HERPUD1 protects against oxidative stress-induced apoptosis through downregulation of the inositol 1,4,5-trisphosphate receptor
Identifieur interne : 000205 ( Pmc/Checkpoint ); précédent : 000204; suivant : 000206HERPUD1 protects against oxidative stress-induced apoptosis through downregulation of the inositol 1,4,5-trisphosphate receptor
Auteurs : Felipe Paredes [Chili] ; Valentina Parra [Chili] ; Natalia Torrealba [Chili] ; Mario Navarro-Marquez [Chili] ; Damian Gatica [Chili] ; Roberto Bravo-Sagua [Chili] ; Rodrigo Troncoso [Chili] ; Christian Pennanen [Chili] ; Clara Quiroga [Chili] ; Mario Chiong [Chili] ; Christa Caesar [États-Unis] ; W Robert Taylor [États-Unis] ; Jordi Molg [France] ; Alejandra San Martin [États-Unis] ; Enrique Jaimovich [Chili] ; Sergio Lavandero [Chili, États-Unis]Source :
- Free radical biology & medicine [ 0891-5849 ] ; 2015.
Abstract
Homocysteine-inducible, endoplasmic reticulum (ER) stress-inducible, ubiquitin-like domain member 1 (HERPUD1), an ER resident protein, is upregulated in response to ER stress and Ca2+ homeostasis deregulation. HERPUD1 exerts cytoprotective effects in various models, but its role during oxidative insult remains unknown. The aim of this study was to investigate whether HERPUD1 contributes to cytoprotection in response to redox stress and participates in mediating the stress-dependent signaling pathways. Our data showed that HERPUD1 protein levels increased in HeLa cells treated for 30 min with H2O2 or angiotensin II and in aortic tissue isolated from mice treated with angiotensin II for 3 weeks. Cell death was higher in
Url:
DOI: 10.1016/j.freeradbiomed.2015.11.024
PubMed: 26616647
PubMed Central: 4710961
Affiliations:
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PMC:4710961Le document en format XML
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<author><name sortKey="Bravo Sagua, Roberto" sort="Bravo Sagua, Roberto" uniqKey="Bravo Sagua R" first="Roberto" last="Bravo-Sagua">Roberto Bravo-Sagua</name>
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<author><name sortKey="Pennanen, Christian" sort="Pennanen, Christian" uniqKey="Pennanen C" first="Christian" last="Pennanen">Christian Pennanen</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">HERPUD1 protects against oxidative stress-induced apoptosis through downregulation of the inositol 1,4,5-trisphosphate receptor</title>
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<author><name sortKey="Bravo Sagua, Roberto" sort="Bravo Sagua, Roberto" uniqKey="Bravo Sagua R" first="Roberto" last="Bravo-Sagua">Roberto Bravo-Sagua</name>
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<author><name sortKey="Troncoso, Rodrigo" sort="Troncoso, Rodrigo" uniqKey="Troncoso R" first="Rodrigo" last="Troncoso">Rodrigo Troncoso</name>
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<author><name sortKey="Pennanen, Christian" sort="Pennanen, Christian" uniqKey="Pennanen C" first="Christian" last="Pennanen">Christian Pennanen</name>
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<author><name sortKey="Quiroga, Clara" sort="Quiroga, Clara" uniqKey="Quiroga C" first="Clara" last="Quiroga">Clara Quiroga</name>
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<author><name sortKey="Chiong, Mario" sort="Chiong, Mario" uniqKey="Chiong M" first="Mario" last="Chiong">Mario Chiong</name>
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<country xml:lang="fr">Chili</country>
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<author><name sortKey="Caesar, Christa" sort="Caesar, Christa" uniqKey="Caesar C" first="Christa" last="Caesar">Christa Caesar</name>
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<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology/Emory University, Atlanta, Georgia</wicri:regionArea>
<placeName><region type="state">Géorgie (États-Unis)</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Taylor, W Robert" sort="Taylor, W Robert" uniqKey="Taylor W" first="W Robert" last="Taylor">W Robert Taylor</name>
