Reactive Oxygen Species (Ros-Induced) Ros Release
Open accessAbstract
We sought to understand the relationship between reactive oxygen species (ROS) and the mitochondrial permeability transition (MPT) in cardiac myocytes based on the observation of increased ROS production at sites of spontaneously deenergized mitochondria. We devised a new model enabling incremental ROS accumulation in individual mitochondria in isolated cardiac myocytes via photoactivation of tetramethylrhodamine derivatives, which also served to report the mitochondrial transmembrane potential, ΔΨ. This ROS accumulation reproducibly triggered abrupt (and sometimes reversible) mitochondrial depolarization. This phenomenon was ascribed to MPT induction because (a) bongkrekic acid prevented it and (b) mitochondria became permeable for calcein (∼620 daltons) concurrently with depolarization. These photodynamically produced “triggering” ROS caused the MPT induction, as the ROS scavenger Trolox prevented it. The time required for triggering ROS to induce the MPT was dependent on intrinsic cellular ROS-scavenging redox mechanisms, particularly glutathione. MPT induction caused by triggering ROS coincided with a burst of mitochondrial ROS generation, as measured by dichlorofluorescein fluorescence, which we have termed mitochondrial “ROS-induced ROS release” (RIRR). This MPT induction/RIRR phenomenon in cardiac myocytes often occurred synchronously and reversibly among long chains of adjacent mitochondria demonstrating apparent cooperativity. The observed link between MPT and RIRR could be a fundamental phenomenon in mitochondrial and cell biology.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
High levels of ROS may damage mitochondria, leading to opening of mitochondrial pores and loss of membrane polarization.
“High levels of ROS may damage mitochondria, leading to the opening of mitochondrial pores and allowing the influx of protons and ions, which leads to a loss of membrane polarization (13, 52).”
From Mitochondrial Dysfunction Contributes to Oncogene-Induced Senescence (2009) · cites this paper as [52]
An oxidant burst in one mitochondrion can spread oxidant production throughout the mitochondrial network via transient MPT pore formation, waves of reduction in mitochondrial potential, and propagation of oxidant bursts, at least in cardiomyocytes.
“An oxidant burst in one mitochondrion may also serve to spread oxidant production throughout the mitochondrial network in a manner that involves transient MPT pore formation, waves of reduction in mitochondrial potential, and propagation of oxidant bursts, at least in cardiomyocytes (48, 481).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [481]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Green, D. R., & Reed, J. C. (1998) · Science · doi:10.1126/science.281.5381.1309 · Cited by 8,998 · see citing works
[70] Determination of glutathione and glutathione disulfide in biological samples
Anderson, M. E. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(85)13073-9 · Cited by 2,755 · see citing works
The mitochondrial permeability transition pore and its role in cell death
CROMPTON, M. (1999) · Biochemical Journal · doi:10.1042/bj3410233 · Cited by 2,432 · see citing works
The mitochondrial permeability transition
Zoratti, M., & Szabó, I. (1995) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(95)00003-a · Cited by 2,395 · see citing works
Mechanisms by which mitochondria transport calcium
Gunter, T. E., & Pfeiffer, D. R. (1990) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1990.258.5.c755 · Cited by 1,640 · see citing works
Wink, D. A., & Mitchell, J. B. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00092-6 · Cited by 1,606 · see citing works
The cellular production of hydrogen peroxide
Boveris, A., Oshino, N., & Chance, B. (1972) · Biochemical Journal · doi:10.1042/bj1280617 · Cited by 1,549 · see citing works
Mitochondrial control of nuclear apoptosis.
