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Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo during stress-induced apoptosis
Abstract
Voltage-dependent anion channel (VDAC)1 is the main channel of the mitochondrial outer membrane (MOM) and it has been proposed to be part of the permeability transition pore (PTP), a putative multiprotein complex candidate agent of the mitochondrial permeability transition (MPT). Working at the single live cell level, we found that overexpression of VDAC1 triggers MPT at the mitochondrial inner membrane (MIM). Conversely, silencing VDAC1 expression results in the inhibition of MPT caused by selenite-induced oxidative stress. This MOM-MIM crosstalk was modulated by Cyclosporin A and mitochondrial Cyclophilin D, but not by Bcl-2 and Bcl-X(L), indicative of PTP operation. VDAC1-dependent MPT engages a positive feedback loop involving reactive oxygen species and p38-MAPK, and secondarily triggers a canonical apoptotic response including Bax activation, cytochrome c release and caspase 3 activation. Our data thus support a model of the PTP complex involving VDAC1 at the MOM, and indicate that VDAC1-dependent MPT is an upstream mechanism playing a causal role in oxidative stress-induced apoptosis.
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“In particular, the outer membrane transporter VDAC has been shown, by several studies, to control mPTP activity [6,22,23,24,25,26,27].”
From The mitochondrial permeability transition: Nexus of aging, disease and longevity (2021) · cites this paper as [22]
Citations
Cites
Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598
Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178
Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis
Chipuk, J. E., Kuwana, T., Bouchier-Hayes, L., Droin, N. M., Newmeyer, D. D., Schuler, M., & Green, D. R. (2004) · Science · doi:10.1126/science.1092734 · Cited by 2,108
Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792
RAS–RAF–MEK-dependent oxidative cell death involving voltage-dependent anion channels
Yagoda, N., von Rechenberg, M., Zaganjor, E., Bauer, A. J., Yang, W. S., Fridman, D. J., Wolpaw, A. J., Smukste, I., Peltier, J. M., Boniface, J. J., et al. (2007) · Nature · doi:10.1038/nature05859 · Cited by 1,631
Mitochondrial Transport of Cations: Channels, Exchangers, and Permeability Transition
Bernardi, P. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1127 · Cited by 1,546
Reactive Oxygen Species (Ros-Induced) Ros Release
Zorov, D. B., Filburn, C. R., Klotz, L.-O., Zweier, J. L., & Sollott, S. J. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.7.1001 · Cited by 1,412
The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
Goldstein, J. C., Waterhouse, N. J., Juin, P. P., Evan, G. I., & Green, D. R. (2000) · Nature Cell Biology · doi:10.1038/35004029 · Cited by 1,073
Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death
Baines, C. P., Kaiser, R. A., Sheiko, T., Craigen, W. J., & Molkentin, J. D. (2007) · Nature Cell Biology · doi:10.1038/ncb1575 · Cited by 971
Han, D., Antunes, F., Canali, R., Rettori, D., & Cadenas, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210269200 · Cited by 711
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Shoshan‐Barmatz, V., Pinto, V. D., Zweckstetter, M., Raviv, Z., Keinan, N., & Arbel, N. (2010) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2010.03.002 · Cited by 824
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Reactive Oxygen Species in Skeletal Muscle Signaling
Barbieri, E., & Sestili, P. (2011) · Journal of Signal Transduction · doi:10.1155/2012/982794 · Cited by 433
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Ham, P. B., & Raju, R. P. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.06.006 · Cited by 374
Is mPTP the gatekeeper for necrosis, apoptosis, or both?