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<wicri:regionArea>Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology/Emory University, Atlanta, Georgia</wicri:regionArea>
<placeName><region type="state">Géorgie (États-Unis)</region>
</placeName>
</affiliation>
<affiliation wicri:level="2"><nlm:aff id="A5">Department of Medicine, Division of Cardiology, Emory University School of Medicine, Atlanta, Georgia, USA</nlm:aff>
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<wicri:regionArea>Department of Medicine, Division of Cardiology, Emory University School of Medicine, Atlanta, Georgia</wicri:regionArea>
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</placeName>
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<author><name sortKey="Molg, Jordi" sort="Molg, Jordi" uniqKey="Molg J" first="Jordi" last="Molg">Jordi Molg</name>
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</placeName>
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</author>
<author><name sortKey="Martin, Alejandra San" sort="Martin, Alejandra San" uniqKey="Martin A" first="Alejandra San" last="Martin">Alejandra San Martin</name>
<affiliation wicri:level="2"><nlm:aff id="A5">Department of Medicine, Division of Cardiology, Emory University School of Medicine, Atlanta, Georgia, USA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Medicine, Division of Cardiology, Emory University School of Medicine, Atlanta, Georgia</wicri:regionArea>
<placeName><region type="state">Géorgie (États-Unis)</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Jaimovich, Enrique" sort="Jaimovich, Enrique" uniqKey="Jaimovich E" first="Enrique" last="Jaimovich">Enrique Jaimovich</name>
<affiliation wicri:level="1"><nlm:aff id="A7">Centro de Estudios Moleculares de la Célula, Facultad de Medicina, Universidad de Chile, Santiago, Chile</nlm:aff>
<country xml:lang="fr">Chili</country>
<wicri:regionArea>Centro de Estudios Moleculares de la Célula, Facultad de Medicina, Universidad de Chile, Santiago</wicri:regionArea>
<wicri:noRegion>Santiago</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Lavandero, Sergio" sort="Lavandero, Sergio" uniqKey="Lavandero S" first="Sergio" last="Lavandero">Sergio Lavandero</name>
<affiliation wicri:level="1"><nlm:aff id="A1">Advanced Center for Chronic Diseases (ACCDiS), Facultad de Ciencias Químicas y Farmacéuticas & Facultad de Medicina, Universidad de Chile, Santiago, Chile</nlm:aff>
<country xml:lang="fr">Chili</country>
<wicri:regionArea>Advanced Center for Chronic Diseases (ACCDiS), Facultad de Ciencias Químicas y Farmacéuticas & Facultad de Medicina, Universidad de Chile, Santiago</wicri:regionArea>
<wicri:noRegion>Santiago</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A7">Centro de Estudios Moleculares de la Célula, Facultad de Medicina, Universidad de Chile, Santiago, Chile</nlm:aff>
<country xml:lang="fr">Chili</country>
<wicri:regionArea>Centro de Estudios Moleculares de la Célula, Facultad de Medicina, Universidad de Chile, Santiago</wicri:regionArea>
<wicri:noRegion>Santiago</wicri:noRegion>
</affiliation>
<affiliation wicri:level="2"><nlm:aff id="A8">Department of Internal Medicine (Cardiology Division), University of Texas Southwestern Medical Center, Dallas, Texas, USA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Internal Medicine (Cardiology Division), University of Texas Southwestern Medical Center, Dallas, Texas</wicri:regionArea>
<placeName><region type="state">Texas</region>
</placeName>
</affiliation>
</author>
</analytic>
<series><title level="j">Free radical biology & medicine</title>
<idno type="ISSN">0891-5849</idno>
<idno type="eISSN">1873-4596</idno>
<imprint><date when="2015">2015</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p id="P1">Homocysteine-inducible, endoplasmic reticulum (ER) stress-inducible, ubiquitin-like domain member 1 (HERPUD1), an ER resident protein, is upregulated in response to ER stress and Ca<sup>2+</sup>
