Elevation of heme oxygenase‐1 by proteasome inhibition affords dopaminergic neuroprotection
Identifieur interne : 002388 ( Main/Corpus ); précédent : 002387; suivant : 002389Elevation of heme oxygenase‐1 by proteasome inhibition affords dopaminergic neuroprotection
Auteurs : Noriyuki Yamamoto ; Yasuhiko Izumi ; Takaaki Matsuo ; Seiko Wakita ; Toshiaki Kume ; Yuki Takada-Takatori ; Hideyuki Sawada ; Akinori AkaikeSource :
- Journal of Neuroscience Research [ 0360-4012 ] ; 2010-07.
English descriptors
Abstract
Postmortem studies have shown that heme oxygenase‐1 (HO‐1) immunoreactivity is increased in patients with Parkinson disease. HO‐1 expression is highly upregulated by a variety of stress. Since the proteasome activity is decreased in patients with Parkinson disease, we investigated whether proteasome activity regulates HO‐1 content. MG‐132, a proteasome inhibitor, increased the amount of HO‐1 protein mainly in astrocytes of primary mesencephalic cultures. Quantitative RT‐PCR analysis revealed that lactacystin upregulated HO‐1 mRNA expression. Proteasome inhibition with MG132 also increased the cytomegalovirus promoter‐driven expression of Flag‐HO‐1 protein and resulted in an accumulation of ubiquitinated Flag‐HO‐1 in Flag‐HO‐1‐overexpressing PC12 cells. In addition, a cycloheximide chase assay demonstrated that the degradation of Flag‐HO‐1 protein was slowed by MG‐132. Next, the function of HO‐1 which was upregulated by proteasome inhibitors was examined. Proteasome inhibitors protected dopaminergic neurons from 6‐hydroxydopamine (6‐OHDA)‐induced toxicity and this neuroprotection was abrogated by co‐treatment with zinc protoporphyrin IX, a HO‐1 inhibitor. Furthermore, 6‐OHDA‐induced toxicity was blocked by bilirubin and carbon monoxide, products of the HO‐1‐catalyzed degradation of heme. These results suggest that mesencephalic HO‐1 protein level is regulated by proteasome activity and the elevation by proteasome inhibition affords neuroprotection. © 2010 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/jnr.22363
Links to Exploration step
ISTEX:838363552C12D01E9EC63C11DAEDE8EB5364C25FLe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Elevation of heme oxygenase‐1 by proteasome inhibition affords dopaminergic neuroprotection</title><author><name sortKey="Yamamoto, Noriyuki" sort="Yamamoto, Noriyuki" uniqKey="Yamamoto N" first="Noriyuki" last="Yamamoto">Noriyuki Yamamoto</name><affiliation><mods:affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Izumi, Yasuhiko" sort="Izumi, Yasuhiko" uniqKey="Izumi Y" first="Yasuhiko" last="Izumi">Yasuhiko Izumi</name><affiliation><mods:affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Matsuo, Takaaki" sort="Matsuo, Takaaki" uniqKey="Matsuo T" first="Takaaki" last="Matsuo">Takaaki Matsuo</name><affiliation><mods:affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Wakita, Seiko" sort="Wakita, Seiko" uniqKey="Wakita S" first="Seiko" last="Wakita">Seiko Wakita</name><affiliation><mods:affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Kume, Toshiaki" sort="Kume, Toshiaki" uniqKey="Kume T" first="Toshiaki" last="Kume">Toshiaki Kume</name><affiliation><mods:affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Takada Akatori, Yuki" sort="Takada Akatori, Yuki" uniqKey="Takada Akatori Y" first="Yuki" last="Takada-Takatori">Yuki Takada-Takatori</name><affiliation><mods:affiliation>Department of Pharmacology, Faculty of Pharmaceutical Sciences, Doshisha Women's College, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Sawada, Hideyuki" sort="Sawada, Hideyuki" uniqKey="Sawada H" first="Hideyuki" last="Sawada">Hideyuki Sawada</name><affiliation><mods:affiliation>Department of Neurology and Clinical Research Center, Center for Neurological Diseases, Utano National Hospital, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Akaike, Akinori" sort="Akaike, Akinori" uniqKey="Akaike A" first="Akinori" last="Akaike">Akinori Akaike</name><affiliation><mods:affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:838363552C12D01E9EC63C11DAEDE8EB5364C25F</idno><date when="2010" year="2010">2010</date><idno type="doi">10.1002/jnr.22363</idno><idno type="url">https://api.istex.fr/document/838363552C12D01E9EC63C11DAEDE8EB5364C25F/fulltext/pdf</idno><idno type="wicri:Area/Main/Corpus">002388</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Elevation of heme