N-acetyl-l-cysteine fosters inactivation and transfer to endolysosomes of c-Src. (Articolo in rivista)

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Label
  • N-acetyl-l-cysteine fosters inactivation and transfer to endolysosomes of c-Src. (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.freeradbiomed.2008.09.012 (literal)
Alternative label
  • Ewa K. Krasnowska a; Eugenia Pittaluga a; Anna Maria Brunati b; Roberto Brunelli c; Graziella Costa a; Marco De Spirito d; Annalucia Serafino a; Fulvio Ursini b; Tiziana Parasassi a (2008)
    N-acetyl-l-cysteine fosters inactivation and transfer to endolysosomes of c-Src.
    in Free radical biology & medicine
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ewa K. Krasnowska a; Eugenia Pittaluga a; Anna Maria Brunati b; Roberto Brunelli c; Graziella Costa a; Marco De Spirito d; Annalucia Serafino a; Fulvio Ursini b; Tiziana Parasassi a (literal)
Pagina inizio
  • 1566 (literal)
Pagina fine
  • 1572 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 45 (literal)
Rivista
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  • Epub ahead of print (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 11 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • PubMe (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • a Istituto di Neurobiologia e Medicina Molecolare, CNR, Roma, Italy; b Dipartimento di Chimica Biologica, Università di Padova, Padova, Italy; c Dipartimento di Ostetricia e Ginecologia, Università Sapienza, Roma, Italy; d Istituto di Fisica, Facoltà di Medicina e Chirurgia, Università Cattolica del Sacro Cuore, Roma, Italy. (literal)
Titolo
  • N-acetyl-l-cysteine fosters inactivation and transfer to endolysosomes of c-Src. (literal)
Abstract
  • The non-receptor-protein tyrosine kinase c-Src is overexpressed and activated in a large number of human cancers, in which it is associated with tumor development and progression. Canonical regulation takes place by means of an alternative phosphorylation of tyrosine residues-Tyr419 for activation and Tyr530 for inactivation. An independent redox regulation mechanism, involving cysteine residues, has also been proposed, in which oxidation activates the enzyme. Here we present a kinetic analysis of the effect of N-acetyl-l-cysteine (NAC) on c-Src, demonstrating that reduction reverts the oxidation-driven activation. In cancer cells, we show that NAC treatment produces an increase in specifically labeled reduced thiols of c-Src cysteines, thus confirming a redox transition. In addition to a decrease in Tyr419 phosphorylation, this leads to a massive shift of c-Src from plasma membranes-where its active form is located-to endolysosomal compartments. With the objective of deciphering the complex issue of c-Src regulation and of devising new strategies to revert its activation in cancers, redox regulation thus emerges as a promising area for study. (literal)
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