Cited by 2,280Mitochondrial Function and PathologyCell death mechanisms and regulationSignaling Pathways in Disease

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Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death

Baines, Christopher P., Kaiser, Robert A., Purcell, Nicole H., Blair, N. Scott, Osinska, Hanna, Hambleton, Michael A., Brunskill, Eric W., Sayen, M. Richard, Gottlieb, Roberta A., Dorn, Gerald W., Robbins, Jeffrey, Molkentin, Jeffery D.·2005·Nature

DOI 10.1038/nature03434

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Abstract

Mitochondria play a critical role in mediating both apoptotic and necrotic cell death. The mitochondrial permeability transition (mPT) leads to mitochondrial swelling, outer membrane rupture and the release of apoptotic mediators. The mPT pore is thought to consist of the adenine nucleotide translocator, a voltage-dependent anion channel, and cyclophilin D (the Ppif gene product), a prolyl isomerase located within the mitochondrial matrix. Here we generated mice lacking Ppif and mice overexpressing cyclophilin D in the heart. Ppif null mice are protected from ischaemia/reperfusion-induced cell death in vivo, whereas cyclophilin D-overexpressing mice show mitochondrial swelling and spontaneous cell death. Mitochondria isolated from the livers, hearts and brains of Ppif null mice are resistant to mitochondrial swelling and permeability transition in vitro. Moreover, primary hepatocytes and fibroblasts isolated from Ppif null mice are largely protected from Ca2+-overload and oxidative stress-induced cell death. However, Bcl-2 family member-induced cell death does not depend on cyclophilin D, and Ppif null fibroblasts are not protected from staurosporine or tumour-necrosis factor-alpha-induced death. Thus, cyclophilin D and the mitochondrial permeability transition are required for mediating Ca2+- and oxidative damage-induced cell death, but not Bcl-2 family member-regulated death.

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Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178
Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD‐specific caspase activation and independently of mitochondrial transmembrane depolarization
Bossy‐Wetzel, E., Newmeyer, D. D., & Green, D. R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.1.37 · Cited by 1,225
Bax and Adenine Nucleotide Translocator Cooperate in the Mitochondrial Control of Apoptosis
Marzo, I., Brenner, C., Zamzami, N., Jürgensmeier, J. M., Susin, S. A., Vieira, H. L. A., Prévost, M.-C., Xie, Z., Matsuyama, S., Reed, J. C., et al. (1998) · Science · doi:10.1126/science.281.5385.2027 · Cited by 1,168
The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
Kokoszka, J. E., Waymire, K. G., Levy, S. E., Sligh, J. E., Cai, J., Jones, D. P., MacGregor, G. R., & Wallace, D. C. (2004) · Nature · doi:10.1038/nature02229 · Cited by 1,086
A Distinct Pathway Remodels Mitochondrial Cristae and Mobilizes Cytochrome c during Apoptosis
Scorrano, L., Ashiya, M., Buttle, K., Weiler, S., Oakes, S. A., Mannella, C. A., & Korsmeyer, S. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(01)00116-2 · Cited by 1,072
Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
Narita, M., Shimizu, S., Ito, T., Chittenden, T., Lutz, R. J., Matsuda, H., & Tsujimoto, Y. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14681 · Cited by 942
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
The permeability transition pore complex: another view
Halestrap, A. P., McStay, G. P., & Clarke, S. J. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01375-5 · Cited by 709
Bax-induced Cytochrome C Release from Mitochondria Is Independent of the Permeability Transition Pore but Highly Dependent on Mg2+ Ions
Eskes, R., Antonsson, B., Osen-Sand, A., Montessuit, S., Richter, C., Sadoul, R., Mazzei, G., Nichols, A., & Martinou, J.-C. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.1.217 · Cited by 651
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