oxygenase‐1 by proteasome inhibition affords dopaminergic neuroprotection</title><author><name sortKey="Yamamoto, Noriyuki" sort="Yamamoto, Noriyuki" uniqKey="Yamamoto N" first="Noriyuki" last="Yamamoto">Noriyuki Yamamoto</name><affiliation><mods:affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Izumi, Yasuhiko" sort="Izumi, Yasuhiko" uniqKey="Izumi Y" first="Yasuhiko" last="Izumi">Yasuhiko Izumi</name><affiliation><mods:affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Matsuo, Takaaki" sort="Matsuo, Takaaki" uniqKey="Matsuo T" first="Takaaki" last="Matsuo">Takaaki Matsuo</name><affiliation><mods:affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Wakita, Seiko" sort="Wakita, Seiko" uniqKey="Wakita S" first="Seiko" last="Wakita">Seiko Wakita</name><affiliation><mods:affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Kume, Toshiaki" sort="Kume, Toshiaki" uniqKey="Kume T" first="Toshiaki" last="Kume">Toshiaki Kume</name><affiliation><mods:affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Takada Akatori, Yuki" sort="Takada Akatori, Yuki" uniqKey="Takada Akatori Y" first="Yuki" last="Takada-Takatori">Yuki Takada-Takatori</name><affiliation><mods:affiliation>Department of Pharmacology, Faculty of Pharmaceutical Sciences, Doshisha Women's College, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Sawada, Hideyuki" sort="Sawada, Hideyuki" uniqKey="Sawada H" first="Hideyuki" last="Sawada">Hideyuki Sawada</name><affiliation><mods:affiliation>Department of Neurology and Clinical Research Center, Center for Neurological Diseases, Utano National Hospital, Kyoto, Japan</mods:affiliation></affiliation></author><author><name sortKey="Akaike, Akinori" sort="Akaike, Akinori" uniqKey="Akaike A" first="Akinori" last="Akaike">Akinori Akaike</name><affiliation><mods:affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Neuroscience Research</title><title level="j" type="abbrev">J. Neurosci. Res.</title><idno type="ISSN">0360-4012</idno><idno type="eISSN">1097-4547</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2010-07">2010-07</date><biblScope unit="volume">88</biblScope><biblScope unit="issue">9</biblScope><biblScope unit="page" from="1934">1934</biblScope><biblScope unit="page" to="1942">1942</biblScope></imprint><idno type="ISSN">0360-4012</idno></series><idno type="istex">838363552C12D01E9EC63C11DAEDE8EB5364C25F</idno><idno type="DOI">10.1002/jnr.22363</idno><idno type="ArticleID">JNR22363</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0360-4012</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Parkinson disease</term><term>heme oxygenase‐1</term><term>neuroprotection</term><term>proteasome</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Postmortem studies have shown that heme oxygenase‐1 (HO‐1) immunoreactivity is increased in patients with Parkinson disease. HO‐1 expression is highly upregulated by a variety of stress. Since the proteasome activity is decreased in patients with Parkinson disease, we investigated whether proteasome activity regulates HO‐1 content. MG‐132, a proteasome inhibitor, increased the amount of HO‐1 protein mainly in astrocytes of primary mesencephalic cultures. Quantitative RT‐PCR analysis revealed that lactacystin upregulated HO‐1 mRNA expression. Proteasome inhibition with MG132 also increased the cytomegalovirus promoter‐driven expression of Flag‐HO‐1 protein and resulted in an accumulation of ubiquitinated Flag‐HO‐1 in Flag‐HO‐1‐overexpressing PC12 cells. In addition, a cycloheximide chase assay demonstrated that the degradation of Flag‐HO‐1 protein was slowed by MG‐132. Next, the function of HO‐1 which was upregulated by proteasome inhibitors was examined. Proteasome inhibitors protected dopaminergic neurons from 6‐hydroxydopamine (6‐OHDA)‐induced toxicity and this neuroprotection was abrogated by co‐treatment with zinc protoporphyrin IX, a HO‐1 inhibitor. Furthermore, 6‐OHDA‐induced toxicity was blocked by bilirubin and carbon monoxide, products of the HO‐1‐catalyzed degradation of heme. These results suggest that mesencephalic HO‐1 protein level is regulated by proteasome activity and the elevation by proteasome inhibition affords neuroprotection. © 2010 Wiley‐Liss, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Noriyuki Yamamoto</name><affiliations><json:string>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</json:string></affiliations></json:item><json:item><name>Yasuhiko