Kinnally, K. W., Peixoto, P. M. V., Ryu, S.-Y., & Dejean, L. M. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.09.013 · Cited by 349
VDAC1 selectively transfers apoptotic Ca2+ signals to mitochondria
Stefani, D. D., Bononi, A., Romagnoli, A., Messina, A. A., Pinto, V. D., Pinton, P., & Rizzuto, R. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.92 · Cited by 330
Self-citationMitochondrial Channels: Ion Fluxes and More
Szabó, I., & Zoratti, M. (2014) · Physiological Reviews · doi:10.1152/physrev.00021.2013 · Cited by 330
Misfolded Mutant SOD1 Directly Inhibits VDAC1 Conductance in a Mouse Model of Inherited ALS
Israelson, A., Arbel, N., Cruz, S. D., Ilieva, H. S., Yamanaka, K., Shoshan‐Barmatz, V., & Cleveland, D. W. (2010) · Neuron · doi:10.1016/j.neuron.2010.07.019 · Cited by 329
The path from mitochondrial ROS to aging runs through the mitochondrial permeability transition pore
Rottenberg, H., & Hoek, J. B. (2017) · Aging Cell · doi:10.1111/acel.12650 · Cited by 275
Keinan, N., Tyomkin, D., & Shoshan‐Barmatz, V. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00165-10 · Cited by 280
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Shoshan‐Barmatz, V., Ben-Hail, D., Admoni, L., Krelin, Y., & Tripathi, S. S. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.10.040 · Cited by 255
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Zhou, B., Kreuzer, J., Kumsta, C., Wu, L., Kamer, K. J., Cedillo, L., Zhang, Y., Li, S., Kacergis, M. C., Webster, C. M., et al. (2019) · Cell · doi:10.1016/j.cell.2019.02.013 · Cited by 220
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Lee, E. A., Angka, L., Rota, S.-G., Hanlon, T., Mitchell, A. S., Hurren, R., Wang, X. M., Gronda, M., Boyacı, E., Bojko, B., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-2676 · Cited by 179
Dai, D.-F., Hsieh, E. J., Liu, Y., Chen, T., Beyer, R. P., Chin, M. T., MacCoss, M. J., & Rabinovitch, P. S. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvr274 · Cited by 178
VDAC1 at the crossroads of cell metabolism, apoptosis and cell stress
Shoshan-Barmatz, V., N. Maldonado, E., & Krelin, Y. (2017) · Cell Stress · doi:10.15698/cst2017.10.104 · Cited by 170
Characterization of human VDAC isoforms: A peculiar function for VDAC3?
Pinto, V. D., Guarino, F., Guarnera, A., Messina, A. A., Reina, S., Tomasello, M. F., Palermo, V., & Mazzoni, C. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.031 · Cited by 159
Self-citationVDAC1 functions in Ca2+ homeostasis and cell life and death in health and disease
Shoshan‐Barmatz, V., Krelin, Y., & Shteinfer‐Kuzmine, A. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.06.007 · Cited by 165
Shoshan‐Barmatz, V., Keinan, N., Abu‐Hamad, S., Tyomkin, D., & Aram, L. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.03.003 · Cited by 155
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Shoshan‐Barmatz, V., & Golan, M. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712798992110 · Cited by 142
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Shoshan‐Barmatz, V., De, S., & Meir, A. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00060 · Cited by 127
Tan, K., Fujimoto, M., Takii, R., Takaki, E., Hayashida, N., & Nakai, A. (2015) · Nature Communications · doi:10.1038/ncomms7580 · Cited by 123
Cyclophilin D Deficiency Rescues Axonal Mitochondrial Transport in Alzheimer’s Neurons
Guo, L., Du, H., Yan, S., Wu, X., McKhann, G. M., Chen, J. X., & Yan, S. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054914 · Cited by 118
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Algor, S. W., Keinan, N., Ben-Hail, D., Arif, T., & Shoshan‐Barmatz, V. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.03.021 · Cited by 108
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Reina, S., Checchetto, V., Saletti, R., Gupta, A., Chaturvedi, D., Guardiani, C., Guarino, F., Scorciapino, M. A., Magrì, A., Foti, S., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.6850 · Cited by 94
Self-citationThe role of mitophagy in innate immune responses triggered by mitochondrial stress
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Luo, Z., Yao, J., Wang, Z., & Xu, J. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04286-1 · Cited by 90
Leone, A., Roca, M. S., Ciardiello, C., Terranova-Barberio, M., Vitagliano, C., Ciliberto, G., Mancini, R., Gennaro, E. D., Bruzzese, F., & Budillon, A. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.07.155 · Cited by 84
Wang, Y., Li, Y., Xue, H., Pritchard, H. W., & Wang, X. (2014) · The Plant Journal · doi:10.1111/tpj.12737 · Cited by 85
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Self-citationZhang, X., Liang, D., Lian, X., Jiang, Y., He, H., Liang, W., Zhao, Y., & Chi, Z. (2016) · APOPTOSIS · doi:10.1007/s10495-016-1234-5 · Cited by 74
