Modulation of mitochondrial K+ permeability and reactive oxygen species production by the p13 protein of human T-cell leukemia virus type 1. (Articolo in rivista)

Type
Label
  • Modulation of mitochondrial K+ permeability and reactive oxygen species production by the p13 protein of human T-cell leukemia virus type 1. (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bbabio.2009.02.001 (literal)
Alternative label
  • Silic-Benussi M.; Cannizzaro E.; Venerando A.; Cavallari I.; Petronilli V.; La Rocca N.; Marin O.; Chieco-Bianchi L.; Di Lisa F.; D'Agostino D.M.; Bernardi P.; Ciminale V. (2009)
    Modulation of mitochondrial K+ permeability and reactive oxygen species production by the p13 protein of human T-cell leukemia virus type 1.
    in Biochimica et biophysica acta. Bioenergetics
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Silic-Benussi M.; Cannizzaro E.; Venerando A.; Cavallari I.; Petronilli V.; La Rocca N.; Marin O.; Chieco-Bianchi L.; Di Lisa F.; D'Agostino D.M.; Bernardi P.; Ciminale V. (literal)
Pagina inizio
  • 947 (literal)
Pagina fine
  • 954 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 1787 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Oncology and Surgical Sciences, University of Padova, Italy; Venetian Institute of Molecular Medicine (VIMM), Padova, Italy; CNR Institute of Neuroscience and Department of Biomedical Sciences, University of Padova, Italy; Department of Biology, University of Padova, Italy; Department of Biological Chemistry, University of Padova, Italy; Istituto Oncologico Veneto-IRRCS, Padova, Italy (literal)
Titolo
  • Modulation of mitochondrial K+ permeability and reactive oxygen species production by the p13 protein of human T-cell leukemia virus type 1. (literal)
Abstract
  • Human T-cell leukemia virus type-1 (HTLV-1) expresses an 87-amino acid protein named p13 that is targeted to the inner mitochondrial membrane. Previous studies showed that a synthetic peptide spanning an alpha helical domain of p13 alters mitochondrial membrane permeability to cations, resulting in swelling. The present study examined the effects of full-length p13 on isolated, energized mitochondria. Results demonstrated that p13 triggers an inward K+ current that leads to mitochondrial swelling and confers a crescent-like morphology distinct from that caused by opening of the permeability transition pore. p13 also induces depolarization, with a matching increase in respiratory chain activity, and augments production of reactive oxygen species (ROS). These effects require an intact alpha helical domain and strictly depend on the presence of K+ in the assay medium. The effects of p13 on ROS are mimicked by the K+ ionophore valinomycin, while the protonophore FCCP decreases ROS, indicating that depolarization induced by K+ vs. H (+) currents has different effects on mitochondrial ROS production, possibly because of their opposite effects on matrix pH (alkalinization and acidification, respectively). The downstream consequences of p13-induced mitochondrial K+ permeability are likely to have an important influence on the redox state and turnover of HTLV-1-infected cells. (literal)
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