[No authors listed]
Oxidative stress serves important roles in cardiac injury during the process of ischemia/reperfusion (I/R). Yâbox protein 1 (YB1), a member of the highly conserved Yâbox protein family, is closely associated with inflammation and stress responses by regulating gene transcription, RNA splicing and mRNA translation. However, the roles of YB1 in oxidative stressâinduced myocardialâI/R (MâI/R) injury are unknown. The aim of the present study was to examine the effects of YB1 on H2O2âinduced cardiomyocyte injury and its underlying mechanism. The results demonstrated that YB1 expression was upregulated during H2O2âinduced myocardial injury. YB1 knockdown through transfection of small interfering RNA significantly aggravated cardiac cell apoptosis. Furthermore, YB1 knockdown significantly reversed the H2O2âmediated increase in phosphorylated signal transducer and activator of transcription but did not affect the phosphorylation of P38, extracellular signalâregulated kinases 1/2, câJun Nâterminal kinases, P65, Janus kinase 1 and 2 or Moreover, protein coâimmunoprecipitation and RNAâbinding protein immunoprecipitation assays revealed that YB1 interacted with protein inhibitor of activated 3 (PIAS3) mRNA but not its translated protein. YB1 overexpression may have promoted PIAS3 mRNA decay, decreasing PIAS3 protein levels, and therefore increased the levels of phosphorylated Finally, YB1 knockdown, mediated by a lentivirus carrying YB1 targeted short hairpin RNA, significantly decreased left ventricle percentage fractional shortening and ejection fraction values, while increasing the infarct sizes in a rat model of MâI/R injury. These results demonstrated for the first time (to the best of our knowledge) that YB1 may protect cardiac myocytes against H2O2 or MâI/Râinduced injury by binding to PIAS3 mRNA and resulting in the phosphorylation of
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