Abstract
The mitochondrial membrane permeability transition induced byCa2+ is inhibited by quinine in a dose-dependent fashion.Competition experiments strongly suggest that quinine displacesCa2+ bound to the inner membrane. This is supported byexperiments showing that quinine inhibits Ca2+-dependent butnot Ca2+-independent mitochondrial swelling induced byphenylarsine oxide. As with Ca2+ chelators, quinine inducespermeability transition pore closure preventing the contraction induced bypoly(ethylene glycol) 2000 in mitochondria preswollen by incubation in KSCNmedium containing Ca2+ and inorganic phosphate. These resultssuggest that quinine dislodges Ca2+ bound to the protein site,which triggers pore opening.
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Catisti, R., Vercesi, A.E. Permeability Transition Pore Closure Promoted by Quinine. J Bioenerg Biomembr 31, 153–157 (1999). https://doi.org/10.1023/A:1005455912711
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DOI: https://doi.org/10.1023/A:1005455912711