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- W1985499396 abstract "Purpose: Heart failure is a leading cause of morbidity and mortality worldwide. Disruption of Endoplasmic Reticulum (ER) homeostasis, a condition referred to as ER stress, has been implicated in many cardiovascular diseases including ischemic heart, heart failure, dilated cardiomyopathy, atherosclerosis and cardiotoxicity. In cardiomyocytes, ER stress is known to trigger autophagy, a dynamic process responsible for the degradation of cell components by the lysosomal pathway. However, it has become apparent that autophagy in the heart may have both adaptive and maladaptive consequences depending on the context. Besides, the NAD-dependent deacetylase SIRT1, the founding member of the sirtuins family, has been shown to be activated in response to different heart stresses to promote cell adaptation and survival. We thus hypothesised that SIRT1 might be involved in the regulation of ER stress-induced autophagy in the heart to provide a cardioprotective adaptation. Methods: H9c2 cells (rat cardiomyoblasts) were treated with the well known ER stress inducer tunicamycin (TN, 10 μg/mL), which impedes N-glycosylation and provokes the accumulation of misfolded proteins in the ER lumen. The level of ER stress (GRP78, GRP94) and autophagy (LC3-II) were assessed by western blot. Autophagy was also evaluated by flow cytometry using Cyto-ID® autophagy detection probe. The role of SIRT1 was studied by using EX527, a specific pharmacological inhibitor of this deacetylase and by RNA interference. For in vivo experiments, mice were injected intraperitoneally with 2 mg/kg TN once daily and heart tissues were analyzed 48h after injection." @default.
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- W1985499396 date "2014-06-27" @default.
- W1985499396 modified "2023-10-18" @default.
- W1985499396 title "P79Sirt1 modulates endoplasmic reticulum stress-induced autophagy in heart" @default.
- W1985499396 doi "https://doi.org/10.1093/cvr/cvu082.22" @default.
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