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Title:
Modulation of the mitochondrial megachannel by divalent cations and protons - PubMed
Description:
In patch-clamp experiments on rat liver mitoplasts, the 1.3 nanosiemens (in 150 mM KCl) mitochondrial megachannel was activated by Ca2+ and competitively inhibited by Mg2+, Mn2+, Ba2+, and Sr2+. Cyclosporin A, which inhibits the megachannel, also showed a competitive behavior versus Ca2+. The pore i …
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Keywords {🔍}
mitochondrial, pmid, doi, megachannel, pore, permeability, transition, zoratti, pharmacology, divalent, cations, bernardi, effects, similar, articles, cited, mesh, biol, chem, szabó, free, article, liver, mitochondria, channel, pmc, main, content, ncbi, abstract, related, resources, feb, modulation, support, pubmed, bioenerg, apr, jun, epub, drug, ion, channels, hhs, page, homepage, navigation, search, full, text,
Topics {✒️}
main page content similar articles cited calcium-induced permeability transition calcium-dependent potassium channel literature sources pore open-closed probability yeast f-atp synthase zajdela hepatoma mitochondria divalent cations mesh keyword permeability transition pore mitochondrial permeability transition effects 7682848 effects resources proteins related rat liver mitoplasts united states government patch-clamp experiments adenine nucleotide translocators biochem soc trans mol cell biochem books pubchem compound similar manner reversible histidine protonation cited 1380498 ca2+-reversible inhibition lower ph values modulating sites involved mitochondria abstract rat liver atp synthase results support pore believed channel formation mitochondrial dysfunction content pubmed wordmark pubmed logo mitochondrial megachannel hhs reversible manner bioenerg biomembr ca2+ threshold linkout official website 150 mm kcl competitively inhibited cyclosporin
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- The mitochondrial permeability transition pore: Is it formed by the ATP synthase, adenine nucleotide translocators or both?
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