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• W2023793642 abstract "Oxidative stress promotes cardiac myocyte death and has been implicated in the pathogenesis of many cardiovascular diseases. Bcl-2 family proteins are key regulators of the apoptotic response, while their functions can be regulated by post-transcriptional modifications including phosphorylation, dimerization or proteolytic cleavage. This study used adult cardiac myocytes to test the hypothesis that activation of specific kinase signalling pathways by oxidative stress may modulate either the expression or the phosphorylation of Bcl-2, with the resulting effect of a decrease or increase in its anti-apoptotic function. Stimulation of cardiac myocytes with 0.2 mM H2O2, which induces apoptosis, resulted in a marked down-regulation of Bcl-2 protein simultaneously with an increase in its phosphorylation. Inhibition of p38-MAPK resulted in attenuation of Bcl-2 phosphorylation, whereas inhibition of ERK1/2, JNKs or PI-3-K had no effect. These data suggest that activation of p38 MAPK by oxidative stress results in the phosphorylation and degradation of Bcl-2 and the inactivation of its anti-apoptotic activity." @default.
• W2023793642 created "2016-06-24" @default.
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• W2023793642 date "2009-01-01" @default.
• W2023793642 modified "2023-09-27" @default.
• W2023793642 title "Regulation of Bcl-2 phosphorylation in response to oxidative stress in cardiac myocytes" @default.
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• W2023793642 doi "https://doi.org/10.1080/10715760903071649" @default.
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