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Fluctuations in mitochondrial membrane potential caused by repetitive gating of the permeability transition pore
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Confocal laser scanning microscopy and the potentiometric fluorescence probe tetramethylrhodamine ethyl ester were used to measure changes in membrane electrical potential (δΨm) in individual mitochondria after isolation or in the living cell. Recordings averaged over small mitochondrial populations revealed a gradual decline in δΨmcaused by the light-induced generation of free radicals. Depolarization was attenuated by dithiothreitol or acidification. In contrast, individual organelles displayed rapid spontaneous depolarizations caused by openings of the mitochondrial permeability transition pore (MTP). Repetitive openings and closings of the pore gave rise to marked fluctuations in δΨm between the fully charged and completely depolarized state. Rapid spontaneous fluctuations in δΨm were observed in mitochondria isolated from rat heart and in mitochondria in living endothelial cells. The loss of δΨm of mitochondria in the living cell coincided with swelling of the organelle and the breakdown of long mitochondrial filaments. In the individual mitochondrion, oxidative stress initially triggered pore openings of shorter duration, before prolonged openings caused the complete dissipation of δΨm and a measurable efflux of larger solutes. Generalizing this scheme, we suggest that under conditions of prolonged oxidative stress and/or cellular Ca2+ overload, short openings of MTP might serve as an emergency mechanism allowing the partial dissipation of δΨm, the fast release of accumulated Ca2+ ions and the decreased generation of endogenous oxygen radicals. In contrast, loss of matrix metabolites, swelling and other structural damage of the organelle render prolonged openings of the transition pore deleterious to mitochondria and to the cell.
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“Ion-channel function is also subject to modification by thiol reducing and oxidizing agents (73, 163, 164).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [164]
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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 2,410
THE MITOCHONDRIAL DEATH/LIFE REGULATOR IN APOPTOSIS AND NECROSIS
Kroemer, G., Dallaporta, B., & Resche-Rigon, M. (1998) · Annual Review of Physiology · doi:10.1146/annurev.physiol.60.1.619 · Cited by 1,975
Bereiter‐Hahn, J., & Vöth, M. (1994) · Microscopy Research and Technique · doi:10.1002/jemt.1070270303 · Cited by 900
Uncoupling: new approaches to an old problem of bioenergetics
Skulachev, V. P. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00091-1 · Cited by 893
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
Palmer, J. W., Tandler, B., & Hoppel, C. L. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75283-1 · Cited by 830
The Ca2+-induced membrane transition in mitochondria
Haworth, R. A., & Hunter, D. R. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90372-2 · Cited by 793
Ichas, F., Jouaville, L. S., & Mazat, J. (1997) · Cell · doi:10.1016/s0092-8674(00)80301-3 · Cited by 748
Broekemeier, K. M., Dempsey, M. E., & Pfeiffer, D. R. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83116-7 · Cited by 699
Petronilli, V., Miotto, G., Canton, M., Brini, M., Colonna, R., Bernardi, P., & Lisa, F. D. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77239-5 · Cited by 677
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Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471
Waterhouse, N. J., Goldstein, J. C., von Ahsen, O., Schüler, M., Newmeyer, D. D., & Green, D. R. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.2.319 · Cited by 460
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Robert, F. F. (2009) · Frontiers in bioscience · doi:10.2741/3303 · Cited by 448
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Effect of denervation on mitochondrially mediated apoptosis in skeletal muscle.