Zamzami, N., Susín, S. A., Marchetti, P., Hirsch, T., Gomez-Monterrey, I. M., Castedo, M., & Kroemer, G. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.4.1533 · Cited by 1,360 · see citing works
Activation of the Cardiac Calcium Release Channel (Ryanodine Receptor) by Poly-S-Nitrosylation
Xu, L., Eu, J. P., Meissner, G., & Stamler, J. S. (1998) · Science · doi:10.1126/science.279.5348.234 · Cited by 991 · see citing works
The Ca2+-induced membrane transition in mitochondria
Hunter, D. R., & Haworth, R. A. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90371-0 · Cited by 860 · see citing works
Reactive oxygen species and programmed cell death
Jacobson, M. D. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)20008-8 · Cited by 753 · see citing works
Fabiato, A., & Fabiato, F. (1975) · The Journal of Physiology · doi:10.1113/jphysiol.1975.sp011026 · Cited by 685 · see citing works
Role of mitochondria in oxidative stress and ageing
Lenaz, G. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00120-0 · Cited by 650 · see citing works
Duchen, M. R. (1999) · The Journal of Physiology · doi:10.1111/j.1469-7793.1999.001aa.x · Cited by 610 · see citing works
Protection by Cyclosporin A of Ischemia/Reperfusion-Induced Damage in Isolated Rat Hearts
Griffiths, E. J., & Halestrap, A. P. (1993) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1993.1162 · Cited by 587 · see citing works
Ichas, F., & Mazat, J. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00119-4 · Cited by 570 · see citing works
The permeability transition pore as a mitochondrial calcium release channel: A critical appraisal
Bernardi, P., & Petronilli, V. (1996) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf02110643 · Cited by 467 · see citing works
Murphy, M. P. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00029-8 · Cited by 455 · see citing works
Nieminen, A. L., Saylor, A. K., Tesfai, S. A., Herman, B. A., & Lemasters, J. J. (1995) · Biochemical Journal · doi:10.1042/bj3070099 · Cited by 381 · see citing works
Integrating cytosolic calcium signals into mitochondrial metabolic responses
Gaspers, L. D., Burnett, P., Rutter, G. A., Denton, R. M., Rizzuto, R., & Thomas, A. P. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.4987 · Cited by 370 · see citing works
The Role of Reactive Oxygen Species in Mitochondrial Permeability Transition
Vercesi, A. E., Kowaltowski, A. J., Grijalba, M. T., Meinicke, A. R., & Castilho, R. F. (1997) · Bioscience Reports · doi:10.1023/a:1027335217774 · Cited by 325 · see citing works
Takeshige, K., & Minakami, S. (1979) · Biochemical Journal · doi:10.1042/bj1800129 · Cited by 299 · see citing works
Amchenkova, A. A., Bakeeva, L. E., Chentsov, Y. S., Skulachev, V. P., & Zorov, D. B. (1988) · The Journal of cell biology · doi:10.1083/jcb.107.2.481 · Cited by 284 · see citing works
Self-citationPetroff, M. V., Younès, A., Egan, J. M., Lakatta, E. G., & Sollott, S. J. (1999) · Circulation Research · doi:10.1161/01.res.84.9.1020 · Cited by 273 · see citing works
Self-citationImaging the Permeability Pore Transition in Single Mitochondria
Hüser, J., Rechenmacher, C. E., & Blatter, L. A. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77920-2 · Cited by 269 · see citing works
[8] Chemical depletion of glutathione in vivo
Plummer, J. L., Smith, B. R., Sies, H., & Bend, J. R. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(81)77010-1 · Cited by 236 · see citing works
Nitric oxide induces apoptosis via triggering mitochondrial permeability transition
Hortelano, S., Dallaporta, B., Zamzami, N., Hirsch, T., Susín, S. A., Marzo, I., Boscá, L., & Kroemer, G. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00623-6 · Cited by 234 · see citing works
Mechanical Transduction of Nitric Oxide Synthesis in the Beating Heart
