http://www.cnr.it/ontology/cnr/individuo/prodotto/ID38451
A maxi chloride channel in the inner membrane of mammalian mitochondria. (Articolo in rivista)
- Type
- Label
- A maxi chloride channel in the inner membrane of mammalian mitochondria. (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bbabio.2008.08.007 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- De Marchi U.; Szabò I.; Cereghetti G.M.; Hoxha P.; Craigen W.J.; Zoratti M. (literal)
- Pagina inizio
- Pagina fine
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- http://www.sciencedirect.com/science/article/pii/S0005272808006592 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- PubMe (literal)
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- CNR Institute of Neuroscience, Department of Biomedical Sciences, University of Padova, Padova, Italy /
Department of Biology, University of Padova, Padova, Italy /
Venetian Institute of Molecular Medicine, Padova, Italy /
Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, USA (literal)
- Titolo
- A maxi chloride channel in the inner membrane of mammalian mitochondria. (literal)
- Abstract
- Patch-clamp experiments on swollen mitochondria of human, mouse and rat origins have revealed activity
by an approximately 400 pS (in 150 mM KCl), voltage-dependent and anion-selective channel. This channel is
located in the inner membrane, as shown by experiments with mitochondria from cells expressing a
fluorescent mitochondrial tag protein and by the co-presence of the 107 pS channel and of the permeability
transition pore (PTP). The frequency of appearance was inversely related to the presence of the PTP. This and
the comparison of its electrophysiological characteristics with those of the PTP indicate that it is closely
related to the latter, possibly corresponding to a monomeric unit whose dimer constitutes the full PTP. The
channel is similar but not identical to isolated-and-reconstituted mitochondrial porin, and it is present also
in mitochondria from cells lacking porin isoforms. Its identification with porin is therefore to be excluded. It
most likely coincides instead with the \"maxi-chloride channel\" characterized in the plasma membrane of
various cell types. (literal)
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