Izumi</name><affiliations><json:string>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</json:string></affiliations></json:item><json:item><name>Takaaki Matsuo</name><affiliations><json:string>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</json:string></affiliations></json:item><json:item><name>Seiko Wakita</name><affiliations><json:string>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</json:string></affiliations></json:item><json:item><name>Toshiaki Kume</name><affiliations><json:string>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</json:string></affiliations></json:item><json:item><name>Yuki Takada‐Takatori</name><affiliations><json:string>Department of Pharmacology, Faculty of Pharmaceutical Sciences, Doshisha Women's College, Kyoto, Japan</json:string></affiliations></json:item><json:item><name>Hideyuki Sawada</name><affiliations><json:string>Department of Neurology and Clinical Research Center, Center for Neurological Diseases, Utano National Hospital, Kyoto, Japan</json:string></affiliations></json:item><json:item><name>Akinori Akaike</name><affiliations><json:string>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>heme oxygenase‐1</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>neuroprotection</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Parkinson disease</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>proteasome</value></json:item></subject><articleId><json:string>JNR22363</json:string></articleId><language><json:string>eng</json:string></language><abstract>Postmortem studies have shown that heme oxygenase‐1 (HO‐1) immunoreactivity is increased in patients with Parkinson disease. HO‐1 expression is highly upregulated by a variety of stress. Since the proteasome activity is decreased in patients with Parkinson disease, we investigated whether proteasome activity regulates HO‐1 content. MG‐132, a proteasome inhibitor, increased the amount of HO‐1 protein mainly in astrocytes of primary mesencephalic cultures. Quantitative RT‐PCR analysis revealed that lactacystin upregulated HO‐1 mRNA expression. Proteasome inhibition with MG132 also increased the cytomegalovirus promoter‐driven expression of Flag‐HO‐1 protein and resulted in an accumulation of ubiquitinated Flag‐HO‐1 in Flag‐HO‐1‐overexpressing PC12 cells. In addition, a cycloheximide chase assay demonstrated that the degradation of Flag‐HO‐1 protein was slowed by MG‐132. Next, the function of HO‐1 which was upregulated by proteasome inhibitors was examined. Proteasome inhibitors protected dopaminergic neurons from 6‐hydroxydopamine (6‐OHDA)‐induced toxicity and this neuroprotection was abrogated by co‐treatment with zinc protoporphyrin IX, a HO‐1 inhibitor. Furthermore, 6‐OHDA‐induced toxicity was blocked by bilirubin and carbon monoxide, products of the HO‐1‐catalyzed degradation of heme. These results suggest that mesencephalic HO‐1 protein level is regulated by proteasome activity and the elevation by proteasome inhibition affords neuroprotection. © 2010 Wiley‐Liss, Inc.</abstract><qualityIndicators><score>7.304</score><pdfVersion>1.3</pdfVersion><pdfPageSize>612 x 810 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>4</keywordCount><abstractCharCount>1495</abstractCharCount><pdfWordCount>5560</pdfWordCount><pdfCharCount>36685</pdfCharCount><pdfPageCount>9</pdfPageCount><abstractWordCount>192</abstractWordCount></qualityIndicators><title>Elevation of heme oxygenase‐1 by proteasome inhibition affords dopaminergic neuroprotection</title><genre><json:string>article</json:string></genre><host><volume>88</volume><publisherId><json:string>JNR</json:string></publisherId><pages><total>9</total><last>1942</last><first>1934</first></pages><issn><json:string>0360-4012</json:string></issn><issue>9</issue><subject><json:item><value>Research Article</value></json:item></subject><genre><json:string>Journal</json:string></genre><language><json:string>unknown</json:string></language><eissn><json:string>1097-4547</json:string></eissn><title>Journal of Neuroscience