Epigallocatechin Gallate (EGCG) Inhibits Alpha-Synuclein Aggregation: A Potential Agent for Parkinson's Disease.
Identifieur interne : 000147 ( PubMed/Corpus ); précédent : 000146; suivant : 000148Epigallocatechin Gallate (EGCG) Inhibits Alpha-Synuclein Aggregation: A Potential Agent for Parkinson's Disease.
Auteurs : Yan Xu ; Yanyan Zhang ; Zhenzhen Quan ; Winnie Wong ; Jianping Guo ; Rongkai Zhang ; Qinghu Yang ; Rongji Dai ; Patrick L. Mcgeer ; Hong QingSource :
- Neurochemical research [ 1573-6903 ] ; 2016.
English descriptors
- KwdEn :
- MESH :
- chemical , analogs & derivatives : Catechin.
- chemical , metabolism : alpha-Synuclein.
- chemical , pharmacology : Catechin.
- drug effects : Lewy Bodies.
- drug therapy : Parkinson Disease.
- metabolism : Lewy Bodies, Parkinson Disease.
- pathology : Parkinson Disease.
- Cells, Cultured, Humans.
Abstract
Protein aggregation is a prominent feature of many neurodegenerative disorders including Parkinson's disease (PD). Aggregation of alpha-synuclein (SNCA) may underlie the pathology of PD. They are the main components of Lewy bodies and dystrophic neurites that are the intraneuronal inclusions characteristic of the disease. We have demonstrated that the polyphenol (-)-epi-gallocatechine gallate (EGCG) inhibited SNCA aggregation, which made it a candidate for therapeutic intervention in PD. Three methods were used: SNCA fibril formation inhibition by EGCG in incubates; inhibition of the SNCA fluorophore A-Syn-HiLyte488 binding to plated SNCA in microwells; and inhibition of the A-Syn-HiLyte488 probe binding to aggregated SNCA in postmortem PD tissue. Recombinant human SNCA was incubated under conditions that result in fibril formation. The aggregation was blocked by 100 nM EGCG in a concentration-dependent manner, as shown by an absence of thioflavin T binding. In the microplate assay system, the ED50 of EGCG inhibition of A-Syn-HiLyte488 binding to coated SNCA was 250 nM. In the PD tissue based assay, SNCA aggregates were recognized by incubation with 7 nM of A-Syn-HiLyte488. This binding was blocked by EGCG in a concentration dependent manner. The SNCA amino acid sites, which potentially interacted with EGCG, were detected on peptide membranes. It was implicated that EGCG binds to SNCA by instable hydrophobic interactions. In this study, we suggested that EGCG could be a potent remodeling agent of SNCA aggregates and a potential disease modifying drug for the treatment of PD and other α-synucleinopathies.
DOI: 10.1007/s11064-016-1995-9
PubMed: 27364962
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Mcgeer</name><affiliation><nlm:affiliation>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Qing, Hong" sort="Qing, Hong" uniqKey="Qing H" first="Hong" last="Qing">Hong Qing</name><affiliation><nlm:affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China. hqing@bit.edu.cn.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:27364962</idno><idno type="pmid">27364962</idno><idno type="doi">10.1007/s11064-016-1995-9</idno><idno type="wicri:Area/PubMed/Corpus">000147</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000147</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Epigallocatechin Gallate (EGCG) Inhibits Alpha-Synuclein Aggregation: A Potential Agent for Parkinson's Disease.</title><author><name sortKey="Xu, Yan" sort="Xu, Yan" uniqKey="Xu Y" first="Yan" last="Xu">Yan Xu</name><affiliation><nlm:affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.</nlm:affiliation></affiliation></author><author><name sortKey="Zhang, Yanyan" sort="Zhang, Yanyan" uniqKey="Zhang Y" first="Yanyan" last="Zhang">Yanyan Zhang</name><affiliation><nlm:affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.</nlm:affiliation></affiliation></author><author><name sortKey="Quan, Zhenzhen" sort="Quan, Zhenzhen" uniqKey="Quan Z" first="Zhenzhen" last="Quan">Zhenzhen Quan</name><affiliation><nlm:affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.