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The Mitochondrial Permeability Transition and the Connection between F1Fo-ATPase and Calcium


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1 Department of Veterinary Medical Sciences, University of Bologna, via Tolara di Sopra 50, 40064 Ozzano Emilia (BO), Italy
 

Recently, He et al. asserted that their new data ‘definitively’ disprove the cring of the mitochondrial F1F0-ATPase as molecular identity of the permeability transition pore (PTP). The authors’ conclusion is also confirmed by the results of the calculated ionic conductance of cring lumen, which would be incompatible with the PTP channel properties. However, in my opinion, the role of calcium- activated F1F0-ATPase as an alternative functioning mode of the F1F0 complex should also be considered in events that trigger the PTP opening.
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  • The Mitochondrial Permeability Transition and the Connection between F1Fo-ATPase and Calcium

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Authors

Salvatore Nesci
Department of Veterinary Medical Sciences, University of Bologna, via Tolara di Sopra 50, 40064 Ozzano Emilia (BO), Italy

Abstract


Recently, He et al. asserted that their new data ‘definitively’ disprove the cring of the mitochondrial F1F0-ATPase as molecular identity of the permeability transition pore (PTP). The authors’ conclusion is also confirmed by the results of the calculated ionic conductance of cring lumen, which would be incompatible with the PTP channel properties. However, in my opinion, the role of calcium- activated F1F0-ATPase as an alternative functioning mode of the F1F0 complex should also be considered in events that trigger the PTP opening.

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DOI: https://doi.org/10.18520/cs%2Fv113%2Fi10%2F1820-1821