Pinsky, D. J., Patton, S. R., Mesároš, Š., Brovkovych, V. M., Kubaszewski, E., Grunfeld, S., & Maliñski, T. (1997) · Circulation Research · doi:10.1161/01.res.81.3.372 · Cited by 233 · see citing works
Pro‐oxidants and mitochondrial Ca2+: their relationship to apoptosis and oncogenesis
Richter, C. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81423-w · Cited by 218 · see citing works
Reactive oxygen species as cellular messengers
Khan, A. U., & Wilson, T. (1995) · Chemistry & Biology · doi:10.1016/1074-5521(95)90259-7 · Cited by 215 · see citing works
Physiological role of mitochondrial Ca2+ transport
Hansford, R. G. (1994) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762734 · Cited by 215 · see citing works
Subcellular metabolic transients and mitochondrial redox waves in heart cells
Romashko, D. N., Marbán, E., & O'Rourke, B. P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1618 · Cited by 211 · see citing works
The mitochondrial site of superoxide formation
Nohl, H., & Jordan, W. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80529-0 · Cited by 207 · see citing works
Korshunov, S., Korkina, O. V., Ruuge, E. K., Skulachev, V. P., & Starkov, A. A. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01073-4 · Cited by 180 · see citing works
Opposite effects of nitric oxide and nitroxyl on postischemic myocardial injury
Ma, X. L., Gao, F., Gao-lin, L., Lopez, B. L., Christopher, T. A., Fukuto, J. M., Wink, D. A., & Feelisch, M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.25.14617 · Cited by 168 · see citing works
Capogrossi, M. C., Kort, A. A., Spurgeon, H. A., et al. (1986) · The Journal of General Physiology · doi:10.1085/jgp.88.5.589 · Cited by 153 · see citing works
Srivastava, R. K., Sollott, S. J., Khan, L., Hansford, R. G., Lakatta, E. G., & Longo, D. L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.8.5659 · Cited by 147 · see citing works
Self-citationMitochondrial Function in the Heart
WILLIAMSON, J. R. (1979) · Annual Review of Physiology · doi:10.1146/annurev.ph.41.030179.002413 · Cited by 117 · see citing works
Modulation of the Mitochondrial Permeability Transition by Nitric Oxide
Balakirev, M. Y., Khramtsov, V. V., & Zimmer, G. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00710.x · Cited by 112 · see citing works
Changes of the Fluidity of Mitochondrial Membranes Induced by the Permeability Transition
Ricchelli, F., Gobbo, S. D., Moreno, G. D., & Salet, C. (1999) · Biochemistry · doi:10.1021/bi9900828 · Cited by 92 · see citing works
Role of Mitochondria in Calcium Regulation of Spontaneously Contracting Cardiac Muscle Cells
Bowser, D. N., Minamikawa, T., Nagley, P., & Williams, D. A. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77642-8 · Cited by 79 · see citing works
Rhodamine dyes as potential agents for photochemotherapy of cancer in human bladder carcinoma cells.
Shea, C. R., Chen, N., Wimberly, J., et al. (1989) · PubMed · Cited by 64 · see citing works
Leist, M., Single, B., Naumann, H., Fava, E., Simon, B., Kühnle, S., & Nicotera, P. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0491 · Cited by 64 · see citing works
Gorbunov, N. V., Tyurina, Y. Y., Salama, G., Day, B. W., Claycamp, H. G., Argyros, G. J., Elsayed, N. M., & Kagan, V. E. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7951 · Cited by 45 · see citing works
Sokolove, P. M., & Kinnally, K. W. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0533 · Cited by 39 · see citing works
Malkevitch, N. V., Dedukhova, V. I., Simonian, R. A., et al. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00666-2 · Cited by 36 · see citing works
Signal Presequences Increase Mitochondrial Permeability and Open the Multiple Conductance Channel
Kushnareva, Y. E., Campo, M. L., Kinnally, K. W., & Sokolove, P. M. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1190 · Cited by 36 · see citing works
