http://www.cnr.it/ontology/cnr/individuo/prodotto/ID21016
Tyrosine phosphorylation of insulin receptor substrates during ischemia/reperfusion-induced apoptosis in rat liver. (Articolo in rivista)
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- Label
- Tyrosine phosphorylation of insulin receptor substrates during ischemia/reperfusion-induced apoptosis in rat liver. (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
- Alternative label
Cursio R, Miele C, Filippa N, Colosetti P, Auberger P, Van Obberghen E, Gugenheim J. (2008)
Tyrosine phosphorylation of insulin receptor substrates during ischemia/reperfusion-induced apoptosis in rat liver.
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Cursio R, Miele C, Filippa N, Colosetti P, Auberger P, Van Obberghen E, Gugenheim J. (literal)
- Note
- ISI Web of Science (WOS) (literal)
- Titolo
- Tyrosine phosphorylation of insulin receptor substrates during ischemia/reperfusion-induced apoptosis in rat liver. (literal)
- Abstract
- Phosphoregulation of signal transduction pathways is a complex series of reactions that may modulate the cellular response to ischemia-reperfusion (I-R). The aim of this study was to evaluate the effect of normothermic liver I/R-induced apoptosis on phosphorylation and activation of signal proteins in tyrosine kinase pathways. MATERIALS AND METHODS: In rats, a segmental normothermic ischemia of the liver was induced for 120 min. Liver apoptosis was determined using terminal deoxynucleotide-transferase-mediated deoxyuridine triphosphate nick end labeling assay, and activity of caspases-3 and -7 was determined by fluorescence. Liver tyrosine phosphorylation of proteins was examined by Western blot analysis. RESULTS: Normothermic I-R resulted in increased in vivo caspases-3 and -7 activity and in liver apoptosis. Shc tyrosine phosphorylation and activation of ERK1/2 were increased after reperfusion, while tyrosine phosphorylation of IRS-1 and activation of PKB/Akt were decreased. CONCLUSIONS: Normothermic liver I-R leads to increased apoptosis and to modifications in protein tyrosine phosphorylation pathways.
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