., Nieto-Arellano, R., Torroja, C., Sánchez‐Cabo, F., Jiménez, C., González-Guerra, A., Carrascoso, I., Benincá, C., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aan4935 · Cited by 93 · see citing works
Mammucari, C., Gherardi, G., & Rizzuto, R. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00139 · Cited by 92 · see citing works
Sepsis-induced myocardial dysfunction: the role of mitochondrial dysfunction
Yang, H., & Zhang, Z. (2021) · Inflammation Research · doi:10.1007/s00011-021-01447-0 · Cited by 91 · see citing works
Ca 2+ channels couple spiking to mitochondrial metabolism in substantia nigra dopaminergic neurons
Zampese, E., Wokosin, D. L., González‐Rodríguez, P., Guzmán, J. N., Tkatch, T., Kondapalli, J., Surmeier, W. C., D’Alessandro, K. B., Stefani, D. D., Rizzuto, R., et al. (2022) · Science Advances · doi:10.1126/sciadv.abp8701 · Cited by 91 · see citing works
Zaglia, T., Ceriotti, P., del Campo, A. F., Borile, G., Armani, A., Carullo, P., Prando, V., Coppini, R., Vida, V. L., Stølen, T., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708772114 · Cited by 88 · see citing works
Crosslink between calcium and sodium signalling
Verkhratsky, A., Trebak, M., Perocchi, F., Khananshvili, D., & Sekler, I. (2017) · Experimental Physiology · doi:10.1113/ep086534 · Cited by 87 · see citing works
Loss of mitochondrial calcium uniporter rewires skeletal muscle metabolism and substrate preference
Gherardi, G., Nogara, L., Ciciliot, S., Fadini, G. P., Blaauw, B., Braghetta, P., Bonaldo, P., Stefani, D. D., Rizzuto, R., & Mammucari, C. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0191-7 · Cited by 86 · see citing works
Bouhamida, E., Morciano, G., Perrone, M., Kahsay, A. E., Della Sala, M., Wieckowski, M. R., Fiorica, F., Pinton, P., Giorgi, C., & Patergnani, S. (2022) · Biology · doi:10.3390/biology11020300 · Cited by 87 · see citing works
MCU Overexpression Rescues Inotropy and Reverses Heart Failure by Reducing SR Ca 2+ Leak
Liu, T., Yang, N., Sidor, A., & O'Rourke, B. P. (2021) · Circulation Research · doi:10.1161/circresaha.120.318562 · Cited by 86 · see citing works
Parks, R. J., Menazza, S., Holmström, K. M., Amanakis, G., Fergusson, M. M., Ma, H., Aponte, A. M., Bernardi, P., Finkel, T., & Murphy, E. (2018) · Cardiovascular Research · doi:10.1093/cvr/cvy218 · Cited by 85 · see citing works
Kaludercic, N., & Giorgio, V. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3869610 · Cited by 88 · see citing works
The mitochondrial calcium uniporter underlies metabolic fuel preference in skeletal muscle
Kwong, J. Q., Huo, J., Bround, M. J., Boyer, J. G., Schwanekamp, J. A., Ghazal, N., Maxwell, J. T., Jang, Y. C., Khuchua, Z. A., Shi, K. Y., et al. (2018) · JCI Insight · doi:10.1172/jci.insight.121689 · Cited by 85 · see citing works
Energy metabolism design of the striated muscle cell
Glancy, B. C., & Balaban, R. S. (2021) · Physiological Reviews · doi:10.1152/physrev.00040.2020 · Cited by 83 · see citing works
Wen, J., Zhang, L., Liu, H., Wang, J., Li, J., Yang, Y., Wang, Y., Cai, H., Li, R., & Zhao, Y. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01135 · Cited by 81 · see citing works
Mitochondrial Dysfunction and Heart Disease: Critical Appraisal of an Overlooked Association
Bisaccia, G., Ricci, F., Gallina, S., Baldassarre, A. D., & Ghinassi, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020614 · Cited by 81 · see citing works
Mitochondrial Calcium Handling in Physiology and Disease
Granatiero, V., Stefani, D. D., & Rizzuto, R. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55330-6_2 · Cited by 77 · see citing works
MCUb Induction Protects the Heart From Postischemic Remodeling
Huo, J., Lü, S., Kwong, J. Q., Bround, M. J., Grimes, K. M., Sargent, M. A., Brown, M. E., Davis, M. E., Bers, D. M., & Molkentin, J. D. (2020) · Circulation Research · doi:10.1161/circresaha.119.316369 · Cited by 72 · see citing works
