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Elucidating Mitochondrial Electron Transport Chain Supercomplexes in the Heart During Ischemia–Reperfusion
Open accessAbstract
AIMS: Mitochondrial supercomplexes (SCs) are the large supramolecular assembly of individual electron transport chain (ETC) complexes that apparently provide highly efficient ATP synthesis and reduce electron leakage and reactive oxygen species (ROS) production. Oxidative stress during cardiac ischemia-reperfusion (IR) can result in degradation of SCs through oxidation of cardiolipin (CL). Also, IR induces calcium overload and enhances reactive oxygen species (mitROS) in mitochondria that result in the opening of the nonselective permeability transition pores (PTP). The opening of the PTP further compromises cellular energetics and increases mitROS ultimately leading to cell death. Here, we examined the role of PTP-induced mitROS in disintegration of SCs during cardiac IR. The relationship between mitochondrial PTP, ROS, and SCs was investigated using Langendorff-perfused rat hearts subjected to global ischemia (25 min) followed by short-time (5 min) or long-time (60 min) reperfusion in the presence or absence of the PTP inhibitor, sanglifehrin A (SfA), and the mitochondrial targeted ROS and electron scavenger, XJB-5-131. Also, the effects of CL deficiency on SC degradation, PTP, and mitROS were investigated in tafazzin knockdown (TazKD) mice. RESULTS: Cardiac IR induced PTP opening and mitROS generation, inhibited by SfA. Percent distributions of SCs were significantly affected by IR, and the effects were dependent on the reperfusion time and reversed by SfA and XJB-5-131. TazKD mice demonstrated a 40% lower SC I + III+IV with reduced basal mitochondrial PTP, ROS, and ETC complex activity. Innovation and Conclusion: Sustained reperfusion after cardiac ischemia induces disintegration of mitochondrial SCs, and PTP-induced ROS presumably play a causal role in SC disassembly. Antioxid. Redox Signal. 27, 57-69.
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“Accordingly, pharmacological inhibitors of CYPD including cyclosporin A (CsA) [376 379–381], sanglifehrin A (SfA) [382, 383], and JW47 [384] limit MPT-driven necrosis and confer protection in multiple rodent models of disease in which oxidative stress and cytosolic Ca2+ overload constitute major etiological determinants (e.g., neuronal, cardiac, and renal ischemia/reperfusion).”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [383]
Citations
Cites
Yellon, D. M., & Hausenloy, D. J. (2007) · New England Journal of Medicine · doi:10.1056/nejmra071667 · Cited by 3,797
Mechanisms Underlying Acute Protection From Cardiac Ischemia-Reperfusion Injury
Murphy, E., & Steenbergen, C. (2008) · Physiological Reviews · doi:10.1152/physrev.00024.2007 · Cited by 1,504
Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
Schägger, H., & Pfeiffer, K. (2000) · The EMBO Journal · doi:10.1093/emboj/19.8.1777 · Cited by 1,356
Halestrap, A. P. (2003) · Cardiovascular Research · doi:10.1016/s0008-6363(03)00533-9 · Cited by 1,244
Cardiolipin Stabilizes Respiratory Chain Supercomplexes
Pfeiffer, K., Gohil, V., Stuart, R. A., Hunte, C., Brandt, U., Greenberg, M. L., & Schägger, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308366200 · Cited by 843
Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion
Griffiths, E. J., & Halestrap, A. P. (1995) · Biochemical Journal · doi:10.1042/bj3070093 · Cited by 838
Supercomplex assembly determines electron flux in the mitochondrial electron transport chain
Lapuente-Brun, E., Moreno-Loshuertos, R., Acín-Pérez, R., Latorre-Pellicer, A., Colás, C., Balsa, E., Perales-Clemente, E., Quirós, P. M., Calvo, E., Rodríguez-Hernández, M. A., et al. (2013) · Science · doi:10.1126/science.1230381 · Cited by 830
Respiratory active mitochondrial supercomplexes
Acín-Pérez, R., Fernández-Silva, P., Peleato, M. L., Pérez-Martos, A., & Enriquez, J. A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.10.021 · Cited by 817
Structure and function of mitochondrial membrane protein complexes
Kühlbrandt, W. (2015) · BMC Biology · doi:10.1186/s12915-015-0201-x · Cited by 780
Cyclosporine before PCI in Patients with Acute Myocardial Infarction