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Menze, M. A., Fortner, G., Nag, S., & Hand, S. C. (2009) · APOPTOSIS · doi:10.1007/s10495-009-0443-6 · Cited by 88
Mitochondrial dysfunction in nonalcoholic steatohepatitis
Serviddio, G., Bellanti, F., Vendemiale, G., & Altomare, E. (2011) · Expert Review of Gastroenterology & Hepatology · doi:10.1586/egh.11.11 · Cited by 87
Calcium Signaling in Liver Injury and Regeneration
Oliva‐Vilarnau, N., Hankeová, S., Vorrink, S. U., Mkrtchian, S., Andersson, E. R., & Lauschke, V. M. (2018) · Frontiers in Medicine · doi:10.3389/fmed.2018.00192 · Cited by 85
Cyclophilin D-mediated regulation of the permeability transition pore is altered in mice lacking the mitochondrial calcium uniporter
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 87
Cell death regulation by MAMs: from molecular mechanisms to therapeutic implications in cardiovascular diseases
Li, Y. E., Sowers, J. R., Hetz, C. A., & Ren, J. T. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04942-2 · Cited by 90
Mitochondrial injury in pancreatitis
Mukherjee, R., Criddle, D. N., GUKVOSKAYA, A., Pandol, S. J., Petersen, O. H., & Sutton, R. (2008) · Cell Calcium · doi:10.1016/j.ceca.2007.11.013 · Cited by 87
Sulforaphane inhibits mitochondrial permeability transition and oxidative stress
Greco, T., Shafer, J. R., & Fiskum, G. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.09.017 · Cited by 85
Reactive oxygen species‐provoked mitochondria‐dependent cell death during ageing of elm (Ulmus pumila L.) seeds
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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Dietl, A., & Maack, C. (2017) · Current Heart Failure Reports · doi:10.1007/s11897-017-0347-7 · Cited by 89
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Gukovsky, I., Pandol, S. J., & Gukovskaya, A. S. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4068 · Cited by 87
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Schmidpeter, P. A. M., & Schmid, F. X. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.01.023 · Cited by 85
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Zhao, X., Khan, N., Gan, H. T., Tzelepis, F., Nishimura, T., Park, S.-Y., Divangahi, M., & Remold, H. G. (2017) · Mucosal Immunology · doi:10.1038/mi.2017.12 · Cited by 80
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Vianello, A., Casolo, V., Petrussa, E., Peresson, C., Patui, S., Bertolini, A. M., Passamonti, S., Braidot, E., & Zancani, M. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.06.620 · Cited by 85
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Panel, M., Ruiz, I., Brillet, R., Lafdil, F., Teixeira-Clerc, F., Nguyễn, C. T., Caldéraro, J., Gelin, M., Allemand, F., Guichou, J., et al. (2019) · Gastroenterology · doi:10.1053/j.gastro.2019.07.026 · Cited by 86
Cyclosporin A Has Direct Effects on Adult Neural Precursor Cells
Hunt, J., Cheng, A., Hoyles, A., Jervis, E., & Morshead, C. M. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5991-09.2010 · Cited by 82
Inhibition of mitochondrial permeability transition pore opening: translation to patients
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Mitochondria “THE” target of myocardial conditioning
Boengler, K., Lochnit, G., & Schulz, R. (2018) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00124.2018 · Cited by 82

Authors: 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., Robbins, J., & Molkentin, J. D.
Affiliations: Cincinnati Children's Hospital Medical Center (US)
Scripps Research Institute (US)
Corresponding author: Molkentin, Jeffery D.
ORCID: Baines, Christopher P.
Kaiser, Robert A.
Purcell, Nicole H.
Gottlieb, Roberta A.
Dorn, Gerald W.
Robbins, Jeffrey
Molkentin, Jeffery D.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2005-03
Volume: 434
Issue: 7033
Pages: 658-662
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature03434
OpenAlex: W2074800090
Cited by: 2,280
References: 28
Citations by year: 2026: 65 · 2025: 72 · 2024: 50 · 2023: 73 · 2022: 82 · 2021: 94 · 2020: 106 · 2019: 85 · 2018: 111 · 2017: 108 · 2016: 122 · 2015: 119 · 2014: 144 · 2013: 114 · 2012: 156
FWCI: 43.92
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: cyclophilin D, mitochondrial permeability transition, mitochondrial swelling, ischemia-reperfusion injury, calcium overload, oxidative stress, cell death, Bcl-2 family proteins, staurosporine, TNF-α, adenine nucleotide translocase, voltage-dependent anion channel, peptidyl-prolyl isomerase, heart, hepatocytes, fibroblasts
MeSH terms: Peptidyl-Prolyl Isomerase F, Adenoviridae, Animals, Atractyloside, Brain, Calcium, Carrier Proteins, Cells, Cultured, Fibroblasts, Hydrogen Peroxide, Liver, Mice, Transgenic, Mitochondria, Mitochondrial Swelling, Cell Death, Gene Deletion, Mice, Knockout, Oxidative Stress, Proto-Oncogene Proteins c-bcl-2, Caspases, Cyclophilins, Myocytes, Cardiac, Cytochromes c, BH3 Interacting Domain Death Agonist Protein, bcl-2-Associated X Protein, Mice

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Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death

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