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Updated: Jul 9, 2026

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
Published on: June 1, 2022
The mitochondrial permeability transition pore.
Paolo Bernardi1, Michael Forte
1Department of Biomedical Sciences and CNR Institute of Neurosciences, University of Padova, Viale Giuseppe Colombo 3, I-35121 Padova, Italy.
The mitochondrial permeability transition pore (PTP) opening is critical in pathology, but its molecular components remain elusive. New inhibitors offer hope for defining the PTP
Area of Science:
- Mitochondrial physiology and pathophysiology
- Molecular biology of ion channels
Background:
- The mitochondrial permeability transition pore (PTP) regulates inner membrane permeability to small solutes.
- PTP opening is implicated in various pathological conditions, yet its molecular composition is unknown.
- Previous studies questioned the roles of adenine nucleotide translocators and voltage-dependent anion channel in PTP formation.
Purpose of the Study:
- To investigate the molecular basis of mitochondrial permeability transition pore (PTP) formation.
- To clarify the role of matrix cyclophilin D in PTP regulation.
- To explore novel therapeutic strategies targeting PTP.
Main Methods:
- Gene inactivation studies of putative PTP components.
- Biochemical assays using novel PTP inhibitors as affinity labels.
Main Results:
- Cyclophilin D confirmed as the mitochondrial receptor for cyclosporin A's PTP-inhibiting effects.
- Involvement of adenine nucleotide translocators and voltage-dependent anion channel in PTP formation questioned.
- Novel inhibitors provide new tools for PTP research.
Conclusions:
- The molecular identity of the PTP remains controversial.
- Cyclophilin D plays a key role in PTP regulation.
- Novel inhibitors are crucial for future PTP molecular definition.
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