Research</title><doi><json:string>10.1002/(ISSN)1097-4547</json:string></doi></host><publicationDate>2010</publicationDate><copyrightDate>2010</copyrightDate><doi><json:string>10.1002/jnr.22363</json:string></doi><id>838363552C12D01E9EC63C11DAEDE8EB5364C25F</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/838363552C12D01E9EC63C11DAEDE8EB5364C25F/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/838363552C12D01E9EC63C11DAEDE8EB5364C25F/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/838363552C12D01E9EC63C11DAEDE8EB5364C25F/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Elevation of heme oxygenase‐1 by proteasome inhibition affords dopaminergic neuroprotection</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><availability><p>WILEY</p></availability><date>2010</date></publicationStmt><notesStmt><note>Grants‐in‐Aid for Scientific Research</note><note>Japan Society for the Promotion of Science Fellows from the Japan Society for the Promotion of Science</note><note>Ministry of Education, Culture, Sports, Science and Technology of Japan</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Elevation of heme oxygenase‐1 by proteasome inhibition affords dopaminergic neuroprotection</title><author><persName><forename type="first">Noriyuki</forename><surname>Yamamoto</surname></persName><affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</affiliation></author><author><persName><forename type="first">Yasuhiko</forename><surname>Izumi</surname></persName><affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</affiliation></author><author><persName><forename type="first">Takaaki</forename><surname>Matsuo</surname></persName><affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</affiliation></author><author><persName><forename type="first">Seiko</forename><surname>Wakita</surname></persName><affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</affiliation></author><author><persName><forename type="first">Toshiaki</forename><surname>Kume</surname></persName><affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</affiliation></author><author><persName><forename type="first">Yuki</forename><surname>Takada‐Takatori</surname></persName><affiliation>Department of Pharmacology, Faculty of Pharmaceutical Sciences, Doshisha Women's College, Kyoto, Japan</affiliation></author><author><persName><forename type="first">Hideyuki</forename><surname>Sawada</surname></persName><affiliation>Department of Neurology and Clinical Research Center, Center for Neurological Diseases, Utano National Hospital, Kyoto, Japan</affiliation></author><author><persName><forename type="first">Akinori</forename><surname>Akaike</surname></persName><note type="correspondence"><p>Correspondence: Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, 46‐29 Yoshida‐shimoadachi‐cho, Sakyo‐ku, Kyoto 606‐8501, Japan</p></note><affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</affiliation></author></analytic><monogr><title level="j">Journal of Neuroscience Research</title><title level="j" type="abbrev">J. Neurosci. Res.</title><idno type="pISSN">0360-4012</idno><idno type="eISSN">1097-4547</idno><idno type="DOI">10.1002/(ISSN)1097-4547</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2010-07"></date><biblScope unit="volume">88</biblScope><biblScope unit="issue">9</biblScope><biblScope unit="page" from="1934">1934</biblScope><biblScope unit="page" to="1942">1942</biblScope></imprint></monogr><idno type="istex">838363552C12D01E9EC63C11DAEDE8EB5364C25F</idno><idno type="DOI">10.1002/jnr.22363</idno><idno type="ArticleID">JNR22363</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2010</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Postmortem studies have shown that heme oxygenase‐1 (HO‐1) immunoreactivity is increased in patients with Parkinson disease. HO‐1 expression is highly upregulated by a variety of stress. Since the proteasome activity is decreased in patients with Parkinson disease, we investigated whether proteasome activity regulates HO‐1 content. MG‐132, a proteasome inhibitor, increased the amount of HO‐1 protein mainly in astrocytes of primary mesencephalic cultures. Quantitative RT‐PCR analysis revealed that lactacystin upregulated HO‐1 mRNA expression. Proteasome inhibition with MG132 also increased the cytomegalovirus promoter‐driven expression of Flag‐HO‐1 protein and resulted in an accumulation of ubiquitinated Flag‐HO‐1 in Flag‐HO‐1‐overexpressing PC12 cells. In addition, a cycloheximide chase assay demonstrated that the degradation of Flag‐HO‐1 protein was slowed by MG‐132. Next, the function of HO‐1 which was upregulated by proteasome inhibitors was examined. Proteasome inhibitors protected dopaminergic neurons from 6‐hydroxydopamine (6‐OHDA)‐induced toxicity and this neuroprotection was abrogated by co‐treatment with zinc protoporphyrin IX, a HO‐1 inhibitor. Furthermore, 6‐OHDA‐induced toxicity was blocked by bilirubin and carbon monoxide, products of the HO‐1‐catalyzed degradation of heme. These results suggest that mesencephalic HO‐1 protein level is regulated by proteasome activity and the elevation by proteasome inhibition affords neuroprotection. © 2010 Wiley‐Liss, Inc.