homeostasis deregulation. HERPUD1 exerts cytoprotective effects in various models, but its role during oxidative insult remains unknown. The aim of this study was to investigate whether HERPUD1 contributes to cytoprotection in response to redox stress and participates in mediating the stress-dependent signaling pathways. Our data showed that HERPUD1 protein levels increased in HeLa cells treated for 30 min with H<sub>2</sub>
O<sub>2</sub>
or angiotensin II and in aortic tissue isolated from mice treated with angiotensin II for 3 weeks. Cell death was higher in <italic>HERPUD1</italic>
knockdown (sh-<italic>HERPUD1</italic>
) in HeLa cells treated with H<sub>2</sub>
O<sub>2</sub>
in comparison with control (sh-<italic>Luc</italic>
) HeLa cells. This effect was abolished by the intracellular Ca<sup>2+</sup>
chelating agent BAPTA-AM or the inositol 1,4,5-trisphosphate receptor (ITPR) antagonist xestospongin B, suggesting that the response to H<sub>2</sub>
O<sub>2</sub>
was dependent on intracellular Ca<sup>2+</sup>
stores and the ITPR. Ca<sup>2+</sup>
kinetics showed that sh-<italic>HERPUD1</italic>
HeLa cells exhibited greater and more sustained cytosolic and mitochondrial Ca<sup>2+</sup>
increases than sh-<italic>Luc</italic>
HeLa cells. This higher sensitivity of sh-<italic>HERPUD1</italic>
HeLa cells to H<sub>2</sub>
O<sub>2</sub>
was prevented with the mitochondrial permeability transition pore inhibitor cyclosporine A. We concluded that the HERPUD1-mediated cytoprotective effect against oxidative stress depends on the ITPR and Ca<sup>2+</sup>
transfer from the ER to mitochondria.</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">8709159</journal-id>
<journal-id journal-id-type="pubmed-jr-id">3902</journal-id>
<journal-id journal-id-type="nlm-ta">Free Radic Biol Med</journal-id>
<journal-id journal-id-type="iso-abbrev">Free Radic. Biol. Med.</journal-id>
<journal-title-group><journal-title>Free radical biology & medicine</journal-title>
</journal-title-group>
<issn pub-type="ppub">0891-5849</issn>
<issn pub-type="epub">1873-4596</issn>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">26616647</article-id>
<article-id pub-id-type="pmc">4710961</article-id>
<article-id pub-id-type="doi">10.1016/j.freeradbiomed.2015.11.024</article-id>
<article-id pub-id-type="manuscript">NIHMS745407</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>HERPUD1 protects against oxidative stress-induced apoptosis through downregulation of the inositol 1,4,5-trisphosphate receptor</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Paredes</surname>
<given-names>Felipe</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Parra</surname>
<given-names>Valentina</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Torrealba</surname>
<given-names>Natalia</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Navarro-Marquez</surname>
<given-names>Mario</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Gatica</surname>
<given-names>Damian</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Bravo-Sagua</surname>
<given-names>Roberto</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Troncoso</surname>
<given-names>Rodrigo</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
<xref ref-type="aff" rid="A2">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Pennanen</surname>
<given-names>Christian</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Quiroga</surname>
<given-names>Clara</given-names>
</name>
<xref ref-type="aff" rid="A3">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Chiong</surname>
<given-names>Mario</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Caesar</surname>
<given-names>Christa</given-names>
</name>
<xref ref-type="aff" rid="A4">4</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Taylor</surname>
<given-names>W Robert</given-names>
</name>
<xref ref-type="aff" rid="A4">4</xref>