</nlm:affiliation></affiliation></author><author><name sortKey="Wong, Winnie" sort="Wong, Winnie" uniqKey="Wong W" first="Winnie" last="Wong">Winnie Wong</name><affiliation><nlm:affiliation>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Guo, Jianping" sort="Guo, Jianping" uniqKey="Guo J" first="Jianping" last="Guo">Jianping Guo</name><affiliation><nlm:affiliation>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Zhang, Rongkai" sort="Zhang, Rongkai" uniqKey="Zhang R" first="Rongkai" last="Zhang">Rongkai Zhang</name><affiliation><nlm:affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Qinghu" sort="Yang, Qinghu" uniqKey="Yang Q" first="Qinghu" last="Yang">Qinghu Yang</name><affiliation><nlm:affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.</nlm:affiliation></affiliation></author><author><name sortKey="Dai, Rongji" sort="Dai, Rongji" uniqKey="Dai R" first="Rongji" last="Dai">Rongji Dai</name><affiliation><nlm:affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.</nlm:affiliation></affiliation></author><author><name sortKey="Mcgeer, Patrick L" sort="Mcgeer, Patrick L" uniqKey="Mcgeer P" first="Patrick L" last="Mcgeer">Patrick L. Mcgeer</name><affiliation><nlm:affiliation>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Qing, Hong" sort="Qing, Hong" uniqKey="Qing H" first="Hong" last="Qing">Hong Qing</name><affiliation><nlm:affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China. hqing@bit.edu.cn.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Neurochemical research</title><idno type="eISSN">1573-6903</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Catechin (analogs & derivatives)</term><term>Catechin (pharmacology)</term><term>Cells, Cultured</term><term>Humans</term><term>Lewy Bodies (drug effects)</term><term>Lewy Bodies (metabolism)</term><term>Parkinson Disease (drug therapy)</term><term>Parkinson Disease (metabolism)</term><term>Parkinson Disease (pathology)</term><term>alpha-Synuclein (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Catechin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Catechin</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Lewy Bodies</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Lewy Bodies</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cells, Cultured</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Protein aggregation is a prominent feature of many neurodegenerative disorders including Parkinson's disease (PD). Aggregation of alpha-synuclein (SNCA) may underlie the pathology of PD. They are the main components of Lewy bodies and dystrophic neurites that are the intraneuronal inclusions characteristic of the disease. We have demonstrated that the polyphenol (-)-epi-gallocatechine gallate (EGCG) inhibited SNCA aggregation, which made it a candidate for therapeutic intervention in PD. Three methods were used: SNCA fibril formation inhibition by EGCG in incubates; inhibition of the SNCA fluorophore A-Syn-HiLyte488 binding to plated SNCA in microwells; and inhibition of the A-Syn-HiLyte488 probe binding to aggregated SNCA in postmortem PD tissue. Recombinant human SNCA was incubated under conditions that result in fibril formation. The aggregation was blocked by 100 nM EGCG in a concentration-dependent manner, as shown by an absence of thioflavin T binding. In the microplate assay system, the ED50 of EGCG inhibition of A-Syn-HiLyte488 binding to coated SNCA was 250 nM. In the PD tissue based assay, SNCA aggregates were recognized by incubation with 7 nM of A-Syn-HiLyte488. This binding was blocked by EGCG in a concentration dependent manner. The SNCA amino acid sites, which potentially interacted with EGCG, were detected on peptide membranes. It was implicated that EGCG binds to SNCA by instable hydrophobic interactions. In this study, we suggested that EGCG could be a potent remodeling agent of SNCA aggregates and a potential disease modifying drug for the treatment of PD and other α-synucleinopathies.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27364962</PMID><DateCreated><Year>2016</Year><Month>07</Month><Day>01</Day></DateCreated><DateCompleted><Year>2017</Year><Month>04</Month><Day>04</Day></DateCompleted><DateRevised><Year>2017</Year><Month>04</Month><Day>04</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1573-6903</ISSN><JournalIssue CitedMedium="Internet"><Volume>41</Volume><Issue>10</Issue><PubDate><Year>2016</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Neurochemical research</Title><ISOAbbreviation>Neurochem. Res.</ISOAbbreviation></Journal><ArticleTitle>Epigallocatechin Gallate (EGCG) Inhibits Alpha-Synuclein Aggregation: A Potential Agent for Parkinson's Disease.