Sirtuin1 and autophagy protect cells from fluoride-induced cell stress
Identifieur interne : 000696 ( Ncbi/Checkpoint ); précédent : 000695; suivant : 000697Sirtuin1 and autophagy protect cells from fluoride-induced cell stress
Auteurs : Maiko Suzuki ; John D. BartlettSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2013.
Abstract
Sirtuin1 (SIRT1) is an (NAD+)-dependent deacetylase functioning in the regulation of metabolism, cell survival and organismal lifespan. Active SIRT1 regulates autophagy during cell stress, including calorie restriction, endoplasmic reticulum stress and oxidative stress. Previously, we reported that fluoride induces endoplasmic reticulum (ER) stress in ameloblasts responsible for enamel formation, suggesting that ER-stress plays a role in dental fluorosis. However, the molecular mechanism of how cells respond to fluoride-induced cell stress is unclear. Here, we demonstrate that fluoride activates SIRT1 and initiates autophagy to protect cells from fluoride exposure. Fluoride treatment of ameloblast-derived cells (LS8) significantly increased
Url:
DOI: 10.1016/j.bbadis.2013.11.023
PubMed: 24296261
PubMed Central: 3913072
Affiliations:
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<front><div type="abstract" xml:lang="en"><p id="P1">Sirtuin1 (SIRT1) is an (NAD<sup>+</sup>
)-dependent deacetylase functioning in the regulation of metabolism, cell survival and organismal lifespan. Active SIRT1 regulates autophagy during cell stress, including calorie restriction, endoplasmic reticulum stress and oxidative stress. Previously, we reported that fluoride induces endoplasmic reticulum (ER) stress in ameloblasts responsible for enamel formation, suggesting that ER-stress plays a role in dental fluorosis. However, the molecular mechanism of how cells respond to fluoride-induced cell stress is unclear. Here, we demonstrate that fluoride activates SIRT1 and initiates autophagy to protect cells from fluoride exposure. Fluoride treatment of ameloblast-derived cells (LS8) significantly increased <italic>Sirt1</italic>
expression and induced SIRT1 phosphorylation resulting in the augmentation of SIRT1 deacetylase activity. To demonstrate that fluoride exposure initiates autophagy, we characterized the expression of autophagy related genes (<italic>Atg</italic>
); <italic>Atg5, Atg7</italic>
and <italic>Atg8/LC3</italic>
and showed that both their transcript and protein levels were significantly increased following fluoride treatment. To confirm that SIRT1 plays a protective role in fluoride toxicity, we used resveratrol (RES) to augmented SIRT1 activity in fluoride treated LS8 cells. RES increased autophagy, inhibited apoptosis, and decreased fluoride cytotoxicity. Rats treated with fluoride (0, 50 and 100 ppm) in drinking water for 6 weeks had significantly elevated expression levels of <italic>Sirt1, Atg5, Atg7</italic>
and <italic>Atg8/LC3</italic>
in their maturation stage enamel organs. Increased protein levels of p-SIRT1, ATG5 and ATG8/LC3 were present in fluoride-treated rat maturation stage ameloblasts. Therefore, the SIRT1/autophagy pathway may play a critical role as a protective response to help prevent dental fluorosis.</p>
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<tree><noCountry><name sortKey="Bartlett, John D" sort="Bartlett, John D" uniqKey="Bartlett J" first="John D." last="Bartlett">John D. Bartlett</name>
<name sortKey="Suzuki, Maiko" sort="Suzuki, Maiko" uniqKey="Suzuki M" first="Maiko" last="Suzuki">Maiko Suzuki</name>
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