<xref ref-type="aff" rid="A5">5</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Molgó</surname>
<given-names>Jordi</given-names>
</name>
<xref ref-type="aff" rid="A6">6</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Martin</surname>
<given-names>Alejandra San</given-names>
</name>
<xref ref-type="aff" rid="A5">5</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Jaimovich</surname>
<given-names>Enrique</given-names>
</name>
<xref ref-type="aff" rid="A7">7</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Lavandero</surname>
<given-names>Sergio</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
<xref ref-type="aff" rid="A7">7</xref>
<xref ref-type="aff" rid="A8">8</xref>
<xref rid="FN1" ref-type="author-notes">#</xref>
</contrib>
</contrib-group>
<aff id="A1"><label>1</label>
Advanced Center for Chronic Diseases (ACCDiS), Facultad de Ciencias Químicas y Farmacéuticas & Facultad de Medicina, Universidad de Chile, Santiago, Chile</aff>
<aff id="A2"><label>2</label>
Instituto de Nutrición y Tecnología de los Alimentos (INTA), Universidad de Chile, Santiago, Chile</aff>
<aff id="A3"><label>3</label>
ACCDiS, Cardiovascular Diseases Division, Faculty of Medicine, Pontifical Catholic University of Chile, Santiago, Chile</aff>
<aff id="A4"><label>4</label>
Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology/Emory University, Atlanta, Georgia, USA</aff>
<aff id="A5"><label>5</label>
Department of Medicine, Division of Cardiology, Emory University School of Medicine, Atlanta, Georgia, USA</aff>
<aff id="A6"><label>6</label>
Institut des Neurosciences Paris-Saclay, UMR 9197, 91190 Gif sur Yvette, France</aff>
<aff id="A7"><label>7</label>
Centro de Estudios Moleculares de la Célula, Facultad de Medicina, Universidad de Chile, Santiago, Chile</aff>
<aff id="A8"><label>8</label>
Department of Internal Medicine (Cardiology Division), University of Texas Southwestern Medical Center, Dallas, Texas, USA</aff>
<author-notes><corresp id="FN1"><label>#</label>
<italic>Correspondence:</italic>
Advanced Center for Chronic Disease (ACCDiS), Facultad de Ciencias Químicas y Farmacéuticas & Facultad Medicina, Universidad de Chile, Santiago 838049, Chile. Phone: +562 2978-2919; <email>slavander@uchile.cl</email>
(S Lavandero)</corresp>
</author-notes>
<pub-date pub-type="nihms-submitted"><day>6</day>
<month>1</month>
<year>2016</year>
</pub-date>
<pub-date pub-type="epub"><day>23</day>
<month>11</month>
<year>2015</year>
</pub-date>
<pub-date pub-type="ppub"><month>1</month>
<year>2016</year>
</pub-date>
<pub-date pub-type="pmc-release"><day>01</day>
<month>1</month>
<year>2017</year>
</pub-date>
<volume>90</volume>
<fpage>206</fpage>
<lpage>218</lpage>
<pmc-comment>elocation-id from pubmed: 10.1016/j.freeradbiomed.2015.11.024</pmc-comment>
<abstract><p id="P1">Homocysteine-inducible, endoplasmic reticulum (ER) stress-inducible, ubiquitin-like domain member 1 (HERPUD1), an ER resident protein, is upregulated in response to ER stress and Ca<sup>2+</sup>
homeostasis deregulation. HERPUD1 exerts cytoprotective effects in various models, but its role during oxidative insult remains unknown. The aim of this study was to investigate whether HERPUD1 contributes to cytoprotection in response to redox stress and participates in mediating the stress-dependent signaling pathways. Our data showed that HERPUD1 protein levels increased in HeLa cells treated for 30 min with H<sub>2</sub>
O<sub>2</sub>
or angiotensin II and in aortic tissue isolated from mice treated with angiotensin II for 3 weeks. Cell death was higher in <italic>HERPUD1</italic>
knockdown (sh-<italic>HERPUD1</italic>
) in HeLa cells treated with H<sub>2</sub>
O<sub>2</sub>
in comparison with control (sh-<italic>Luc</italic>
) HeLa cells. This effect was abolished by the intracellular Ca<sup>2+</sup>
chelating agent BAPTA-AM or the inositol 1,4,5-trisphosphate receptor (ITPR) antagonist xestospongin B, suggesting that the response to H<sub>2</sub>
O<sub>2</sub>