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>heme oxygenase‐1</term></item><item><term>neuroprotection</term></item><item><term>Parkinson disease</term></item><item><term>proteasome</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>article category</head><item><term>Research Article</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2009-08-10">Received</change><change when="2009-11-21">Registration</change><change when="2010-07">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/838363552C12D01E9EC63C11DAEDE8EB5364C25F/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Wiley Subscription Services, Inc., A Wiley Company</publisherName><publisherLoc>Hoboken</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1097-4547</doi><issn type="print">0360-4012</issn><issn type="electronic">1097-4547</issn><idGroup><id type="product" value="JNR"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="JOURNAL OF NEUROSCIENCE RESEARCH">Journal of Neuroscience Research</title><title type="short">J. Neurosci. Res.</title></titleGroup></publicationMeta><publicationMeta level="part" position="90"><doi origin="wiley" registered="yes">10.1002/jnr.v88:9</doi><numberingGroup><numbering type="journalVolume" number="88">88</numbering><numbering type="journalIssue">9</numbering></numberingGroup><coverDate startDate="2010-07">July 2010</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="110" status="forIssue"><doi origin="wiley" registered="yes">10.1002/jnr.22363</doi><idGroup><id type="unit" value="JNR22363"></id></idGroup><countGroup><count type="pageTotal" number="9"></count></countGroup><titleGroup><title type="articleCategory">Research Article</title><title type="tocHeading1">Research Articles</title></titleGroup><copyright ownership="publisher">Copyright © 2010 Wiley‐Liss, Inc.</copyright><eventGroup><event type="manuscriptReceived" date="2009-08-10"></event><event type="manuscriptRevised" date="2009-11-16"></event><event type="manuscriptAccepted" date="2009-11-21"></event><event type="publishedOnlineEarlyUnpaginated" date="2010-02-12"></event><event type="firstOnline" date="2010-02-12"></event><event type="publishedOnlineFinalForm" date="2010-05-10"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.6 mode:FullText source:FullText result:FullText" date="2010-05-11"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-31"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-30"></event></eventGroup><numberingGroup><numbering type="pageFirst">1934</numbering><numbering type="pageLast">1942</numbering></numberingGroup><correspondenceTo>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, 46‐29 Yoshida‐shimoadachi‐cho, Sakyo‐ku, Kyoto 606‐8501, Japan</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:JNR.JNR22363.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="6"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="43"></count><count type="wordTotal" number="5818"></count></countGroup><titleGroup><title type="main" xml:lang="en">Elevation of heme oxygenase‐1 by proteasome inhibition affords dopaminergic neuroprotection</title><title type="short" xml:lang="en">Neuroprotection of Upregulated HO‐1</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Noriyuki</givenNames><familyName>Yamamoto</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Yasuhiko</givenNames><familyName>Izumi</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Takaaki</givenNames><familyName>Matsuo</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Seiko</givenNames><familyName>Wakita</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Toshiaki</givenNames><familyName>Kume</familyName></personName></creator><creator xml:id="au6" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Yuki</givenNames><familyName>Takada‐Takatori</familyName></personName></creator><creator