Cung, T.-T., Morel, O., Cayla, G., Rioufol, G., Garcia-Dorado, D., Angoulvant, D., Bonnefoy-Cudraz, E., Guérin, P., Elbaz, M., Delarche, N., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1505489 · Cited by 713
Gluing the Respiratory Chain Together
Zhang, M., Mileykovskaya, E., & Dowhan, W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200551200 · Cited by 642
Functional role of cardiolipin in mitochondrial bioenergetics
Paradies, G., Paradies, V., Benedictis, V. D., Ruggiero, F. M., & Petrosillo, G. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.006 · Cited by 505
Bernardi, P., & Lisa, F. D. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.09.023 · Cited by 503
Maranzana, E., Barbero, G., Falasca, A. I., Lenaz, G., & Genova, M. L. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4845 · Cited by 445
Mitochondrial Respiratory Chain Supercomplexes Are Destabilized in Barth Syndrome Patients
McKenzie, M., Lazarou, M., Thorburn, D. R., & Ryan, M. T. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.057 · Cited by 424
Role of reactive oxygen species and cardiolipin in the release of cytochrome c from mitochondria
Petrosillo, G., Ruggiero, F. M., & Paradies, G. (2003) · The FASEB Journal · doi:10.1096/fj.03-0012com · Cited by 384
Paradies, G., Petrosillo, G., Pistolese, M., & Ruggiero, F. M. (2002) · Gene · doi:10.1016/s0378-1119(01)00814-9 · Cited by 384
Clarke, S. J., McStay, G. P., & Halestrap, A. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202191200 · Cited by 376
Cardiac mitochondria in heart failure: decrease in respirasomes and oxidative phosphorylation
Rosca, M. G., Vazquez, E. J., Kerner, J., Parland, W., Chandler, M. P., Stanley, W. C., Sabbah, H. N., & Hoppel, C. L. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn184 · Cited by 373
Specific inhibition of the mitochondrial permeability transition prevents lethal reperfusion injury
Argaud, L., Gateau-Roesch, O., Muntean, D. M., Chalabreysse, L., Loufouat, J., Robert, D., & Ovize, M. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2004.12.001 · Cited by 359
Chaban, Y. L., Boekema, E. J., & Dudkina, N. V. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.004 · Cited by 349
Zhang, M., Mileykovskaya, E., & Dowhan, W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504955200 · Cited by 338
Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1
Althoff, T., Mills, D. J., Popot, J., & Kühlbrandt, W. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.324 · Cited by 334
A Method for the Localization of Sites for Oxidative Phosphorylation
Chance, B., & Williams, G. R. (1955) · Nature · doi:10.1038/176250a0 · Cited by 294
The Mitochondrial Respiratory Chain Is Partially Organized in a Supercomplex Assembly
Bianchi, C., Genova, M. L., Castelli, G. P., & Lenaz, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405135200 · Cited by 277
Lim, S. Y., Davidson, S. M., Hausenloy, D. J., & Yellon, D. M. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.04.022 · Cited by 269
Batandier, C., Leverve, X., & Fontaine, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310329200 · Cited by 264
Petrosillo, G., Francesca, M. R., Di Venosa, N., & Paradies, A. G. (2003) · The FASEB Journal · doi:10.1096/fj.02-0729fje · Cited by 261
Cardiac and Skeletal Muscle Defects in a Mouse Model of Human Barth Syndrome
Acehan, D., Vaz, F. M., Houtkooper, R. H., James, J. F., Moore, V., Tokunaga, C., Kulik, W., Wansapura, J. P., Toth, M. J., Strauss, A. W., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.171439 · Cited by 258
Self-citationReversal of Various Types of Mitochondrial Swelling by Adenosine Triphosphate
Lehninger, A. L. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69836-9 · Cited by 227
Lim, K. H. H., Javadov, S. A., Das, M., Clarke, S. J., Suleiman, M. S., & Halestrap, A. P. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.031484 · Cited by 219
Self-citationSupercomplexes and subcomplexes of mitochondrial oxidative phosphorylation
Wittig, I., Carrozzo, R., Santorelli, F. M., & Schägger, H. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.05.006 · Cited by 218
Myocardial ischemia selectively depletes cardiolipin in rabbit heart subsarcolemmal mitochondria
Lesnefsky, E. J., Slabe, T. J., Stoll, M. S. K., Minkler, P. E., & Hoppel, C. L. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.280.6.h2770 · Cited by 194
