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                <title level="j">Cells</title>
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                  <biblScope unit="issue">2</biblScope>
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                  <date type="datePub">2020</date>
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                <term xml:lang="en">cardioprotection</term>
                <term xml:lang="en">cell death</term>
                <term xml:lang="en">autophagy/mitophagy</term>
                <term xml:lang="en">endoplasmic reticulum stress</term>
                <term xml:lang="en">Sirtuin 1</term>
              </keywords>
              <classCode scheme="mesh">Animals</classCode>
              <classCode scheme="mesh">Autophagy</classCode>
              <classCode scheme="mesh">Myocytes, Cardiac</classCode>
              <classCode scheme="mesh">RNA Interference</classCode>
              <classCode scheme="mesh">RNA, Small Interfering</classCode>
              <classCode scheme="mesh">Rats</classCode>
              <classCode scheme="mesh">Sequestosome-1 Protein</classCode>
              <classCode scheme="mesh">Signal Transduction</classCode>
              <classCode scheme="mesh">Sirtuin 1</classCode>
              <classCode scheme="mesh">Tunicamycin</classCode>
              <classCode scheme="mesh">Elongation Factor 2 Kinase</classCode>
              <classCode scheme="mesh">Endoplasmic Reticulum Stress</classCode>
              <classCode scheme="mesh">Heat-Shock Proteins</classCode>
              <classCode scheme="mesh">Isoproterenol</classCode>
              <classCode scheme="mesh">Mice</classCode>
              <classCode scheme="mesh">Mice, Inbred C57BL</classCode>
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              <p>Many recent studies have demonstrated the involvement of endoplasmic reticulum (ER) stress in the development of cardiac diseases and have suggested that modulation of ER stress response could be cardioprotective. Previously, we demonstrated that the deacetylase Sirtuin 1 (SIRT1) attenuates ER stress response and promotes cardiomyocyte survival. Here, we investigated whether and how autophagy plays a role in SIRT1-afforded cardioprotection against ER stress. The results revealed that protective autophagy was initiated before cell death in response to tunicamycin (TN)-induced ER stress in cardiac cells. SIRT1 inhibition decreased ER stress-induced autophagy, whereas its activation enhanced autophagy. In response to TN- or isoproterenol-induced ER stress, mice deficient for SIRT1 exhibited suppressed autophagy along with exacerbated cardiac dysfunction. At the molecular level, we found that in response to ER stress (i) the extinction of eEF2 or its kinase eEF2K not only reduced autophagy but further activated cell death, (ii) inhibition of SIRT1 inhibited the phosphorylation of eEF2, (iii) eIF2?? co-immunoprecipitated with eEF2K, and (iv) knockdown of eIF2?? reduced the phosphorylation of eEF2. Our results indicate that in response to ER stress, SIRT1 activation promotes cardiomyocyte survival by enhancing autophagy at least through activation of the eEF2K/eEF2 pathway.</p>
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