http://www.cnr.it/ontology/cnr/individuo/prodotto/ID4900
N-acetyl-l-cysteine fosters inactivation and transfer to endolysosomes of c-Src. (Articolo in rivista)
- Type
- 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
- 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)
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- Epub ahead of print (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
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- 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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