Mechanisms for Ca <sup>2+</sup> -dependent permeability transition in mitochondria
Paolo Bernardi
Abstract
In a recent study in cells lacking an assembled F-ATP synthase the conclusion was reached that this enzyme cannot form the mitochondrial permeability transition pore (PTP) (1). As in previous studies (2, 3) the key argument is that mitochondria still undergo cyclosporin A (CsA)-sensitive swelling and Ca2+-induced Ca2+release (1⇓–3). The PTP (or mitochondrial megachannel, MMC) is an inner membrane channel activated by matrix Ca2+ and inhibited by CsA through cyclophilin (CyP) D, a matrix peptidyl-prolyl cis–trans isomerase. The PTP can reach conductances up to 1.2 to 1.5 nS but is rich in smaller subconductance states (4). Based on the … [↵][1]1Email: bernardi{at}bio.unipd.it. [1]: #xref-corresp-1-1
Topics & Concepts
CyclophilinMitochondrionMitochondrial permeability transition poreMitochondrial matrixInner mitochondrial membraneIsomeraseATP synthaseChemistryBiophysicsPermeability (electromagnetism)Inner membraneEnzymeMembraneStereochemistryBiochemistryBiologyCytosolGeneProgrammed cell deathApoptosisMitochondrial Function and PathologyATP Synthase and ATPases ResearchSignaling Pathways in Disease