Features and applications of blue‐native and clear‐native electrophoresis
Wittig, I., & Schägger, H. (2008) · PROTEOMICS · doi:10.1002/pmic.200800017 · Cited by 189
Blaza, J. N., Serreli, R., Jones, A. J. Y., Mohammed, K., & Hirst, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1413855111 · Cited by 181
Tompkins, A. J., Burwell, L. S., Digerness, S. B., Zaragoza, C., Holman, W. L., & Brookes, P. S. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.10.001 · Cited by 162
Wipf, P., Xiao, J., Jiang, J., Belikova, N. A., Tyurin, V. A., Fink, M. P., & Kagan, V. E. (2005) · Journal of the American Chemical Society · doi:10.1021/ja053679l · Cited by 159
Self-citationCardioprotection by metabolic shut-down and gradual wake-up
Burwell, L. S., Nadtochiy, S. M., & Brookes, P. S. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.02.026 · Cited by 146
Paradies, G., Petrosillo, G., Pistolese, M., & Ruggiero, F. M. (2001) · Mitochondrion · doi:10.1016/s1567-7249(01)00011-3 · Cited by 139
Petrosillo, G., Casanova, G., Matera, M., Ruggiero, F. M., & Paradies, G. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.10.036 · Cited by 137
Genova, M. L., Baracca, A., Biondi, A., Casalena, G., Faccioli, M., Falasca, A. I., Formiggini, G., Sgarbi, G., Solaini, G., & Lenaz, G. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.04.007 · Cited by 128
Supercomplexes of the mitochondrial electron transport chain decline in the aging rat heart
Gómez, L. A., Monette, J. S., Chavez, J. D., Maier, C. S., & Hagen, T. M. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.08.002 · Cited by 127
Petrosillo, G., Moro, N., Ruggiero, F. M., & Paradies, G. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.06.032 · Cited by 117
Characterization of a Transgenic Short Hairpin RNA-Induced Murine Model of Tafazzin Deficiency
Soustek, M. S., Falk, D. J., Mah, C. S., Toth, M. J., Schlame, M., Lewin, A. S., & Byrne, B. J. (2010) · Human Gene Therapy · doi:10.1089/hum.2010.199 · Cited by 116
Protein carbonylation: avoiding pitfalls in the 2,4-dinitrophenylhydrazine assay
Luo, S., & Wehr, N. B. (2009) · Redox Report · doi:10.1179/135100009x392601 · Cited by 116
Phoon, C. K. L., Acehan, D., Schlame, M., Stokes, D. L., Edelman‐Novemsky, I., Yu, D., Xu, Y., Viswanathan, N., & Ren, M. (2012) · Journal of the American Heart Association · doi:10.1161/jaha.111.000455 · Cited by 111
Hemigramicidin–TEMPO conjugates: Novel mitochondria-targeted anti-oxidants
Fink, M. P., Macias, C. A., Xiao, J., Tyurina, Y. Y., Jiang, J., Belikova, N. A., Delude, R. L., Greenberger, J. S., Kagan, V. E., & Wipf, P. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.05.019 · Cited by 107
Self-citationJavadov, S. A., Choi, A., Rajapurohitam, V., Zeidan, A., Basnakian, A. G., & Karmazyn, M. (2007) · Cardiovascular Research · doi:10.1093/cvr/cvm039 · Cited by 93
Self-citationHernández, J. S., Barreto‐Torres, G., Kuznetsov, A. V., Khuchua, Z. A., & Javadov, S. A. (2014) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12220 · Cited by 92
Self-citationEscobales, N., Nuñez, R. E., Jang, S., Parodi‐Rullán, R. M., Ayala‐Peña, S., Sacher, J. R., Skoda, E. M., Wipf, P., Frontera, W. R., & Javadov, S. A. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.10.009 · Cited by 88
Self-citationMitochondrial Cyclophilin D in Vascular Oxidative Stress and Hypertension
Itani, H. A., Dikalova, A., McMaster, W. G., Nazarewicz, R. R., Bikineyeva, A. T., Harrison, D. G., & Dikalov, S. (2016) · Hypertension · doi:10.1161/hypertensionaha.115.07085 · Cited by 86
Domańska‐Janik, K., Bużańska, L., Dłużniewska, J., Kozłowska, H., Sarnowska, A., & Zabłocka, B. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2003.11.006 · Cited by 77
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Powers, C., Huang, Y., Strauss, A. W., & Khuchua, Z. A. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00074 · Cited by 68
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Huang, Y., Powers, C., Madala, S. K., Greis, K. D., Haffey, W. D., Towbin, J. A., Purevjav, E., Javadov, S. A., Strauss, A. W., & Khuchua, Z. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0128561 · Cited by 68
