Cyanidin-3-glucoside activates Nrf2-antioxidant response element and protects against glutamate-induced oxidative and endoplasmic reticulum stress in HT22 hippocampal neuronal cells.
Identifieur interne : 000189 ( Main/Exploration ); précédent : 000188; suivant : 000190Cyanidin-3-glucoside activates Nrf2-antioxidant response element and protects against glutamate-induced oxidative and endoplasmic reticulum stress in HT22 hippocampal neuronal cells.
Auteurs : Monruedee Sukprasansap [Thaïlande] ; Pithi Chanvorachote [Thaïlande] ; Tewin Tencomnao [Thaïlande]Source :
- BMC complementary medicine and therapies [ 2662-7671 ] ; 2020.
Descripteurs français
- KwdFr :
- Acide glutamique (MeSH), Animaux (MeSH), Anthocyanes (pharmacologie), Antioxydants (métabolisme), Cytométrie en flux (MeSH), Extraits de plantes (pharmacologie), Facteur-2 apparenté à NF-E2 (métabolisme), Glucosides (pharmacologie), Hippocampe (cytologie), Lignée cellulaire (MeSH), Neurones (effets des médicaments et des substances chimiques), Neuroprotecteurs (pharmacologie), Souris (MeSH), Stress du réticulum endoplasmique (effets des médicaments et des substances chimiques), Structure moléculaire (MeSH).
- MESH :
- cytologie : Hippocampe.
- effets des médicaments et des substances chimiques : Neurones, Stress du réticulum endoplasmique.
- métabolisme : Antioxydants, Facteur-2 apparenté à NF-E2.
- pharmacologie : Anthocyanes, Extraits de plantes, Glucosides, Neuroprotecteurs.
- Acide glutamique, Animaux, Cytométrie en flux, Lignée cellulaire, Souris, Structure moléculaire.
English descriptors
- KwdEn :
- Animals (MeSH), Anthocyanins (pharmacology), Antioxidants (metabolism), Cell Line (MeSH), Endoplasmic Reticulum Stress (drug effects), Flow Cytometry (MeSH), Glucosides (pharmacology), Glutamic Acid (MeSH), Hippocampus (cytology), Mice (MeSH), Molecular Structure (MeSH), NF-E2-Related Factor 2 (metabolism), Neurons (drug effects), Neuroprotective Agents (pharmacology), Plant Extracts (pharmacology).
- MESH :
- chemical , metabolism : Antioxidants, NF-E2-Related Factor 2.
- chemical , pharmacology : Anthocyanins, Glucosides, Neuroprotective Agents, Plant Extracts.
- cytology : Hippocampus.
- drug effects : Endoplasmic Reticulum Stress, Neurons.
- Animals, Cell Line, Flow Cytometry, Glutamic Acid, Mice, Molecular Structure.
Abstract
BACKGROUND
Cyanidin-3-glucoside (C3G), a major anthocyanin present in berries, exhibits a strong antioxidant and has been shown to possess a neuroprotection. Prolonged exposure to glutamate will lead to oxidative damage and endoplasmic reticulum stress which could play a key detrimental role in the development of neurodegenerative disorders (NDs). In the present study, we investigated the neuroprotective effect and underlying mechanisms of C3G on the reduction of oxidative/ER stress-induced apoptosis by glutamate in HT22 mouse hippocampal neuronal cells.
METHOD
Cells were pre-treated with C3G in various concentrations, followed by glutamate. Cell viability and toxicity were examined using MTT and LDH assays. The apoptotic and necrotic cell death were carried out by Annexin V-FITC/propidium iodide co-staining assays. Generation of intracellular reactive oxygen species (ROS) in cells was measured by flow cytometry using DCFH-DA probe. Expression of antioxidant genes was evaluated by Real-time polymerase chain reaction analysis. The possible signaling pathways and proteins involved were subsequently demonstrated by Western blot analysis.