Tomasello, M. F., Guarino, F., Reina, S., Messina, A. A., & Pinto, V. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081522 · Cited by 72
Self-citationMagrì, A., Belfiore, R., Reina, S., Tomasello, M. F., Rosa, M. C. D., Guarino, F., Leggio, L., Pinto, V. D., & Messina, A. A. (2016) · Scientific Reports · doi:10.1038/srep34802 · Cited by 70
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Chen, W., Guo, C., Feng, H., & Chen, Y. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.615451 · Cited by 64
Chen, H., Gao, W., Yang, Y., Guo, S., Wang, H., Wang, W., Zhang, S., Zhou, Q., Xu, H., Yao, J., et al. (2014) · APOPTOSIS · doi:10.1007/s10495-014-1045-5 · Cited by 62
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Shen, X. L., Zhang, Y., Xu, W., Liang, R., Zheng, J., Luo, Y., Wang, Y., & Huang, K. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.10.010 · Cited by 57
Qian, B., Jiang, R.-J., Song, J., & Wang, C.-Q. (2022) · Chemosphere · doi:10.1016/j.chemosphere.2022.136345 · Cited by 56
Niedźwiecka, K., Tisi, R., Penna, S., Lichocka, M., Płochocka, D., & Kucharczyk, R. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.10.003 · Cited by 58
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Amodeo, G. F., Scorciapino, M. A., Messina, A. A., Pinto, V. D., & Ceccarelli, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103879 · Cited by 50
Self-citationShi, T.-F., Zhou, Z., Jiang, W., Huang, T.-L., Si, J., & Li, L. (2024) · Redox Report · doi:10.1080/13510002.2024.2382943 · Cited by 49
Guo, B., Yang, M., Liang, D., Yang, L., Cao, J., & Zhang, L. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-1105-x · Cited by 49
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Huang, Q., Ma, B., Su, Y., Chan, K., Qu, H., Huang, J., Wang, D., Qiu, J., Liu, H., Yang, X., et al. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.42019 · Cited by 45
An, E., Narayanan, M., Manes, N. P., & Nita‐Lazar, A. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.034371 · Cited by 42
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Self-citationKoul, M., Kumar, A., Deshidi, R., Sharma, V., Singh, R. D., Singh, J., Sharma, P. R., Shah, B. A., Jaglan, S., & Singh, S. K. (2017) · BMC Cell Biology · doi:10.1186/s12860-017-0141-0 · Cited by 40
Li, Y., He, X., Yang, X., Huang, K., Luo, Y., Zhu, L., Li, Y., & Xu, W. (2015) · Scientific Reports · doi:10.1038/srep14277 · Cited by 40
Ghio, A. J., Soukup, J. M., Dailey, L. A., & Madden, M. C. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.007 · Cited by 39
Fang, Y.-D., Xu, X., Dang, Y.-M., Zhang, Y., Zhang, J.-P., Hu, J., Zhang, Q., Dai, X., Teng, M., Zhang, D., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028052 · Cited by 40
Joo, H. K., Lee, Y. R., Lim, S., Lee, E. J., Choi, S., Cho, E., Park, M. S., Ryoo, S., Park, J. B., & Jeon, B. H. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.03.049 · Cited by 38
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Gałgańska, H., Karachitos, A., Wojtkowska, M., Stobienia, O., Budzińska, M., & Kmita, H. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.004 · Cited by 40
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Lenhausen, A. M., Wilkinson, A. S., Lewis, E. M., Dailey, K. M., Scott, A. J., Khan, S., & Wilkinson, J. C. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00306 · Cited by 37
Li, K., Sun, J., Yang, J., Roberts, S. M., Zhang, X., Cui, X., Wei, S., & Ma, L. Q. (2017) · Environmental Science & Technology · doi:10.1021/acs.est.7b02690 · Cited by 33
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Hsiao, C., Wang, D., Kaushal, A., Chen, M., & Saligan, L. N. (2014) · Journal of Pain and Symptom Management · doi:10.1016/j.jpainsymman.2014.03.010 · Cited by 33
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Zhao, Z., Song, X., Wang, Y., Yu, L., Huang, G., Li, Y., Zong, R., Liu, T., Ji, Q., Zheng, Y., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01334-1 · Cited by 32
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Giusti, L., Cetani, F., Ciregia, F., Valle, Y. D., Donadio, E., Giannaccini, G., Banti, C., Pardi, E., Saponaro, F., Basolo, F., et al. (2010) · Molecular BioSystems · doi:10.1039/c0mb00191k · Cited by 32
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Rai, N., Gupta, P., Verma, A. K., Tiwari, R. K., Madhukar, P., Kamble, S. C., Kumar, A., Kumar, R., Singh, S. K., & Gautam, V. (2023) · ACS Omega · doi:10.1021/acsomega.2c05746 · Cited by 31
Wang, Y., Peng, X., Yang, Z., Zhao, W., Xu, W., Hao, J., Wu, W., Shen, X. L., Luo, Y., & Huang, K. (2017) · Toxins · doi:10.3390/toxins9050167 · Cited by 28
