2012
DOI: 10.18632/aging.100470
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Abstract: Muscle contraction is associated with the production of reactive oxygen species (ROS). Mechanisms of ROS scavenging are fundamental to avoid muscle damage. We had previously discovered a stretch-induced genetic program in myotubes that triggers an antioxidant defense. At the core of this mechanism, transcriptional activation of SIRT1 by the early growth response protein EGR1 results in increased MnSOD activity through the activation of Sod2 by SIRT1/FOXO pathway. In this report, we show experimental evidence t… Show more

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Cited by 16 publications
(18 citation statements)
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References 20 publications
(25 reference statements)
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“…2A and B). Since SIRT1 activity was identified as a contributing element for NFAT5 dependent AR expression, it was inferred that the fluctuation observed in SIRT1 expression during the time course may be explained by the paradigm that SIRT1 activity negatively regulates its own expression [21,24,85,86]. In line with this paradigm, pharmacological activator of SIRT1, resveratrol and PARP1 inhibitor, 3-aminobenzamide decreased SIRT1 expression in U937 cells under osmotic stress, whereas SIRT1 inhibitor, Ex-527 increased it (Fig.…”
Section: Discussionmentioning
confidence: 73%
See 1 more Smart Citation
“…2A and B). Since SIRT1 activity was identified as a contributing element for NFAT5 dependent AR expression, it was inferred that the fluctuation observed in SIRT1 expression during the time course may be explained by the paradigm that SIRT1 activity negatively regulates its own expression [21,24,85,86]. In line with this paradigm, pharmacological activator of SIRT1, resveratrol and PARP1 inhibitor, 3-aminobenzamide decreased SIRT1 expression in U937 cells under osmotic stress, whereas SIRT1 inhibitor, Ex-527 increased it (Fig.…”
Section: Discussionmentioning
confidence: 73%
“…SIRT1 is a NAD + dependent histone/protein deacetylase which has been implicated in a wide array of cellular events including starvation, inflammation, oxidative stress and senescence [21]. SIRT1 mediates these cellular events in part through directly deacetylating several transcription factors such as p53 [22], FOXOs [23], Egr-1 [24], p65 [25], and NFATc3 [26]. Among these transcription factors, Rel family members p65 and NFATc3 were identified to be negatively regulated by direct SIRT1 dependent deacetylation [25,26].…”
Section: Introductionmentioning
confidence: 99%
“…Normally, extracellular hormones work through receptors to stimulate adenylate cyclase 1(AC) to convert ATP into cAMP, which in turn stimulates EPAC 1. Higher EPAC activity indirectly leads to activation of AMPactivated protein kinase (AMPK), a key regulator of cellular energy utilization [51][52][53][54][55][56] report that resveratrol inhibited the phosphodiesterase (PDE-4) in vitro and stimulated EPAC activity and AMPK phosphorylation in cell culture. In a mouse model of diet-induced obesity, the generic PDE-4 inhibitor increased AMPK activity and Sirt1 activation [56].…”
Section: Discussionmentioning
confidence: 99%
“…Stress such as quinolinic acid suppress Sirt1 function and prevent the deacetylation, leading to mitochondrial dysfunction. In addition, Sirt1 leads to the FOXO-dependent activation of the SOD2 gene and the consequently increased MnSOD activity promotes ROS scavenging, which improves mitochondrial activity and prevents neurodegeneration [51][52][53][54][55][56][57].…”
Section: Discussionmentioning
confidence: 99%
“…In some cases, the SIRT1 protein regulates the function of the interacting partner (such as EGR1 94 and AP1 95 ), while in other cases, the interacting partner regulates SIRT1 activity (e.g., DBC1 96,97 and AROS 98 ). A recent meta-analysis puts SIRT1 into an exclusive class of highly Note: Those proteins labeled in bold are normally cytoplasmic, while those not in bold are at least partially nuclear.…”
Section: Sirt1 Is a Protein Network Hubmentioning
confidence: 99%