xml:id="au7" creatorRole="author" affiliationRef="#af3"><personName><givenNames>Hideyuki</givenNames><familyName>Sawada</familyName></personName></creator><creator xml:id="au8" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Akinori</givenNames><familyName>Akaike</familyName></personName><contactDetails><email normalForm="aakaike@pharm.kyoto-u.ac.jp">aakaike@pharm.kyoto‐u.ac.jp</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="JP" type="organization"><unparsedAffiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="JP" type="organization"><unparsedAffiliation>Department of Pharmacology, Faculty of Pharmaceutical Sciences, Doshisha Women's College, Kyoto, Japan</unparsedAffiliation></affiliation><affiliation xml:id="af3" countryCode="JP" type="organization"><unparsedAffiliation>Department of Neurology and Clinical Research Center, Center for Neurological Diseases, Utano National Hospital, Kyoto, Japan</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">heme oxygenase‐1</keyword><keyword xml:id="kwd2">neuroprotection</keyword><keyword xml:id="kwd3">Parkinson disease</keyword><keyword xml:id="kwd4">proteasome</keyword></keywordGroup><fundingInfo><fundingAgency>Grants‐in‐Aid for Scientific Research</fundingAgency></fundingInfo><fundingInfo><fundingAgency>Japan Society for the Promotion of Science Fellows from the Japan Society for the Promotion of Science</fundingAgency></fundingInfo><fundingInfo><fundingAgency>Ministry of Education, Culture, Sports, Science and Technology of Japan</fundingAgency></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Postmortem studies have shown that heme oxygenase‐1 (HO‐1) immunoreactivity is increased in patients with Parkinson disease. HO‐1 expression is highly upregulated by a variety of stress. Since the proteasome activity is decreased in patients with Parkinson disease, we investigated whether proteasome activity regulates HO‐1 content. MG‐132, a proteasome inhibitor, increased the amount of HO‐1 protein mainly in astrocytes of primary mesencephalic cultures. Quantitative RT‐PCR analysis revealed that lactacystin upregulated HO‐1 mRNA expression. Proteasome inhibition with MG132 also increased the cytomegalovirus promoter‐driven expression of Flag‐HO‐1 protein and resulted in an accumulation of ubiquitinated Flag‐HO‐1 in Flag‐HO‐1‐overexpressing PC12 cells. In addition, a cycloheximide chase assay demonstrated that the degradation of Flag‐HO‐1 protein was slowed by MG‐132. Next, the function of HO‐1 which was upregulated by proteasome inhibitors was examined. Proteasome inhibitors protected dopaminergic neurons from 6‐hydroxydopamine (6‐OHDA)‐induced toxicity and this neuroprotection was abrogated by co‐treatment with zinc protoporphyrin IX, a HO‐1 inhibitor. Furthermore, 6‐OHDA‐induced toxicity was blocked by bilirubin and carbon monoxide, products of the HO‐1‐catalyzed degradation of heme. These results suggest that mesencephalic HO‐1 protein level is regulated by proteasome activity and the elevation by proteasome inhibition affords neuroprotection. © 2010 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Elevation of heme oxygenase‐1 by proteasome inhibition affords dopaminergic neuroprotection</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Neuroprotection of Upregulated HO‐1</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Elevation of heme oxygenase‐1 by proteasome inhibition affords dopaminergic neuroprotection</title></titleInfo><name type="personal"><namePart type="given">Noriyuki</namePart><namePart type="family">Yamamoto</namePart><affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Yasuhiko</namePart><namePart type="family">Izumi</namePart><affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Takaaki</namePart><namePart type="family">Matsuo</namePart><affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Seiko</namePart><namePart type="family">Wakita</namePart><affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Toshiaki</namePart><namePart type="family">Kume</namePart><affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Yuki</namePart><namePart type="family">Takada‐Takatori</namePart><affiliation>Department of Pharmacology, Faculty of Pharmaceutical Sciences, Doshisha Women's College, Kyoto, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Hideyuki</namePart><namePart type="family">Sawada</namePart><affiliation>Department of Neurology and Clinical Research