Epigallocatechin Gallate (EGCG) Inhibits Alpha-Synuclein Aggregation: A Potential Agent for Parkinson's Disease.
Identifieur interne : 000364 ( Main/Exploration ); précédent : 000363; suivant : 000365Epigallocatechin Gallate (EGCG) Inhibits Alpha-Synuclein Aggregation: A Potential Agent for Parkinson's Disease.
Auteurs : Yan Xu [République populaire de Chine] ; Yanyan Zhang [République populaire de Chine] ; Zhenzhen Quan [République populaire de Chine] ; Winnie Wong [Canada] ; Jianping Guo [Canada] ; Rongkai Zhang [République populaire de Chine] ; Qinghu Yang [République populaire de Chine] ; Rongji Dai [République populaire de Chine] ; Patrick L. Mcgeer [Canada] ; Hong Qing [République populaire de Chine]Source :
- 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
Affiliations:
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type="wicri:Area/Main/Curation">000364</idno><idno type="wicri:Area/Main/Exploration">000364</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 wicri:level="1"><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><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081</wicri:regionArea><wicri:noRegion>100081</wicri:noRegion></affiliation></author><author><name sortKey="Zhang, Yanyan" sort="Zhang, Yanyan" uniqKey="Zhang Y" first="Yanyan" last="Zhang">Yanyan Zhang</name><affiliation wicri:level="1"><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><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081</wicri:regionArea><wicri:noRegion>100081</wicri:noRegion></affiliation></author><author><name sortKey="Quan, Zhenzhen" sort="Quan, Zhenzhen" uniqKey="Quan Z" first="Zhenzhen" last="Quan">Zhenzhen Quan</name><affiliation wicri:level="1"><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><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081</wicri:regionArea><wicri:noRegion>100081</wicri:noRegion></affiliation></author><author><name sortKey="Wong, Winnie" sort="Wong, Winnie" uniqKey="Wong W" first="Winnie" last="Wong">Winnie Wong</name><affiliation wicri:level="1"><nlm:affiliation>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC</wicri:regionArea><wicri:noRegion>BC</wicri:noRegion></affiliation></author><author><name sortKey="Guo, Jianping" sort="Guo, Jianping" uniqKey="Guo J" first="Jianping" last="Guo">Jianping Guo</name><affiliation wicri:level="1"><nlm:affiliation>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC</wicri:regionArea><wicri:noRegion>BC</wicri:noRegion></affiliation></author><author><name sortKey="Zhang, Rongkai" sort="Zhang, Rongkai" uniqKey="Zhang R" first="Rongkai" last="Zhang">Rongkai Zhang</name><affiliation wicri:level="1"><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><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081</wicri:regionArea><wicri:noRegion>100081</wicri:noRegion></affiliation></author><author><name sortKey="Yang, Qinghu" sort="Yang, Qinghu" uniqKey="Yang Q" first="Qinghu" last="Yang">Qinghu Yang</name><affiliation wicri:level="1"><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><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081</wicri:regionArea><wicri:noRegion>100081</wicri:noRegion></affiliation></author><author><name sortKey="Dai, Rongji" sort="Dai, Rongji" uniqKey="Dai R" first="Rongji" last="Dai">Rongji Dai</name><affiliation wicri:level="1"><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><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081</wicri:regionArea><wicri:noRegion>100081</wicri:noRegion></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 wicri:level="1"><nlm:affiliation>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Kinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC</wicri:regionArea><wicri:noRegion>BC</wicri:noRegion></affiliation></author><author><name sortKey="Qing, Hong" sort="Qing, Hong" uniqKey="Qing H" first="Hong" last="Qing">Hong Qing</name><affiliation wicri:level="1"><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><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Research Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081</wicri:regionArea><wicri:noRegion>100081</wicri:noRegion></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><affiliations><list><country><li>Canada</li><li>République populaire de Chine</li></country></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Xu, Yan" sort="Xu, Yan" uniqKey="Xu Y" first="Yan" last="Xu">Yan Xu</name></noRegion><name sortKey="Dai, Rongji" sort="Dai, Rongji" uniqKey="Dai R" first="Rongji" last="Dai">Rongji Dai</name><name sortKey="Qing, Hong" sort="Qing, Hong" uniqKey="Qing H" first="Hong" last="Qing">Hong Qing</name><name sortKey="Quan, Zhenzhen" sort="Quan, Zhenzhen" uniqKey="Quan Z" first="Zhenzhen" last="Quan">Zhenzhen Quan</name><name sortKey="Yang, Qinghu" sort="Yang, Qinghu" uniqKey="Yang Q" first="Qinghu" last="Yang">Qinghu Yang</name><name sortKey="Zhang, Rongkai" sort="Zhang, Rongkai" uniqKey="Zhang R" first="Rongkai" last="Zhang">Rongkai Zhang</name><name sortKey="Zhang, Yanyan" sort="Zhang, Yanyan" uniqKey="Zhang Y" first="Yanyan" last="Zhang">Yanyan Zhang</name></country><country name="Canada"><noRegion><name sortKey="Wong, Winnie" sort="Wong, Winnie" uniqKey="Wong W" first="Winnie" last="Wong">Winnie Wong</name></noRegion><name sortKey="Guo, Jianping" sort="Guo, Jianping" uniqKey="Guo J" first="Jianping" last="Guo">Jianping Guo</name><name sortKey="Mcgeer, Patrick L" sort="Mcgeer, Patrick L" uniqKey="Mcgeer P" first="Patrick L" last="Mcgeer">Patrick L. 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