We are analyzing https://link.springer.com/article/10.1007/bf00762735.

Title:
Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane | Journal of Bioenergetics and Biomembranes
Description:
The mitochondrial permeability transition pore allows solutes with a m.w. ≲1500 to equilibrate across the inner membrane. A closed pore is favored by cyclosporin A acting at a high-affinity site, which may be the matrix space cylophilin isozyme. Early results obtained with cyclosporin A analogs and metabolites support this hypothesis. Inhibition by cyclosporin does not appear to require inhibition of calcineurin activity; however, it may relate to inhibition of cyclophilin peptide bond isomerase activity. The permeability transition pore is strongly regulated by both the membrane potential (Δψ) and ΔpH components of the mitochondrial protonmotive force. A voltage sensor which is influenced by the disulfide/sulhydryl state of vicinal sulfhydryls is proposed to render pore opening sensitive to Δψ. Early results indicate that this sensor is also responsive to membrane surface potential and/or to surface potential gradients. Histidine residues located on the matrix side of the inner membrane render the pore responsive to ΔpH. The pore is also regulated by several ions and metabolites which act at sites that are interactive. There are many analogies between the systems which regulate the permeability transition pore and the NMDA receptor channel. These suggest structural similarities and that the permeability transition pore belongs to the family of ligand gated ion channels.
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Topics {✒️}

membrane surface potential month download article/chapter surface potential gradients mitochondrial ion transport membrane potential mitochondrial membrane published permeability transition pore mitochondrial permeability transition related subjects cyclosporin-sensitive pore privacy choices/manage cookies full article pdf mitochondrial membrane mitochondrial protonmotive force disulfide/sulhydryl state membrane render european economic area histidine residues located nmda receptor channel suggest structural similarities conditions privacy policy check access instant access ohio state university accepting optional cookies high-affinity site early results obtained journal finder publish main content log article journal closed pore membrane article bernardi article log pore responsive privacy policy personal data recent progress essential cookies article cite analogs calcineurin activity books a optional cookies manage preferences biomembranes aims metabolites support early results matrix side journal publish

Schema {🗺️}

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         description:The mitochondrial permeability transition pore allows solutes with a m.w. ≲1500 to equilibrate across the inner membrane. A closed pore is favored by cyclosporin A acting at a high-affinity site, which may be the matrix space cylophilin isozyme. Early results obtained with cyclosporin A analogs and metabolites support this hypothesis. Inhibition by cyclosporin does not appear to require inhibition of calcineurin activity; however, it may relate to inhibition of cyclophilin peptide bond isomerase activity. The permeability transition pore is strongly regulated by both the membrane potential (Δψ) and ΔpH components of the mitochondrial protonmotive force. A voltage sensor which is influenced by the disulfide/sulhydryl state of vicinal sulfhydryls is proposed to render pore opening sensitive to Δψ. Early results indicate that this sensor is also responsive to membrane surface potential and/or to surface potential gradients. Histidine residues located on the matrix side of the inner membrane render the pore responsive to ΔpH. The pore is also regulated by several ions and metabolites which act at sites that are interactive. There are many analogies between the systems which regulate the permeability transition pore and the NMDA receptor channel. These suggest structural similarities and that the permeability transition pore belongs to the family of ligand gated ion channels.
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            cyclosporin analogs
            transmembrane potential
            membrane surface potential
            lipid mediators
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      headline:Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane
      description:The mitochondrial permeability transition pore allows solutes with a m.w. ≲1500 to equilibrate across the inner membrane. A closed pore is favored by cyclosporin A acting at a high-affinity site, which may be the matrix space cylophilin isozyme. Early results obtained with cyclosporin A analogs and metabolites support this hypothesis. Inhibition by cyclosporin does not appear to require inhibition of calcineurin activity; however, it may relate to inhibition of cyclophilin peptide bond isomerase activity. The permeability transition pore is strongly regulated by both the membrane potential (Δψ) and ΔpH components of the mitochondrial protonmotive force. A voltage sensor which is influenced by the disulfide/sulhydryl state of vicinal sulfhydryls is proposed to render pore opening sensitive to Δψ. Early results indicate that this sensor is also responsive to membrane surface potential and/or to surface potential gradients. Histidine residues located on the matrix side of the inner membrane render the pore responsive to ΔpH. The pore is also regulated by several ions and metabolites which act at sites that are interactive. There are many analogies between the systems which regulate the permeability transition pore and the NMDA receptor channel. These suggest structural similarities and that the permeability transition pore belongs to the family of ligand gated ion channels.
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      dateModified:
      pageStart:509
      pageEnd:517
      sameAs:https://doi.org/10.1007/BF00762735
      keywords:
         Mitochondrial permeability transition
         cyclosporin A
         cyclosporin analogs
         transmembrane potential
         membrane surface potential
         lipid mediators
         Bioorganic Chemistry
         Biochemistry
         general
         Animal Anatomy / Morphology / Histology
         Animal Biochemistry
         Organic Chemistry
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                     name:From the Department of Medical Biochemistry, The Ohio State University, Columbus
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