We are analyzing https://link.springer.com/article/10.1007/s10863-005-6565-9.

Title:
Genetic Dissection of the Permeability Transition Pore | Journal of Bioenergetics and Biomembranes
Description:
The permeability transition pore (PTP) regulates the structural re-organization of mitochondria in response to changes in cellular Ca2+ and is thought to be an important participant in mitochondrial responses to cell death signals. Although the proteins forming the PTP have yet to be rigorously identified, recent examination of the response of mitochondria, cells and tissues lacking putative components of the PTP have been reported. Studies on mitochondria lacking cyclophilin D (CyP-D) have proved that this protein is the target for PTP inhibition by CsA; yet they have also unequivocally demonstrated that the PTP can form and open in the absence of CyP-D. Likewise, studies in mice lacking the two adenine nucleotide translocators expressed in this species have shown that a functional PTP can form in the absence of these proteins. Thus, the inner mitochondrial membrane components of the PTP remain to be identified, and the absence of CyP-D may not preclude PTP opening in vivo – a finding that questions the conclusion that the PTP participates in cell death pathways only in response to a restricted set of challenges.
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Keywords {🔍}

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Topics {✒️}

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Schema {🗺️}

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         headline:Genetic Dissection of the Permeability Transition Pore
         description:The permeability transition pore (PTP) regulates the structural re-organization of mitochondria in response to changes in cellular Ca2+ and is thought to be an important participant in mitochondrial responses to cell death signals. Although the proteins forming the PTP have yet to be rigorously identified, recent examination of the response of mitochondria, cells and tissues lacking putative components of the PTP have been reported. Studies on mitochondria lacking cyclophilin D (CyP-D) have proved that this protein is the target for PTP inhibition by CsA; yet they have also unequivocally demonstrated that the PTP can form and open in the absence of CyP-D. Likewise, studies in mice lacking the two adenine nucleotide translocators expressed in this species have shown that a functional PTP can form in the absence of these proteins. Thus, the inner mitochondrial membrane components of the PTP remain to be identified, and the absence of CyP-D may not preclude PTP opening in vivo – a finding that questions the conclusion that the PTP participates in cell death pathways only in response to a restricted set of challenges.
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         dateModified:
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            cyclophilin D
            adenine nucleotide translocator
            cell death
            apoptosis
            necrosis
            “knock-out” mice
            calcium
            Bioorganic Chemistry
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            general
            Animal Anatomy / Morphology / Histology
            Animal Biochemistry
            Organic Chemistry
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      headline:Genetic Dissection of the Permeability Transition Pore
      description:The permeability transition pore (PTP) regulates the structural re-organization of mitochondria in response to changes in cellular Ca2+ and is thought to be an important participant in mitochondrial responses to cell death signals. Although the proteins forming the PTP have yet to be rigorously identified, recent examination of the response of mitochondria, cells and tissues lacking putative components of the PTP have been reported. Studies on mitochondria lacking cyclophilin D (CyP-D) have proved that this protein is the target for PTP inhibition by CsA; yet they have also unequivocally demonstrated that the PTP can form and open in the absence of CyP-D. Likewise, studies in mice lacking the two adenine nucleotide translocators expressed in this species have shown that a functional PTP can form in the absence of these proteins. Thus, the inner mitochondrial membrane components of the PTP remain to be identified, and the absence of CyP-D may not preclude PTP opening in vivo – a finding that questions the conclusion that the PTP participates in cell death pathways only in response to a restricted set of challenges.
      datePublished:
      dateModified:
      pageStart:121
      pageEnd:128
      sameAs:https://doi.org/10.1007/s10863-005-6565-9
      keywords:
         Permeability transition pore
         cyclophilin D
         adenine nucleotide translocator
         cell death
         apoptosis
         necrosis
         “knock-out” mice
         calcium
         Bioorganic Chemistry
         Biochemistry
         general
         Animal Anatomy / Morphology / Histology
         Animal Biochemistry
         Organic Chemistry
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