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Brown, D. A., & O'Rourke, B. P. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq231 · Cited by 228
Characteristics and possible functions of mitochondrial Ca2+ transport mechanisms
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The renaissance of mitochondrial pH
Domingo, J. S., & Demaurex, N. (2012) · The Journal of General Physiology · doi:10.1085/jgp.201110767 · Cited by 219
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Widlansky, M. E., & Gutterman, D. D. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3642 · Cited by 218
Bhamra, G. S., Hausenloy, D. J., Davidson, S. M., Carr, R. D., Paiva, M. S. A., Wynne, A. M., Mocanu, M. M., & Yellon, D. M. (2007) · Basic Research in Cardiology · doi:10.1007/s00395-007-0691-y · Cited by 211
Merlini, L., Angelin, A., Tiepolo, T., Braghetta, P., Sabatelli, P., Zamparelli, A., Ferlini, A., Maraldi, N. M., Bonaldo, P., & Bernardi, P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800962105 · Cited by 207
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Seidlmayer, L. K., Juettner, V. V., Kettlewell, S., Pavlov, E. V., Blatter, L. A., & Dedkova, E. N. (2015) · Cardiovascular Research · doi:10.1093/cvr/cvv097 · Cited by 192
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Penna, C. R. R., Perrelli, M.-G., & Pagliaro, P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4459 · Cited by 182
Alexandratou, E., Yova, D. M., Handris, P., Kletsas, D., & Loukas, S. (2002) · Photochemical & Photobiological Sciences · doi:10.1039/b110213n · Cited by 175
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The permeability transition pore as a Ca2+ release channel: New answers to an old question
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Mitochondrial permeability transition pore as a target for cardioprotection in the human heart
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Briston, T., Roberts, M., Lewis, S., Powney, B., M. Staddon, J., Szabadkai, G., & Duchen, M. R. (2017) · Scientific Reports · doi:10.1038/s41598-017-10673-8 · Cited by 152
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Nadtochiy, S. M., Tompkins, A. J., & Brookes, P. S. (2006) · Biochemical Journal · doi:10.1042/bj20051927 · Cited by 127
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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
Obame, F. N., Plin, C., Assaly, R., Zini, R., Dubois‐Randé, J., Berdeaux, A., & Morin, D. (2008) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.108.138008 · Cited by 118
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Millar, T. M., Phan, V., & Tibbles, L. A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.01.015 · Cited by 103
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Pouvreau, S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013035 · Cited by 100
Pravdić, D., Sedlić, F., Mio, Y., Vladic, N., Bienengraeber, M., & Bosnjak, Z. J. (2009) · Anesthesiology · doi:10.1097/aln.0b013e3181a91957 · Cited by 100
Javadov, S. A., Jang, S., Parodi‐Rullán, R. M., Khuchua, Z. A., & Kuznetsov, A. V. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2502-4 · Cited by 101
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Metadata
- Authors
- HüSER, J., & BLATTER, L. A.
- Affiliations
- Loyola University Chicago (US)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1999-10-08
- Volume
- 343
- Issue
- 2
- Pages
- 311-317
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1220555
- OpenAlex
- W2018776448
- Cited by
- 266
- References
- 28
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 2 · 2023: 10 · 2022: 8 · 2021: 11 · 2020: 6 · 2019: 9 · 2018: 7 · 2017: 13 · 2016: 16 · 2015: 11 · 2014: 15 · 2013: 14 · 2012: 17
- FWCI
- 1.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- Deutsche Forschungsgemeinschaft
- 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
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Ischemia and Reperfusion
- Keywords
- mitochondrial membrane potential, mitochondrial permeability transition pore, pore gating, membrane potential fluctuations, mitochondrial depolarization, oxidative stress, calcium overload, mitochondrial swelling, mitochondrial calcium release, oxygen free radicals, dithiothreitol, endothelial cells, heart mitochondria
- MeSH terms
- Mitochondrial Permeability Transition Pore, Animals, Calcium, Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone, Cattle, Cells, Cultured, Dithiothreitol, Electric Conductivity, Endothelium, Vascular, Fluorescence, Heart Ventricles, Hydrogen-Ion Concentration, Intracellular Membranes, Ion Channels, Membrane Potentials, Membrane Proteins, Mitochondria, Mitochondria, Heart, Permeability, Pulmonary Artery, Rhodamines, Oxidative Stress, Mitochondrial Membrane Transport Proteins, Rats
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