Nishihata, T., Caldwell, L. J., & Sakai, K. (1988) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(88)90216-9 · Cited by 8 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release
Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383 · see citing works
Self-citationMitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598 · see citing works
Reactive Oxygen Species in Metabolic and Inflammatory Signaling
Forrester, S. J., Kikuchi, D. S., Hernandes, M. S., Xu, Q., & Griendling, K. K. (2018) · Circulation Research · doi:10.1161/circresaha.117.311401 · Cited by 2,081 · see citing works
Mitochondria and reactive oxygen species
Kowaltowski, A. J., de Souza-Pinto, N. C., Castilho, R. F., & Vercesi, A. E. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.004 · Cited by 1,162 · see citing works
Inhibiting Mitochondrial Fission Protects the Heart Against Ischemia/Reperfusion Injury
Ong, S.-B., Subrayan, S., Lim, S. Y., Yellon, D. M., Davidson, S. M., & Hausenloy, D. J. (2010) · Circulation · doi:10.1161/circulationaha.109.906610 · Cited by 986 · see citing works
ROS, mitochondria and the regulation of autophagy
Scherz-Shouval, R., & Elazar, Z. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.07.009 · Cited by 954 · see citing works
Real-time imaging of the intracellular glutathione redox potential
Gutscher, M., Pauleau, A.-L., Marty, L., Brach, T., Wabnitz, G. H., Samstag, Y., Meyer, A. J., & Dick, T. P. (2008) · Nature Methods · doi:10.1038/nmeth.1212 · Cited by 894 · see citing works
NADPH oxidase 4 (Nox4) is a major source of oxidative stress in the failing heart
Kuroda, J., Ago, T., Matsushima, S., Zhai, P., Schneider, M. D., & Sadoshima, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002178107 · Cited by 772 · see citing works
Endothelial cell superoxide generation: regulation and relevance for cardiovascular pathophysiology
Li, J.-M., & Shah, A. M. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00124.2004 · Cited by 773 · see citing works
Superoxide flashes in single mitochondria
Wang, W., Fang, H., Groom, L., Cheng, A., Zhang, W., Liu, J., Wang, X., Li, K., Han, P., Zheng, M., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.017 · Cited by 715 · see citing works
NADPH Oxidases in Cardiovascular Health and Disease
Cave, A. C., Brewer, A. C., Narayanapanicker, A., Ray, R., Grieve, D. J., Walker, S., & Shah, A. M. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.691 · Cited by 630 · see citing works
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
Aon, M. A., Cortassa, S., Marbán, E., & O'Rourke, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302673200 · Cited by 521 · see citing works
Ago, T., Kuroda, J., Pain, J., Fu, C., Li, H., & Sadoshima, J. (2010) · Circulation Research · doi:10.1161/circresaha.109.213116 · Cited by 506 · see citing works
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471 · see citing works
Yu, T., Sheu, S.-S., Robotham, J. L., & Yoon, Y. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn104 · Cited by 462 · see citing works
An Attempt to Prevent Senescence: A Mitochondrial Approach
Skulachev, V. P., Anisimov, V. N., Antonenko, Y. N., Bakeeva, L. E., Chernyak, B. V., Erichev, V. P., Filenko, O. F., Kalinina, N. I., Kapelko, V. I., Kolosova, N. G., et al. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.12.008 · Cited by 430 · see citing works
Self-citationParone, P. A., Da Cruz, S., Tondera, D., Mattenberger, Y., James, D. I., Maechler, P., Barja, F., & Martinou, J.-C. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003257 · Cited by 415 · see citing works
Mitochondrial Dysfunction Contributes to Oncogene-Induced Senescence
