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Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
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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“To date, peptidylprolyl isomerase F (PPIF; best known as cyclophilin D, CYPD) is the only protein whose in vivo requirement for MPT induction has been formally validated with robust genetic tools (although there is consensus around the notion that CYPD does not constitute the pore-forming unit of the PTPC) [376–379].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [376]
In the citing paper
“although there is consensus around the notion that CYPD does not constitute the pore-forming unit of the PTPC) [376–379].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [376]
In the citing paper
“Interestingly, at very high levels of Ca2+, cyclophilin D-deficient cells or cells treated with cyclosporin A still have an MPT response (25, 31, 167, 309).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [25]
In the citing paper
“In addition, in the absence of cyclophilin D, mice are more protected from cardiac damage after ischemia/reperfusion (25, 309);”
From Redox regulation of mitochondrial function (2012) · cites this paper as [25]
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“Indeed, deletion of the gene encoding CypD renders mitochondria resistant to Ca2+ overload– induced swelling and the heart and brain partially resistant to cell death due to ischemic injury (Baines et al., 2005; Nakagawa et al., 2005; Schinzel et al., 2005).”
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Metadata
- 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
- Venue
- Nature
- Published
- 2005-03
- Volume
- 434
- Issue
- 7033
- Pages
- 658-662
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- 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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