Self-citationRuiz‐Meana, M., Inserte, J., Fernández‐Sanz, C., García-Hernando, V., Miró‐Casas, E., Barba, I., & David Garcia-dorado, A. (2011) · Basic Research in Cardiology · doi:10.1007/s00395-011-0225-5 · Cited by 67
Javadov, S. A., Jang, S., Rodriguez, N., Rodríguez‐Zayas, A. E., Hernández, J. S., Krainz, T., Wipf, P., & Frontera, W. R. (2015) · Oncotarget · doi:10.18632/oncotarget.5783 · Cited by 67
Self-citationDeciphering of Mitochondrial Cardiolipin Oxidative Signaling in Cerebral Ischemia-Reperfusion
Ji, J., Baart, S., Vikulina, A. S., Clark, R. S. B., Anthonymuthu, T. S., Tyurin, V. A., Du, L., Croix, C. M. S., Tyurina, Y. Y., Lewis, J., et al. (2014) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2014.204 · Cited by 66
Self-citationAltered Proteome Biology of Cardiac Mitochondria Under Stress Conditions
Zhang, J., Liem, D. A., Mueller, M., Wang, Y., Zong, C., Deng, N., Vondriska, T. M., Kôrge, P., Drews, O., MacLellan, W. R., et al. (2008) · Journal of Proteome Research · doi:10.1021/pr070371f · Cited by 64
Barreto‐Torres, G., Parodi‐Rullán, R. M., & Javadov, S. A. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13067694 · Cited by 61
Self-citationKloner, R. A., & Longacre, L. S. (2011) · Journal of Cardiovascular Pharmacology and Therapeutics · doi:10.1177/1074248411402501 · Cited by 61
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Wong, R., Aponte, A. M., Steenbergen, C., & Murphy, E. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00515.2009 · Cited by 60
Brown, D. A., Sabbah, H. N., & Shaikh, S. R. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.07.005 · Cited by 52
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Esposti, M. D. (2001) · Methods in cell biology · doi:10.1016/s0091-679x(01)65005-2 · Cited by 51
Xu, A., Szczepanek, K., Maceyka, M. W., Ross, T., Bowler, E., Hu, Y., Kenny, B., Mehfoud, C., Desai, P. N., Baumgarten, C. M., et al. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00241.2013 · Cited by 46
Wang, P., & Powell, S. R. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.005 · Cited by 38
Jang, S., & Javadov, S. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113526 · Cited by 38
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Szczepanek, K., Allegood, J. C., Aluri, H. S., Hu, Y., Chen, Q., & Lesnefsky, E. J. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2015.12.004 · Cited by 20
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Husainy, M. A., Dickenson, J. M., & Galiñanes, M. (2010) · Journal of Surgical Research · doi:10.1016/j.jss.2010.11.879 · Cited by 11
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Metadata
- Authors
- Jang, S., Lewis, T. S., Powers, C., Khuchua, Z., Baines, C. P., Wipf, P., & Javadov, S.
- Affiliations
- University of Puerto Rico, Medical Sciences Campus (PR)
- University of Pittsburgh (US)
- Cincinnati Children's Hospital Medical Center (US)
- University of Missouri (US)
- Corresponding author
- Javadov, Sabzali
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2017-07
- Volume
- 27
- Issue
- 1
- Pages
- 57-69
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- PMC
- PMC5488255
- OpenAlex
- W2556127230
- Cited by
- 103
- References
- 69
- Citations by year
- 2026: 5 · 2025: 11 · 2024: 14 · 2023: 7 · 2022: 11 · 2021: 10 · 2020: 9 · 2019: 10 · 2018: 11 · 2017: 15
- FWCI
- 6.23
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL094404, SC1HL118669, R01HL108867)
- National Center for Research Resources (G12RR003051)
- National Institute on Minority Health and Health Disparities (G12MD007600)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Ischemia and Reperfusion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial supercomplexes, electron transport chain, cardiac ischemia-reperfusion, mitochondrial permeability transition pore, mitochondrial reactive oxygen species, cardiolipin, tafazzin, sanglifehrin A, oxidative stress, calcium overload, mitochondrial dysfunction
- MeSH terms
- Mitochondrial Permeability Transition Pore, Animals, Cyclic N-Oxides, Disease Models, Animal, Electron Transport, Female, Lactones, Male, Mitochondria, Heart, Spiro Compounds, Myocardial Reperfusion Injury, Reactive Oxygen Species, Oxidative Stress, Mitochondrial Membrane Transport Proteins, Rats
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