Mitochondrial Ca2+ Homeostasis: Emerging Roles and Clinical Significance in Cardiac Remodeling
Zhang, D., Wang, F., Li, P., & Gao, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063025 · Cited by 75 · see citing works
The Mitochondrial Calcium Uniporter (MCU): Molecular Identity and Role in Human Diseases
D’Angelo, D., & Rizzuto, R. (2023) · Biomolecules · doi:10.3390/biom13091304 · Cited by 80 · see citing works
Lee, S. H. J., Duron, H. E., & Chaudhuri, D. (2023) · Biochemical Society Transactions · doi:10.1042/bst20230012 · Cited by 74 · see citing works
Excitation–contraction coupling of human induced pluripotent stem cell-derived cardiomyocytes
Kane, C., Couch, L. S., & Terracciano, C. M. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00059 · Cited by 73 · see citing works
Novorolsky, R. J., Nichols, M. T., Kim, J. S., Pavlov, E. V., Woods, J. J., Wilson, J. J., & Robertson, G. S. (2020) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x20908523 · Cited by 72 · see citing works
The mechanism of MICU-dependent gating of the mitochondrial Ca2+uniporter
Garg, V., Suzuki, J., Paranjpe, I., Unsulangi, T., Boyman, L., Milescu, L. S., Lederer, W. J., & Kirichok, Y. (2021) · eLife · doi:10.7554/elife.69312 · Cited by 72 · see citing works
Penna, E., Espino, J., Stefani, D. D., & Rizzuto, R. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.08.008 · Cited by 71 · see citing works
Mario, A. D., Tosatto, A., Hill, J. M., Kriston-Vizi, J., Ketteler, R., Reane, D. V., Cortopassi, G. A., Szabadkai, G., Rizzuto, R., & Mammucari, C. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109275 · Cited by 71 · see citing works
Dhaouadi, N., Vitto, V. A. M., Pinton, P., Galluzzi, L., & Marchi, S. (2023) · Cell Calcium · doi:10.1016/j.ceca.2023.102759 · Cited by 71 · see citing works
de la Fuente, S., Lambert, J. P., Nichtová, Z., Fernández‐Sanz, C., Elrod, J. W., Sheu, S., & Csordás, G. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.08.040 · Cited by 71 · see citing works
Self-citationMolecular structure and pathophysiological roles of the Mitochondrial Calcium Uniporter
Mammucari, C., Raffaello, A., Reane, D. V., & Rizzuto, R. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.03.006 · Cited by 70 · see citing works
- Authors
- Luongo, T. S., Lambert, J. P., Yuan, A., Zhang, X., Gross, P., Song, J., Shanmughapriya, S., Gao, E., Jain, M., Houser, S. R., Koch, W. J., Cheung, J. Y., Madesh, M., & Elrod, J. W.
- Affiliations
- Temple University (US)
- University of California San Diego (US)
- Corresponding author
- Elrod, John W.
- ORCID
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2015-07
- Volume
- 12
- Issue
- 1
- Pages
- 23-34
- ISSN
- 2211-1247 (ISSN-L)
- PMC
- PMC4517182
- OpenAlex
- W1622243645
- Cited by
- 384
- References
- 52
- Citations by year
- 2026: 19 · 2025: 34 · 2024: 25 · 2023: 38 · 2022: 26 · 2021: 49 · 2020: 43 · 2019: 39 · 2018: 43 · 2017: 35 · 2016: 28 · 2015: 5
- FWCI
- 16.06
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Funders
- National Heart, Lung, and Blood Institute (R01HL123966, P01HL091799, HL123966, R01HL119306)
- National Institute on Drug Abuse (P01DA037830)
- National Institute of General Medical Sciences (R01GM109882)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Pathology and Forensic Medicine › Cardiac Ischemia and Reperfusion
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
- Keywords
- mitochondrial calcium uniporter, cardiomyocytes, mitochondrial permeability transition pore, myocardial ischemia-reperfusion injury, intracellular calcium, cardiac contractility, beta-adrenergic signaling, mitochondrial dehydrogenases, infarct size
- MeSH terms
- Animals, Calcium, Cells, Cultured, Energy Metabolism, Mice, Inbred C57BL, Myocardial Contraction, Stress, Physiological, Calcium Channels, Myocardial Reperfusion Injury, Myocytes, Cardiac, Mice
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