GSK3: a key target for the development of novel treatments for type 2 diabetes mellitus and Alzheimer disease
Identifieur interne : 002483 ( Main/Corpus ); précédent : 002482; suivant : 002484GSK3: a key target for the development of novel treatments for type 2 diabetes mellitus and Alzheimer disease
Auteurs : Chong Gao ; Christian Hölscher ; Yueze Liu ; Lin LiSource :
- Reviews in the Neurosciences [ 0334-1763 ] ; 2012-02-01.
Abstract
As a constitutively active kinase, glycogen synthase kinase 3 (GSK3) is a kinase which regulates body metabolism by phosphorylation of glycogen synthase (GS) and other substrates. Considerable evidence suggests that GSK3 is involved in the common pathology underlying Alzheimer’s disease (AD) and type 2 diabetes mellitus (T2DM). The overexpression or overactivation of GSK3 could induce a series of pathological changes, most of which are hallmarks of AD and T2DM. Therefore, GSK3 could be a novel target to treat these two age-dependent diseases. The inhibition of this kinase can prevent the aggregation of β-amyloid (Aβ) and hyperphosphorylation of tau protein. GSK3 inhibition can also be a promising strategy to ameliorate neurodegenerative developments. Its potential association with memory formation has been shown in electrophysiological and behavioral experiments. The neuroprotective effects of novel drugs developed to treat T2DM, glucagon-like peptide 1 (GLP-1) and its long-lasting analogs, have a possible link to GSK3 modification. Recent investigations of the interaction between the phosphatidylinositol 3 kinase (PI3K) signaling pathway and the protective effect of novel GPL-1 receptor agonist geniposide on PC12 cells support this theory.
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DOI: 10.1515/rns.2011.061
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Considerable evidence suggests that GSK3 is involved in the common pathology underlying Alzheimer’s disease (AD) and type 2 diabetes mellitus (T2DM). The overexpression or overactivation of GSK3 could induce a series of pathological changes, most of which are hallmarks of AD and T2DM. Therefore, GSK3 could be a novel target to treat these two age-dependent diseases. The inhibition of this kinase can prevent the aggregation of β-amyloid (Aβ) and hyperphosphorylation of tau protein. GSK3 inhibition can also be a promising strategy to ameliorate neurodegenerative developments. Its potential association with memory formation has been shown in electrophysiological and behavioral experiments. The neuroprotective effects of novel drugs developed to treat T2DM, glucagon-like peptide 1 (GLP-1) and its long-lasting analogs, have a possible link to GSK3 modification. Recent investigations of the interaction between the phosphatidylinositol 3 kinase (PI3K) signaling pathway and the protective effect of novel GPL-1 receptor agonist geniposide on PC12 cells support this theory.</div></front></TEI><istex><corpusName>degruyter-journals</corpusName><author><json:item><name>Chong Gao</name><affiliations><json:string>Department of Physiology, Key Laboratory of Cellular Physiology, Ministry of Education, Shanxi Medical University, Taiyuan, 030001, China</json:string></affiliations></json:item><json:item><name>Christian Hölscher</name><affiliations><json:string>School of Biomedical Sciences, University of Ulster, Coleraine, BT52 1SA, UK</json:string></affiliations></json:item><json:item><name>Yueze Liu</name><affiliations><json:string>Department of Physiology, Key Laboratory of Cellular Physiology, Ministry of Education, Shanxi Medical University, Taiyuan, 030001, China</json:string></affiliations></json:item><json:item><name>Lin Li</name><affiliations><json:string>Department of Physiology, Key Laboratory of Cellular Physiology, Ministry of Education, Shanxi Medical University, Taiyuan, 030001, China</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Alzheimer’s disease</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>β-amyloid (Aβ)</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>glucagon-like peptide 1 (GLP-1)</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>glycogen synthase kinase 3 (GSK3)</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>neurofibrillary tangles (NFTs)</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>type 2 diabetes mellitus (T2DM)</value></json:item></subject><language><json:string>eng</json:string></language><abstract>As a constitutively active kinase, glycogen synthase kinase 3 (GSK3) is a kinase which regulates body metabolism by phosphorylation of glycogen synthase (GS) and other substrates. 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Recent investigations of the interaction between the phosphatidylinositol 3 kinase (PI3K) signaling pathway and the protective effect of novel GPL-1 receptor agonist geniposide on PC12 cells support this theory.