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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Sirtuin1 and autophagy protect cells from fluoride-induced cell stress</title><author><name sortKey="Suzuki, Maiko" sort="Suzuki, Maiko" uniqKey="Suzuki M" first="Maiko" last="Suzuki">Maiko Suzuki</name></author><author><name sortKey="Bartlett, John D" sort="Bartlett, John D" uniqKey="Bartlett J" first="John D." last="Bartlett">John D. Bartlett</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">24296261</idno><idno type="pmc">3913072</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3913072</idno><idno type="RBID">PMC:3913072</idno><idno type="doi">10.1016/j.bbadis.2013.11.023</idno><date when="2013">2013</date><idno type="wicri:Area/Pmc/Corpus">000380</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000380</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Sirtuin1 and autophagy protect cells from fluoride-induced cell stress</title><author><name sortKey="Suzuki, Maiko" sort="Suzuki, Maiko" uniqKey="Suzuki M" first="Maiko" last="Suzuki">Maiko Suzuki</name></author><author><name sortKey="Bartlett, John D" sort="Bartlett, John D" uniqKey="Bartlett J" first="John D." last="Bartlett">John D. Bartlett</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><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></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">0217513</journal-id><journal-id journal-id-type="pubmed-jr-id">1037</journal-id><journal-id journal-id-type="nlm-ta">Biochim Biophys Acta</journal-id><journal-id journal-id-type="iso-abbrev">Biochim. Biophys. Acta</journal-id><journal-title-group><journal-title>Biochimica et biophysica acta</journal-title></journal-title-group><issn pub-type="ppub">0006-3002</issn></journal-meta><article-meta><article-id pub-id-type="pmid">24296261</article-id><article-id pub-id-type="pmc">3913072</article-id><article-id pub-id-type="doi">10.1016/j.bbadis.2013.11.023</article-id><article-id pub-id-type="manuscript">NIHMS549499</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Sirtuin1 and autophagy protect cells from fluoride-induced cell stress</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Suzuki</surname><given-names>Maiko</given-names></name></contrib><contrib contrib-type="author"><name><surname>Bartlett</surname><given-names>John D.</given-names></name><xref ref-type="corresp" rid="cor1">*</xref></contrib><aff id="A1">Department of Mineralized Tissue Biology and Harvard School of Dental Medicine, The Forsyth Institute, 245 First Street, Cambridge, MA, 02142, USA</aff></contrib-group><author-notes><corresp id="cor1"><label>*</label>Corresponding author at: Department of Mineralized Tissue Biology, The Forsyth Institute, 245 First Street, Cambridge, MA 02142, USA, Tel.: +1-(617) 892-8388; Fax: +1-(617) 892-8510 <email>jbartlett@forsyth.org</email> (J.D. Bartlett)</corresp></author-notes><pub-date pub-type="nihms-submitted"><day>27</day><month>1</month><year>2014</year></pub-date><pub-date pub-type="epub"><day>01</day><month>12</month><year>2013</year></pub-date><pub-date pub-type="ppub"><month>2</month><year>2014</year></pub-date><pub-date pub-type="pmc-release"><day>01</day><month>2</month><year>2015</year></pub-date><volume>1842</volume><issue>2</issue><fpage>245</fpage><lpage>255</lpage><pmc-comment>elocation-id from pubmed: 10.1016/j.bbadis.2013.11.023</pmc-comment>
<permissions><copyright-statement>© 2013 Elsevier B.V. All rights reserved.</copyright-statement><copyright-year>2013</copyright-year></permissions><abstract><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></abstract><kwd-group><kwd>Sirt1</kwd><kwd>autophagy</kwd><kwd>fluoride</kwd><kwd>enamel</kwd><kwd>ameloblast</kwd><kwd>dental fluorosis</kwd></kwd-group><funding-group><award-group><funding-source country="United States">National Institute of Dental and Craniofacial Research : NIDCR</funding-source><award-id>R01 DE018106 || DE</award-id></award-group></funding-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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