http://www.cnr.it/ontology/cnr/individuo/prodotto/ID170514
Assessing the molecular basis for rat-selective induction of the mitochondrial permeability transition by norbormide (Articolo in rivista)
- Type
- Label
- Assessing the molecular basis for rat-selective induction of the mitochondrial permeability transition by norbormide (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bbabio.2007.04.002 (literal)
- Alternative label
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- Zulian A; Petronilli V; Bova S; Dabbeni-Sala F; Cargnelli G; Cavalli M; Rennison D; Stäb J; Laita O; Lee DJ; Brimble MA; Hopkins B; Bernardi P; Ricchelli F (literal)
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- ISI Web of Science (WOS) (literal)
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- Rennison D, Brimble MA, Stab J, Laita O, Lee DJ, University of Auckland, Auckland, New Zealand; Bova S, Cavalli M, Zulian A, Dabbeni-Sala F, Cargnelli G, Bernardi P, University of Padova; Hopkins B, Landcare Research, Lincoln, New Zealand; Ricchelli F, Petronilli V, CNR (literal)
- Titolo
- Assessing the molecular basis for rat-selective induction of the mitochondrial permeability transition by norbormide (literal)
- Abstract
- It was recently demonstrated that the rat-selective toxicant norbormide also induces rat-selective opening of the permeability transition pore (PTP) in isolated mitochondria. Norbormide is a mixture of endo and exo stereoisomers; however, only the endo forms are lethal to rats. In the present study we tested both endo and exo isomers as well as neutral and cationic derivatives of norbormide to: (i) verify if the PTP-regulatory activity by norbormide is stereospecific; (ii) define the structural features of norbormide responsible for PTP-activation, (iii) elucidate the basis for the drug species-specificity. Our results show that: (i) norbormide isomers affect PTP in a rat-selective fashion; however, no relevant differences between lethal and non-lethal forms are observed suggesting that drug regulation of PTP-activity and lethality in rats are unrelated phenomena; (ii) a (phenylvinyl)pyridine moiety represents the key element conferring the PTP-activating effect; (iii) cationic derivatives of rat-active compounds
accumulate in the matrix via the membrane potential and activate the PTP also in mouse and guinea pig mitochondria. These findings suggest that the norbormide-sensitive PTP-target is present in all species examined, and is presumably located on the matrix side. The species-selectivity may depend on the unique properties of a transport system allowing drug internalisation in rat mitochondria. (literal)
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