Moiseeva, O., Bourdeau, V., Roux, A., Deschênes-Simard, X., & Ferbeyre, G. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01868-08 · Cited by 408 · see citing works
The role of mitochondria in protection of the heart by preconditioning
Halestrap, A. P., Clarke, S. J., & Khaliulin, I. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.05.008 · Cited by 390 · see citing works
Münzel, T., Gori, T., Keaney, J. F., Maack, C., & Daiber, A. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv305 · Cited by 394 · see citing works
Effects of ionizing radiation on mitochondria
Kam, W. W.-Y., & Banati, R. B. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.024 · Cited by 386 · see citing works
Endothelial Mitochondria: Contributing to Vascular Function and Disease
Davidson, S. M., & Duchen, M. R. (2007) · Circulation Research · doi:10.1161/01.res.0000261970.18328.1d · Cited by 381 · see citing works
Hausenloy, D., Wynne, A., Duchen, M., & Yellon, D. (2004) · Circulation · doi:10.1161/01.cir.0000126294.81407.7d · Cited by 366 · see citing works
The role of the mitochondrial permeability transition pore in heart disease
Halestrap, A. P., & Pasdois, P. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.12.017 · Cited by 362 · see citing works
TNF-α-induced ROS production triggering apoptosis is directly linked to Romo1 and Bcl-XL
Kim, J. J., Lee, S. B., Park, J. K., & Yoo, Y. D. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2010.19 · Cited by 344 · see citing works
Tai, H., Wang, Z., Gong, H., Han, X., Zhou, J., Wang, X., Wei, X., Ding, Y., Huang, N., Qin, J., et al. (2017) · Autophagy · doi:10.1080/15548627.2016.1247143 · Cited by 334 · see citing works
Mitochondrial pathways in sarcopenia of aging and disuse muscle atrophy
Calvani, R., Joseph, A.-M., Adhihetty, P. J., Miccheli, A., Bossola, M., Leeuwenburgh, C., Bernabei, R., & Marzetti, E. (2013) · bchm · doi:10.1515/hsz-2012-0247 · Cited by 328 · see citing works
Biochemical basis and metabolic interplay of redox regulation
Zhang, L., Wang, X., Cueto, R., Effi, C., Zhang, Y., Tan, H., Qin, X., Ji, Y., Yang, X., & Wang, H. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101284 · Cited by 308 · see citing works
Skeletal muscle insulin resistance: role of mitochondria and other ROS sources
Di Meo, S., Iossa, S., & Venditti, P. (2017) · Journal of Endocrinology · doi:10.1530/joe-16-0598 · Cited by 282 · see citing works
Kimura, S., Zhang, G.-X., Nishiyama, A., Shokoji, T., Yao, L., Fan, Y.-Y., Rahman, M., Suzuki, T., Maeta, H., & Abe, Y. (2005) · Hypertension · doi:10.1161/01.hyp.0000163462.98381.7f · Cited by 264 · see citing works
A Mitochondrial Oscillator Dependent on Reactive Oxygen Species
Cortassa, S., Aon, M. A., Winslow, R. L., & O’Rourke, B. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.041749 · Cited by 235 · see citing works
Redox interplay between mitochondria and peroxisomes
Lismont, C., Nordgren, M., Van Veldhoven, P. P., & Fransen, M. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00035 · Cited by 214 · see citing works
HANLEY, P., & DAUT, J. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.04.002 · Cited by 218 · see citing works
CaMKII induces permeability transition through Drp1 phosphorylation during chronic β-AR stimulation
Xu, S., Wang, P., Zhang, H., Gong, G., Gutierrez Cortes, N., Zhu, W., Yoon, Y., Tian, R., & Wang, W. (2016) · Nature Communications · doi:10.1038/ncomms13189 · Cited by 218 · see citing works
Molecular Mechanisms and Genetics of Oxidative Stress in Alzheimer’s Disease
Cioffi, F., Adam, R. H. I., & Broersen, K. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190863 · Cited by 204 · see citing works
“Moreover, cytosolic ROS was observed to induce signals leading to mPTP opening resulting in further ROS release and this phenomenon is referred to as “ROS-induced ROS release (RIRR)” [460].”