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Alzheimer’s disease</term></item><item><term>β-amyloid (Aβ)</term></item><item><term>glucagon-like peptide 1 (GLP-1)</term></item><item><term>glycogen synthase kinase 3 (GSK3)</term></item><item><term>neurofibrillary tangles (NFTs)</term></item><item><term>type 2 diabetes mellitus (T2DM)</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2011-12-21">Created</change><change when="2012-02-01">Published</change><change xml:id="refBibs-istex" who="#ISTEX-API" when="2016-3-13">References added</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/42B2B54B46BC722D15DD9A320B25B12251AD24DC/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus degruyter-journals" wicri:toSee="no header"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//Atypon//DTD Atypon Systems Archival NLM DTD Suite v2.2.0 20090301//EN" URI="nlm-dtd/archivearticle.dtd" name="istex:docType"></istex:docType><istex:document><article article-type="research-article" xml:lang="EN"><front><journal-meta><journal-id journal-id-type="publisher-id">revneuro</journal-id><abbrev-journal-title abbrev-type="full">Reviews in the Neurosciences</abbrev-journal-title><issn pub-type="epub">2191-0200</issn><issn pub-type="ppub">0334-1763</issn><publisher><publisher-name>Walter de Gruyter</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">rns.2011.061</article-id><article-id pub-id-type="doi">10.1515/rns.2011.061</article-id><article-categories><subj-group subj-group-type="heading"><subject></subject></subj-group></article-categories><title-group><article-title>GSK3: a key target for the development of novel treatments for type 2 diabetes mellitus and Alzheimer disease</article-title></title-group><contrib-group><contrib contrib-type="author"><name name-style="western"><given-names>Chong</given-names><x> </x><surname>Gao</surname></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><x>, </x></contrib><contrib contrib-type="author"><name name-style="western"><given-names>Christian</given-names><x> </x><surname>Hölscher</surname></name><xref ref-type="aff" rid="aff2"><sup>2</sup></xref><x>, </x></contrib><contrib contrib-type="author"><name name-style="western"><given-names>Yueze</given-names><x> </x><surname>Liu</surname></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><x>, </x></contrib><contrib contrib-type="author"><name name-style="western"><given-names>Lin</given-names><x> </x><surname>Li</surname></name><email>linlilin999@163.com</email><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><x>, </x></contrib><aff id="aff1"><sup>1</sup>Department of Physiology, Key Laboratory of Cellular Physiology, Ministry of Education, Shanxi Medical University, Taiyuan, 030001, China</aff><aff id="aff2"><sup>2</sup>School of Biomedical Sciences, University of Ulster, Coleraine, BT52 1SA, UK</aff></contrib-group><author-notes><corresp>Corresponding author</corresp></author-notes><pub-date pub-type="ppub"><day>01</day><month>02</month><year>2012</year><string-date>February 2012</string-date></pub-date><pub-date pub-type="epub"><day>21</day><month>12</month><year>2011</year></pub-date><volume>23</volume><issue>1</issue><fpage>1</fpage><lpage>11</lpage><history><date date-type="received"><day>14</day><month>9</month><year>2011</year></date><date date-type="accepted"><day>21</day><month>12</month><year>2011</year></date></history><copyright-statement>©2012 by Walter de Gruyter Berlin Boston</copyright-statement><copyright-year>2012</copyright-year><related-article related-article-type="pdf" xlink:href="rns.2011.061.pdf"></related-article><abstract><title>Abstract</title><p>As a constitutively active kinase, glycogen synthase kinase 3 (GSK3) is a kinase which regulates body metabolism by phosphorylation of glycogen synthase (GS) and other substrates. Considerable evidence suggests that GSK3 is involved in the common pathology underlying Alzheimer’s disease (AD) and type 2 diabetes mellitus (T2DM). The overexpression or overactivation of GSK3 could induce a series of pathological changes, most of which are hallmarks of AD and T2DM. Therefore, GSK3 could be a novel target to treat these two age-dependent diseases. The inhibition of this kinase can prevent the aggregation of β-amyloid (Aβ) and hyperphosphorylation of tau protein. GSK3 inhibition can also be a promising strategy to ameliorate neurodegenerative developments. Its potential association with memory formation has been shown in electrophysiological and behavioral experiments. The neuroprotective effects of novel drugs developed to treat T2DM, glucagon-like peptide 1 (GLP-1) and its long-lasting analogs, have a possible link to GSK3 modification. Recent investigations of the interaction between the phosphatidylinositol 3 kinase (PI3K) signaling pathway and the protective effect of novel GPL-1 receptor agonist geniposide on PC12 cells support this theory.