Cited by 809Mitochondrial Function and PathologySignaling Pathways in DiseaseATP Synthase and ATPases Research

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Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D

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Basso, Emy, Fante, Lisa, Fowlkes, Jonathan, Petronilli, Valeria, Forte, Michael A., Bernardi, Paolo·2005·Journal of Biological Chemistry

DOI 10.1074/jbc.c500089200

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Abstract

We have studied the properties of the permeability transition pore (PTP) in mitochondria from the liver of mice where the Ppif gene encoding for mitochondrial Cyclophilin D (CyP-D) had been inactivated. Mitochondria from Ppif-/- mice had no CyP-D and displayed a striking desensitization of the PTP to Ca2+, in that pore opening required about twice the Ca2+ load necessary to open the pore in strain-matched, wild-type mitochondria. Mitochondria lacking CyP-D were insensitive to Cyclosporin A (CsA), which increased the Ca2+ retention capacity only in mitochondria from wild-type mice. The PTP response to ubiquinone 0, depolarization, pH, adenine nucleotides, and thiol oxidants was similar in mitochondria from wild-type and Ppif-/- mice. These experiments demonstrate that (i) the PTP can form and open in the absence of CyP-D, (ii) that CyP-D represents the target for PTP inhibition by CsA, and (iii) that CyP-D modulates the sensitivity of the PTP to Ca2+ but not its regulation by the proton electrochemical gradient, adenine nucleotides, and oxidative stress. These results have major implications for our current understanding of the PTP and its modulation in vitro and in vivo.

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Authors: Basso, E., Fante, L., Fowlkes, J., Petronilli, V., Forte, M. A., & Bernardi, P.
Affiliations: University of Padua (IT)
Oregon Health & Science University (US)
Corresponding author: Forte, Michael A.
Bernardi, Paolo
ORCID: Basso, Emy
Petronilli, Valeria
Forte, Michael A.
Bernardi, Paolo
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2005-05
Volume: 280
Issue: 19
Pages: 18558-18561
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.c500089200
OpenAlex: W1971608015
Cited by: 808
References: 44
Citations by year: 2026: 10 · 2025: 12 · 2024: 11 · 2023: 21 · 2022: 20 · 2021: 32 · 2020: 27 · 2019: 31 · 2018: 35 · 2017: 36 · 2016: 34 · 2015: 45 · 2014: 71 · 2013: 36 · 2012: 48
FWCI: 19.20
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5630 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Padua Research Archive (University of Padova) (submittedVersion, cc-by)
INFM-OAR (INFN Catania) (submittedVersion, cc-by)
Funders: National Institute of General Medical Sciences (R01GM069883, GM 69883)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords: mitochondrial permeability transition pore, cyclophilin D, cyclosporine, calcium sensitivity, calcium retention capacity, mitochondrial permeability transition, proton gradient, adenine nucleotides, liver mitochondria
MeSH terms: Peptidyl-Prolyl Isomerase F, Alleles, Animals, Calcium, Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone, Diamide, Electrochemistry, Hydrogen-Ion Concentration, Liver, Mice, Inbred C57BL, Mice, Transgenic, Mitochondria, Mitochondria, Liver, Models, Genetic, Oxygen, Oxygen Consumption, Permeability, Protons, Benzoquinones, Cyclosporine, Oxidative Stress, Cyclophilins, Mitochondrial Proteins, Mice

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Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D

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