BackgroundValencia, A., & Kochevar, I. E. (2008) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700960 · Cited by 194 · see citing works
Loss of Mitofusin 2 Promotes Endoplasmic Reticulum Stress
Ngoh, G. A., Papanicolaou, K. N., & Walsh, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.359174 · Cited by 183 · see citing works
Moon, Y., Lee, K. H., Park, J., Geum, D., & Kim, K. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03112.x · Cited by 174 · see citing works
ROS-induced ROS release in vascular biology: redox-redox signaling
Zinkevich, N. S., & Gutterman, D. D. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01271.2010 · Cited by 163 · see citing works
Tomasello, F., Messina, A., Lartigue, L., Schembri, L., Medina, C., Reina, S., Thoraval, D., Crouzet, M., Ichas, F., De Pinto, V., et al. (2009) · Cell Research · doi:10.1038/cr.2009.98 · Cited by 161 · see citing works
V. Skulachev, M., N. Antonenko, Y., N. Anisimov, V., V. Chernyak, B., A. Cherepanov, D., A. Chistyakov, V., V. Egorov, M., G. Kolosova, N., A. Korshunova, G., G. Lyamzaev, K., et al. (2011) · Current Drug Targets · doi:10.2174/138945011795528859 · Cited by 156 · see citing works
Mitochondrial contact sites: their role in energy metabolism and apoptosis
Brdiczka, D. G., Zorov, D. B., & Sheu, S.-S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.09.007 · Cited by 150 · see citing works
Self-citationDILISA, F., & BERNARDI, P. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.02.009 · Cited by 139 · see citing works
Mechanisms of Sudden Cardiac Death: Oxidants and Metabolism
Yang, K.-C., Kyle, J. W., Makielski, J. C., & Dudley, S. C. (2015) · Circulation Research · doi:10.1161/circresaha.116.304691 · Cited by 127 · see citing works
Brady, N. R., Elmore, S. P., van Beek, J. J. H. G. M., Krab, K., Courtoy, P. J., Hue, L., & Westerhoff, H. V. (2004) · Biophysical Journal · doi:10.1529/biophysj.103.035097 · Cited by 118 · see citing works
Agarwal, R., MacMillan-Crow, L. A., Rafferty, T. M., Saba, H., Roberts, D. W., Fifer, E. K., James, L. P., & Hinson, J. A. (2011) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.176321 · Cited by 116 · see citing works
Autophagy as a Potential Target for Sarcopenia: AUTOPHAGY REGULATION IN SARCOPENIA
Fan, J., Kou, X., Jia, S., Yang, X., Yang, Y., & Chen, N. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25260 · Cited by 101 · see citing works
Joseph, L. C., Barca, E., Subramanyam, P., Komrowski, M., Pajvani, U., Colecraft, H. M., Hirano, M., & Morrow, J. P. (2016) · PLOS ONE · doi:10.1371/journal.pone.0145750 · Cited by 99 · see citing works
Detaille, D., Vial, G., Borel, A.-L., Cottet-Rouselle, C., Hallakou-Bozec, S., Bolze, S., Fouqueray, P., & Fontaine, E. (2016) · Cell Death Discovery · doi:10.1038/cddiscovery.2015.72 · Cited by 99 · see citing works
Chelko, S. P., Keceli, G., Carpi, A., Doti, N., Agrimi, J., Asimaki, A., Beti, C. B., Miyamoto, M., Amat-Codina, N., Bedja, D., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abf0891 · Cited by 92 · see citing works
Redox implications in adipose tissue (dys)function-A new look at old acquaintances
Jankovic, A., Korac, A., Buzadzic, B., Otasevic, V., Stancic, A., Daiber, A., & Korac, B. (2015) · Redox Biology · doi:10.1016/j.redox.2015.06.018 · Cited by 91 · see citing works
Nox2 mediates skeletal muscle insulin resistance induced by a high fat diet
Souto Padron de Figueiredo, A., Salmon, A. B., Bruno, F., Jimenez, F., Martinez, H. G., Halade, G. V., Ahuja, S. S., Clark, R. A., DeFronzo, R. A., Abboud, H. E., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.626077 · Cited by 79 · see citing works