</ArticleTitle><Pagination><MedlinePgn>2788-2796</MedlinePgn></Pagination><Abstract><AbstractText>Protein aggregation is a prominent feature of many neurodegenerative disorders including Parkinson's disease (PD). Aggregation of alpha-synuclein (SNCA) may underlie the pathology of PD. They are the main components of Lewy bodies and dystrophic neurites that are the intraneuronal inclusions characteristic of the disease. We have demonstrated that the polyphenol (-)-epi-gallocatechine gallate (EGCG) inhibited SNCA aggregation, which made it a candidate for therapeutic intervention in PD. Three methods were used: SNCA fibril formation inhibition by EGCG in incubates; inhibition of the SNCA fluorophore A-Syn-HiLyte488 binding to plated SNCA in microwells; and inhibition of the A-Syn-HiLyte488 probe binding to aggregated SNCA in postmortem PD tissue. Recombinant human SNCA was incubated under conditions that result in fibril formation. The aggregation was blocked by 100 nM EGCG in a concentration-dependent manner, as shown by an absence of thioflavin T binding. In the microplate assay system, the ED50 of EGCG inhibition of A-Syn-HiLyte488 binding to coated SNCA was 250 nM. In the PD tissue based assay, SNCA aggregates were recognized by incubation with 7 nM of A-Syn-HiLyte488. This binding was blocked by EGCG in a concentration dependent manner. The SNCA amino acid sites, which potentially interacted with EGCG, were detected on peptide membranes. It was implicated that EGCG binds to SNCA by instable hydrophobic interactions. In this study, we suggested that EGCG could be a potent remodeling agent of SNCA aggregates and a potential disease modifying drug for the treatment of PD and other α-synucleinopathies.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>Yan</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Yanyan</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Quan</LastName><ForeName>Zhenzhen</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wong</LastName><ForeName>Winnie</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Jianping</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Rongkai</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Qinghu</ForeName><Initials>Q</Initials><AffiliationInfo><Affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dai</LastName><ForeName>Rongji</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>McGeer</LastName><ForeName>Patrick L</ForeName><Initials>PL</Initials><AffiliationInfo><Affiliation>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Qing</LastName><ForeName>Hong</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China. hqing@bit.edu.cn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>06</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Neurochem Res</MedlineTA><NlmUniqueID>7613461</NlmUniqueID><ISSNLinking>0364-3190</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C497604">SNCA protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical><Chemical><RegistryNumber>8R1V1STN48</RegistryNumber><NameOfSubstance UI="D002392">Catechin</NameOfSubstance></Chemical><Chemical><RegistryNumber>BQM438CTEL</RegistryNumber><NameOfSubstance UI="C045651">epigallocatechin gallate</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002392" MajorTopicYN="N">Catechin</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016631" MajorTopicYN="N">Lewy Bodies</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">EGCG</Keyword><Keyword MajorTopicYN="Y">Parkinson’s disease</Keyword><Keyword MajorTopicYN="Y">SNCA aggregation</Keyword><Keyword MajorTopicYN="Y">α-synucleinopathy</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>11</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>06</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>06</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>7</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>4</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>7</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27364962</ArticleId><ArticleId IdType="doi">10.1007/s11064-016-1995-9</ArticleId><ArticleId IdType="pii">10.1007/s11064-016-1995-9</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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