Center, Center for Neurological Diseases, Utano National Hospital, Kyoto, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Akinori</namePart><namePart type="family">Akaike</namePart><affiliation>Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan</affiliation><description>Correspondence: Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, 46‐29 Yoshida‐shimoadachi‐cho, Sakyo‐ku, Kyoto 606‐8501, Japan</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2010-07</dateIssued><dateCaptured encoding="w3cdtf">2009-08-10</dateCaptured><dateValid encoding="w3cdtf">2009-11-21</dateValid><copyrightDate encoding="w3cdtf">2010</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">6</extent><extent unit="references">43</extent><extent unit="words">5818</extent></physicalDescription><abstract lang="en">Postmortem studies have shown that heme oxygenase‐1 (HO‐1) immunoreactivity is increased in patients with Parkinson disease. HO‐1 expression is highly upregulated by a variety of stress. Since the proteasome activity is decreased in patients with Parkinson disease, we investigated whether proteasome activity regulates HO‐1 content. MG‐132, a proteasome inhibitor, increased the amount of HO‐1 protein mainly in astrocytes of primary mesencephalic cultures. Quantitative RT‐PCR analysis revealed that lactacystin upregulated HO‐1 mRNA expression. Proteasome inhibition with MG132 also increased the cytomegalovirus promoter‐driven expression of Flag‐HO‐1 protein and resulted in an accumulation of ubiquitinated Flag‐HO‐1 in Flag‐HO‐1‐overexpressing PC12 cells. In addition, a cycloheximide chase assay demonstrated that the degradation of Flag‐HO‐1 protein was slowed by MG‐132. Next, the function of HO‐1 which was upregulated by proteasome inhibitors was examined. Proteasome inhibitors protected dopaminergic neurons from 6‐hydroxydopamine (6‐OHDA)‐induced toxicity and this neuroprotection was abrogated by co‐treatment with zinc protoporphyrin IX, a HO‐1 inhibitor. Furthermore, 6‐OHDA‐induced toxicity was blocked by bilirubin and carbon monoxide, products of the HO‐1‐catalyzed degradation of heme. These results suggest that mesencephalic HO‐1 protein level is regulated by proteasome activity and the elevation by proteasome inhibition affords neuroprotection. © 2010 Wiley‐Liss, Inc.</abstract><note type="funding">Grants‐in‐Aid for Scientific Research</note><note type="funding">Japan Society for the Promotion of Science Fellows from the Japan Society for the Promotion of Science</note><note type="funding">Ministry of Education, Culture, Sports, Science and Technology of Japan</note><subject lang="en"><genre>Keywords</genre><topic>heme oxygenase‐1</topic><topic>neuroprotection</topic><topic>Parkinson disease</topic><topic>proteasome</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Neuroscience Research</title></titleInfo><titleInfo type="abbreviated"><title>J. Neurosci. Res.</title></titleInfo><genre type="Journal">journal</genre><subject><genre>article category</genre><topic>Research Article</topic></subject><identifier type="ISSN">0360-4012</identifier><identifier type="eISSN">1097-4547</identifier><identifier type="DOI">10.1002/(ISSN)1097-4547</identifier><identifier type="PublisherID">JNR</identifier><part><date>2010</date><detail type="volume"><caption>vol.</caption><number>88</number></detail><detail type="issue"><caption>no.</caption><number>9</number></detail><extent unit="pages"><start>1934</start><end>1942</end><total>9</total></extent></part></relatedItem><identifier type="istex">838363552C12D01E9EC63C11DAEDE8EB5364C25F</identifier><identifier type="DOI">10.1002/jnr.22363</identifier><identifier type="ArticleID">JNR22363</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2010 Wiley‐Liss, Inc.</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Wiley Subscription Services, Inc., A Wiley Company</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonV1/Data/Main/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002388 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 002388 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Sante
|area= ParkinsonV1
|flux= Main
|étape= Corpus
|type= RBID
|clé= ISTEX:838363552C12D01E9EC63C11DAEDE8EB5364C25F
|texte= Elevation of heme oxygenase‐1 by proteasome inhibition affords dopaminergic neuroprotection
}}
| This area was generated with Dilib version V0.6.23. |  |