was dependent on intracellular Ca<sup>2+</sup>
stores and the ITPR. Ca<sup>2+</sup>
kinetics showed that sh-<italic>HERPUD1</italic>
HeLa cells exhibited greater and more sustained cytosolic and mitochondrial Ca<sup>2+</sup>
increases than sh-<italic>Luc</italic>
HeLa cells. This higher sensitivity of sh-<italic>HERPUD1</italic>
HeLa cells to H<sub>2</sub>
O<sub>2</sub>
was prevented with the mitochondrial permeability transition pore inhibitor cyclosporine A. We concluded that the HERPUD1-mediated cytoprotective effect against oxidative stress depends on the ITPR and Ca<sup>2+</sup>
transfer from the ER to mitochondria.</p>
</abstract>
<kwd-group><kwd>HERPUD1</kwd>
<kwd>oxidative stress</kwd>
<kwd>IP3 receptor</kwd>
<kwd>cell death</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>Chili</li>
<li>France</li>
<li>États-Unis</li>
</country>
<region><li>Géorgie (États-Unis)</li>
<li>Texas</li>
<li>Île-de-France</li>
</region>
<settlement><li>Gif sur Yvette</li>
</settlement>
</list>
<tree><country name="Chili"><noRegion><name sortKey="Paredes, Felipe" sort="Paredes, Felipe" uniqKey="Paredes F" first="Felipe" last="Paredes">Felipe Paredes</name>
</noRegion>
<name sortKey="Bravo Sagua, Roberto" sort="Bravo Sagua, Roberto" uniqKey="Bravo Sagua R" first="Roberto" last="Bravo-Sagua">Roberto Bravo-Sagua</name>
<name sortKey="Chiong, Mario" sort="Chiong, Mario" uniqKey="Chiong M" first="Mario" last="Chiong">Mario Chiong</name>
<name sortKey="Gatica, Damian" sort="Gatica, Damian" uniqKey="Gatica D" first="Damian" last="Gatica">Damian Gatica</name>
<name sortKey="Jaimovich, Enrique" sort="Jaimovich, Enrique" uniqKey="Jaimovich E" first="Enrique" last="Jaimovich">Enrique Jaimovich</name>
<name sortKey="Lavandero, Sergio" sort="Lavandero, Sergio" uniqKey="Lavandero S" first="Sergio" last="Lavandero">Sergio Lavandero</name>
<name sortKey="Lavandero, Sergio" sort="Lavandero, Sergio" uniqKey="Lavandero S" first="Sergio" last="Lavandero">Sergio Lavandero</name>
<name sortKey="Navarro Marquez, Mario" sort="Navarro Marquez, Mario" uniqKey="Navarro Marquez M" first="Mario" last="Navarro-Marquez">Mario Navarro-Marquez</name>
<name sortKey="Parra, Valentina" sort="Parra, Valentina" uniqKey="Parra V" first="Valentina" last="Parra">Valentina Parra</name>
<name sortKey="Pennanen, Christian" sort="Pennanen, Christian" uniqKey="Pennanen C" first="Christian" last="Pennanen">Christian Pennanen</name>
<name sortKey="Quiroga, Clara" sort="Quiroga, Clara" uniqKey="Quiroga C" first="Clara" last="Quiroga">Clara Quiroga</name>
<name sortKey="Torrealba, Natalia" sort="Torrealba, Natalia" uniqKey="Torrealba N" first="Natalia" last="Torrealba">Natalia Torrealba</name>
<name sortKey="Troncoso, Rodrigo" sort="Troncoso, Rodrigo" uniqKey="Troncoso R" first="Rodrigo" last="Troncoso">Rodrigo Troncoso</name>
<name sortKey="Troncoso, Rodrigo" sort="Troncoso, Rodrigo" uniqKey="Troncoso R" first="Rodrigo" last="Troncoso">Rodrigo Troncoso</name>
</country>
<country name="États-Unis"><region name="Géorgie (États-Unis)"><name sortKey="Caesar, Christa" sort="Caesar, Christa" uniqKey="Caesar C" first="Christa" last="Caesar">Christa Caesar</name>
</region>
<name sortKey="Lavandero, Sergio" sort="Lavandero, Sergio" uniqKey="Lavandero S" first="Sergio" last="Lavandero">Sergio Lavandero</name>
<name sortKey="Martin, Alejandra San" sort="Martin, Alejandra San" uniqKey="Martin A" first="Alejandra San" last="Martin">Alejandra San Martin</name>
<name sortKey="Taylor, W Robert" sort="Taylor, W Robert" uniqKey="Taylor W" first="W Robert" last="Taylor">W Robert Taylor</name>
<name sortKey="Taylor, W Robert" sort="Taylor, W Robert" uniqKey="Taylor W" first="W Robert" last="Taylor">W Robert Taylor</name>
</country>
<country name="France"><region name="Île-de-France"><name sortKey="Molg, Jordi" sort="Molg, Jordi" uniqKey="Molg J" first="Jordi" last="Molg">Jordi Molg</name>
</region>
</country>
</tree>
</affiliations>
</record>
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