Triggering Mitochondrial Radical Release: A New Function for NADPH Oxidases
Brandes, R. P. (2005) · Hypertension · doi:10.1161/01.hyp.0000165019.32059.b2 · Cited by 79 · see citing works
Yin, X., Zheng, F., Pan, Q., Zhang, S., Yu, D., Xu, Z., & Li, H. (2015) · Journal of Molecular Endocrinology · doi:10.1530/jme-15-0101 · Cited by 67 · see citing works
Dynamics of the mitochondrial permeability transition pore: Transient and permanent opening events
Boyman, L., Coleman, A. K., Zhao, G., Wescott, A. P., Joca, H. C., Greiser, B. M., Karbowski, M., Ward, C. W., & Lederer, W. J. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.03.016 · Cited by 68 · see citing works
Mitochondrial health, the epigenome and healthspan
Aon, M. A., Cortassa, S., Juhaszova, M., & Sollott, S. J. (2016) · Clinical Science · doi:10.1042/cs20160002 · Cited by 66 · see citing works
Shimura, T., Kobayashi, J., Komatsu, K., & Kunugita, N. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1156276 · Cited by 55 · see citing works
Cardioprotection and thyroid hormones
Pingitore, A., Nicolini, G., Kusmic, C., Iervasi, G., Grigolini, P., & Forini, F. (2016) · Heart Failure Reviews · doi:10.1007/s10741-016-9545-8 · Cited by 51 · see citing works
Walia, V., Kaushik, D., Mittal, V., Kumar, K., Verma, R., Parashar, J., Akter, R., Rahman, M. H., Bhatia, S., Al-Harrasi, A., et al. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02617-1 · Cited by 47 · see citing works
Miao, Y., Xie, L., Song, J., Cai, X., Yang, J., Ma, X., Chen, S., & Xie, P. (2024) · Physiological Reports · doi:10.14814/phy2.15917 · Cited by 50 · see citing works
“…swelling and SOCS3 upregulation NMJ deterioration Bannow et al. (2022) the study also found that mitochondrial function within the muscle decreased during aging, as well as in response to altered neuronal redox status prior to NMJ deterioration or loss of muscle mass and force (Zorov et al., 2000).”
BackgroundJankauskas, S. S., Pevzner, I. B., Andrianova, N. V., Zorova, L. D., Popkov, V. A., Silachev, D. N., Kolosova, N. G., Plotnikov, E. Y., & Zorov, D. B. (2017) · Scientific Reports · doi:10.1038/srep44430 · Cited by 41 · see citing works
Self-citation
- Authors
- Zorov, D. B., Filburn, C. R., Klotz, L.-O., Zweier, J. L., & Sollott, S. J.
- Affiliations
- National Institutes of Health (US)
- Johns Hopkins University (US)
- Venue
- The Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2000-10-02
- Volume
- 192
- Issue
- 7
- Pages
- 1001-1014
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC2193314
- OpenAlex
- W2135314348
- Cited by
- 1,412
- References
- 48
- Citations by year
- 2026: 34 · 2025: 40 · 2024: 62 · 2023: 71 · 2022: 69 · 2021: 82 · 2020: 71 · 2019: 56 · 2018: 67 · 2017: 70 · 2016: 78 · 2015: 65 · 2014: 68 · 2013: 67 · 2012: 70
- FWCI
- 5.31
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL-38324, R01HL063744, HL52315, P50HL052315, HL 63744, R01HL038324)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- reactive oxygen species, mitochondrial permeability transition, cardiomyocytes, mitochondrial depolarization, mitochondrial membrane potential, bongkrekic acid, glutathione, mitochondrial ROS generation
- MeSH terms
- Animals, Calcium, Cells, Cultured, Fluorescent Dyes, Heart, Mitochondria, Heart, Myocardium, Oxidation-Reduction, Permeability, Proteins, Solubility, Sulfhydryl Compounds, Reactive Oxygen Species, 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 ›
Are you an author, or do you see a problem with this page? Request a review