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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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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