</p></abstract><kwd-group><title>Keywords</title><kwd>Alzheimer’s disease</kwd><x>, </x><kwd>β-amyloid (Aβ)</kwd><x>, </x><kwd>glucagon-like peptide 1 (GLP-1)</kwd><x>, </x><kwd>glycogen synthase kinase 3 (GSK3)</kwd><x>, </x><kwd>neurofibrillary tangles (NFTs)</kwd><x>, </x><kwd>type 2 diabetes mellitus (T2DM)</kwd></kwd-group><counts><fig-count count="6"></fig-count><table-count count="0"></table-count><ref-count count="134"></ref-count></counts></article-meta></front></article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>GSK3: a key target for the development of novel treatments for type 2 diabetes mellitus and Alzheimer disease</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>GSK3: a key target for the development of novel treatments for type 2 diabetes mellitus and Alzheimer disease</title></titleInfo><name type="personal"><namePart type="given">Chong</namePart><namePart type="family">Gao</namePart><affiliation>Department of Physiology, Key Laboratory of Cellular Physiology, Ministry of Education, Shanxi Medical University, Taiyuan, 030001, China</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Christian</namePart><namePart type="family">Hölscher</namePart><affiliation>School of Biomedical Sciences, University of Ulster, Coleraine, BT52 1SA, UK</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Yueze</namePart><namePart type="family">Liu</namePart><affiliation>Department of Physiology, Key Laboratory of Cellular Physiology, Ministry of Education, Shanxi Medical University, Taiyuan, 030001, China</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Lin</namePart><namePart type="family">Li</namePart><affiliation>Department of Physiology, Key Laboratory of Cellular Physiology, Ministry of Education, Shanxi Medical University, Taiyuan, 030001, China</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="research-article"></genre><originInfo><publisher>Walter de Gruyter</publisher><dateIssued encoding="w3cdtf">2012-02-01</dateIssued><dateCreated encoding="w3cdtf">2011-12-21</dateCreated><copyrightDate encoding="w3cdtf">2012</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">6</extent><extent unit="references">134</extent></physicalDescription><abstract lang="en">As a constitutively active kinase, glycogen synthase kinase 3 (GSK3) is a kinase which regulates body metabolism by phosphorylation of glycogen synthase (GS) and other substrates. Considerable evidence suggests that GSK3 is involved in the common pathology underlying Alzheimer’s disease (AD) and type 2 diabetes mellitus (T2DM). The overexpression or overactivation of GSK3 could induce a series of pathological changes, most of which are hallmarks of AD and T2DM. Therefore, GSK3 could be a novel target to treat these two age-dependent diseases. The inhibition of this kinase can prevent the aggregation of β-amyloid (Aβ) and hyperphosphorylation of tau protein. GSK3 inhibition can also be a promising strategy to ameliorate neurodegenerative developments. Its potential association with memory formation has been shown in electrophysiological and behavioral experiments. The neuroprotective effects of novel drugs developed to treat T2DM, glucagon-like peptide 1 (GLP-1) and its long-lasting analogs, have a possible link to GSK3 modification. Recent investigations of the interaction between the phosphatidylinositol 3 kinase (PI3K) signaling pathway and the protective effect of novel GPL-1 receptor agonist geniposide on PC12 cells support this theory.</abstract><note type="author-notes">Corresponding author</note><subject><genre>Keywords</genre><topic>Alzheimer’s disease</topic><topic>β-amyloid (Aβ)</topic><topic>glucagon-like peptide 1 (GLP-1)</topic><topic>glycogen synthase kinase 3 (GSK3)</topic><topic>neurofibrillary tangles (NFTs)</topic><topic>type 2 diabetes mellitus (T2DM)</topic></subject><relatedItem type="host"><titleInfo><title>Reviews in the Neurosciences</title></titleInfo><titleInfo type="abbreviated"><title>Reviews in the Neurosciences</title></titleInfo><genre type="Journal">journal</genre><identifier type="ISSN">0334-1763</identifier><identifier type="eISSN">2191-0200</identifier><identifier type="PublisherID">revneuro</identifier><part><date>2012</date><detail type="volume"><caption>vol.</caption><number>23</number></detail><detail type="issue"><caption>no.</caption><number>1</number></detail><extent unit="pages"><start>1</start><end>11</end></extent></part></relatedItem><relatedItem type="reviewOf"><genre>pdf</genre><identifier type="pdf">rns.2011.061.pdf</identifier></relatedItem><identifier type="istex">42B2B54B46BC722D15DD9A320B25B12251AD24DC</identifier><identifier type="DOI">10.1515/rns.2011.061</identifier><identifier type="ArticleID">rns.2011.061</identifier><identifier type="Related-article-Href">rns.2011.061.pdf</identifier><accessCondition type="use and reproduction" contentType="copyright">©2012 by Walter de Gruyter Berlin Boston</accessCondition><recordInfo><recordContentSource>De Gruyter</recordContentSource></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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