A peptide containing residues 26-44 of tau protein impairs mithocondrial oxidative phosphorylation acting ... (Articolo in rivista)

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  • A peptide containing residues 26-44 of tau protein impairs mithocondrial oxidative phosphorylation acting ... (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.2008.07.004 (literal)
Alternative label
  • Atlante A a; Amadoro G b; Bobba A a; de Bari L a; Corsetti V b,c; Pappalardo G d; Marra E a; Calissano P b,c; Passarella Se (2008)
    A peptide containing residues 26-44 of tau protein impairs mithocondrial oxidative phosphorylation acting ...
    in Biochimica et biophysica acta. Bioenergetics
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Atlante A a; Amadoro G b; Bobba A a; de Bari L a; Corsetti V b,c; Pappalardo G d; Marra E a; Calissano P b,c; Passarella Se (literal)
Pagina inizio
  • 1289 (literal)
Pagina fine
  • 1300 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • Impact factor BBA-Bioenergetics Anno 2008 : 4.447 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 1777 (literal)
Rivista
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  • 10 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • a Institute of Biomembranes and Bioenergetics, CNR, Via G. Amendola 165/A, 70126 Bari, Italy b Institute of Neurobiology and Molecular Medicine, CNR, Via del Fosso di Fiorano 64-65, 00143 Rome, Italy c European Brain Research Institute (EBRI), Via del Fosso di Fiorano 64-65, 00143 Rome, Italy d Institute of Biostructures and Bioimaging, CNR, Viale A. Doria 6, 95125 Catania. Italye Department of Health Sciences, University of Molise, Via F. De Sanctis, 86100 Campobasso, Italy (literal)
Titolo
  • A peptide containing residues 26-44 of tau protein impairs mithocondrial oxidative phosphorylation acting ... (literal)
Abstract
  • Having confirmed that adenovirus-mediated overexpression of NH(2)-tau fragment lacking the first 25 aminoacids evokes a potent neurotoxic effect, sustained by protracted stimulation of NMDA receptors, in primary neuronal cultures we investigated whether and how chemically synthesized NH(2)-derived tau peptides, i.e. NH(2)-26-44 and NH(2)-1-25 fragments, affect mitochondrial function. We tested both fragments on each step of the processes leading to ATP synthesis via oxidative phosphorylation: i) electron flow via the respiratory chain from physiological substrates to oxygen with the activity of each individual complex of the respiratory chain investigated in some detail, ii) membrane potential generation arising from externally added succinate and iii) the activity of both the adenine nucleotide translocator and iv) ATP synthase. Oxidative phosphorylation is not affected by NH(2)-1-25 tau fragment, but dramatically impaired by NH(2)-26-44 tau fragment. Both cytochrome c oxidase and the adenine nucleotide translocator are targets of NH(2)-26-44 tau fragment, but adenine nucleotide translocator is the unique mitochondrial target responsible for impairment of oxidative phosphorylation by the NH(2)-26-44 tau fragment, which then exerts deleterious effects on cellular availability of ATP synthesized into mitochondria. (literal)
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