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Joo, H. K., Lee, Y. R., Kang, G., Choi, S., Kim, C., Ryoo, S., Park, J. B., & Jeon, B. H. (2015) · Molecules and Cells · doi:10.14348/molcells.2015.0165 · Cited by 28
Fiocchetti, M., Cipolletti, M., Brandi, V., Polticelli, F., & Ascenzi, P. (2017) · Journal of Molecular Recognition · doi:10.1002/jmr.2654 · Cited by 28
Hseu, Y., Thiyagarajan, V., Ou, T., & Yang, H. (2017) · Archives of Toxicology · doi:10.1007/s00204-017-2050-6 · Cited by 28
Yang, J., Zhong, Y.-T., Hao, W.-N., Liu, X.-X., Shen, Q. “., Li, Y.-F., Ren, S., Wang, Z., Li, W., & Zhao, L. (2020) · RSC Advances · doi:10.1039/d0ra00020e · Cited by 27
RetractedMo, X., Li, X., She, C., Lu, X., Xiao, C., Wang, S.-H., & Huang, G. (2018) · Brain Research · doi:10.1016/j.brainres.2018.09.037 · Cited by 27
Li, S., Wang, T., Zhai, L., Ge, K., Zhao, J., Cong, W., & Guo, Y. (2017) · Journal of Molecular Neuroscience · doi:10.1007/s12031-017-1012-z · Cited by 26
Messina, A. A., Reina, S., Guarino, F., Magrì, A., Tomasello, M. F., Clark, R. E., Ramsay, R. R., & Pinto, V. D. (2014) · Molecular BioSystems · doi:10.1039/c4mb00237g · Cited by 26
Self-citationMazure, N. M. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00193 · Cited by 25
Glucocorticoids can induce BIM to trigger apoptosis in the absence of BAX and BAK1
Li, D., & Vaux, D. L. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2599-5 · Cited by 24
Qi, Y., Mao, F.-F., Zhou, Z.-Q., Liu, D., MinYU, Deng, X., Li, J., & Mei, F. (2018) · PROTOPLASMA · doi:10.1007/s00709-018-1256-7 · Cited by 24
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Guardiani, C., Scorciapino, M. A., Amodeo, G., Grdadolnik, J., Pappalardo, G., Pinto, V. D., Ceccarelli, M., & Casu, M. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00469 · Cited by 20
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Ghio, A. J., Stonehuerner, J., Soukup, J. M., Dailey, L. A., Kesic, M. J., & Cohen, M. D. (2015) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2015.03.008 · Cited by 19
Shi, S., Zhang, W., Liu, X., Ren, X., Li, M., Sun, J., Wang, Y., Yue, T., & Wang, J. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.127749 · Cited by 18
Kalashnyk, O., Lykhmus, O., Uspenska, K., Izmailov, M., Комісаренко, С. В., & Skok, M. (2020) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2020.105879 · Cited by 18
Zeng, F., Wen, W., Cui, W., Zheng, W., Liu, Y., Sun, X., Hou, N., Ma, D., Yuan, Y., Shi, H., et al. (2018) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2018.10.015 · Cited by 16
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Self-citationColella, F., Scillitani, G., & Pierri, C. L. (2020) · Toxicology · doi:10.1016/j.tox.2020.152612 · Cited by 17
Sekigawa, A., Fujita, M., Sekiyama, K., Takamatsu, Y., Hatano, T., Rockenstein, E. M., Spada, A. R. L., Masliah, E., & Hashimoto, M. (2012) · Molecular Brain · doi:10.1186/1756-6606-5-34 · Cited by 15
Metadata
- Authors
- Tomasello, F., Messina, A., Lartigue, L., Schembri, L., Medina, C., Reina, S., Thoraval, D., Crouzet, M., Ichas, F., De Pinto, V., & De Giorgi, F.
- Affiliations
- University of Catania (IT)
- Inserm (FR)
- Centre National de la Recherche Scientifique (FR)
- Venue
- Cell Research
- Published
- 2009-08-11
- Volume
- 19
- Issue
- 12
- Pages
- 1363-1376
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- OpenAlex
- W2054828537
- Cited by
- 161
- References
- 71
- Citations by year
- 2026: 11 · 2025: 13 · 2024: 7 · 2023: 5 · 2022: 4 · 2021: 8 · 2020: 13 · 2019: 7 · 2018: 7 · 2017: 12 · 2016: 11 · 2015: 11 · 2014: 14 · 2013: 8 · 2012: 8
- FWCI
- 4.02
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cell Research (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Institut National de la Santé et de la Recherche Médicale
- Ligue Contre le Cancer
- Università di Catania
- Institut Bergonié
- 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
- VDAC1, mitochondrial permeability transition, mitochondrial permeability transition pore, mitochondrial outer membrane, inner mitochondrial membrane, oxidative stress-induced apoptosis, selenite, cyclosporine, cyclophilin D, reactive oxygen species, p38 MAPK, Bax activation, cytochrome c release, caspase-3
- MeSH terms
- Peptidyl-Prolyl Isomerase F, Animals, Cell Membrane Permeability, Chlorocebus aethiops, HeLa Cells, Humans, Stress, Physiological, Cyclosporine, Sodium Selenite, Oxidative Stress, COS Cells, Gene Silencing, Cyclophilins, Feedback, Physiological, Voltage-Dependent Anion Channel 1, Apoptosis Regulatory Proteins, Mitochondrial Membranes, Membrane Potential, Mitochondrial
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