RESULT
The pretreatment of the HT22 cells with C3G protected cell death from oxidative toxicity induced by glutamate. We demonstrated that treatment cells with glutamate caused several radical forms of ROS formation, and they were abolished by specific ROS inhibitors. Interestingly, C3G directly scavenged radical activity and inhibited intracellular ROS generation in our cell-based system. In addition, C3G pretreatment suppressed the up-regulation of specific ER proteins namely calpain, caspase-12 and C/EBP homologous proteins (CHOP) induced by glutamate-mediated oxidative and ER stress signal by up-regulating the expressions of survival proteins, including extracellular regulated protein kinase (ERK) and nuclear factor E2-related factor 2 (Nrf2). Furthermore, dramatically activated gene expression of endogenous antioxidant enzymes (i.e. superoxide dismutases (SODs), catalase (CAT) and glutathione peroxidase (GPx)), and phase II enzymes (glutathione-S-transferases (GSTs)) was found in C3G-treated with cells.
CONCLUSIONS
Our finding suggest that C3G could be a promising neuroprotectant via inhibition of glutamate-induced oxidative and ER stress signal and activation of ERK/Nrf2 antioxidant mechanism pathways.
DOI: 10.1186/s12906-020-2819-7
PubMed: 32046712
PubMed Central: PMC7076852
Affiliations:
Links toward previous steps (curation, corpus...)
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uniqKey="Chanvorachote P" first="Pithi" last="Chanvorachote">Pithi Chanvorachote</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pharmacology and Physiology, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, 10330, Thailand.</nlm:affiliation><country xml:lang="fr">Thaïlande</country><wicri:regionArea>Department of Pharmacology and Physiology, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, 10330</wicri:regionArea><wicri:noRegion>10330</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Cell-based Drug and Health Products Development Research Unit, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, 10330, Thailand.</nlm:affiliation><country xml:lang="fr">Thaïlande</country><wicri:regionArea>Cell-based Drug and Health Products Development Research Unit, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, 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4 Road, Salaya, Nakhon Pathom, 73170, Thailand.</nlm:affiliation><country xml:lang="fr">Thaïlande</country><wicri:regionArea>Food Toxicology Unit, Institute of Nutrition, Mahidol University, Salaya campus, 25/25 Phuttamonthon 4 Road, Salaya, Nakhon Pathom, 73170</wicri:regionArea><wicri:noRegion>73170</wicri:noRegion></affiliation></author><author><name sortKey="Chanvorachote, Pithi" sort="Chanvorachote, Pithi" uniqKey="Chanvorachote P" first="Pithi" last="Chanvorachote">Pithi Chanvorachote</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pharmacology and Physiology, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, 10330, Thailand.</nlm:affiliation><country xml:lang="fr">Thaïlande</country><wicri:regionArea>Department of Pharmacology and Physiology, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, 10330</wicri:regionArea><wicri:noRegion>10330</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Cell-based Drug and Health Products Development Research Unit, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, 10330, Thailand.</nlm:affiliation><country xml:lang="fr">Thaïlande</country><wicri:regionArea>Cell-based Drug and Health Products Development Research Unit, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, 10330</wicri:regionArea><wicri:noRegion>10330</wicri:noRegion></affiliation></author><author><name sortKey="Tencomnao, Tewin" sort="Tencomnao, Tewin" uniqKey="Tencomnao T" first="Tewin" last="Tencomnao">Tewin Tencomnao</name><affiliation wicri:level="1"><nlm:affiliation>Age-Related Inflammation and Degeneration Research Unit, Department of Clinical Chemistry, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok, 10330, Thailand. tewin.t@chula.ac.th.</nlm:affiliation><country xml:lang="fr">Thaïlande</country><wicri:regionArea>Age-Related Inflammation and Degeneration Research Unit, Department of Clinical Chemistry, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok, 10330</wicri:regionArea><wicri:noRegion>10330</wicri:noRegion></affiliation></author></analytic><series><title level="j">BMC complementary medicine and therapies</title><idno type="eISSN">2662-7671</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Anthocyanins (pharmacology)</term><term>Antioxidants (metabolism)</term><term>Cell Line (MeSH)</term><term>Endoplasmic Reticulum Stress (drug effects)</term><term>Flow Cytometry (MeSH)</term><term>Glucosides (pharmacology)</term><term>Glutamic Acid (MeSH)</term><term>Hippocampus (cytology)</term><term>Mice (MeSH)</term><term>Molecular Structure (MeSH)</term><term>NF-E2-Related Factor 2 (metabolism)</term><term>Neurons (drug effects)</term><term>Neuroprotective Agents (pharmacology)</term><term>Plant Extracts (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide glutamique (MeSH)</term><term>Animaux (MeSH)</term><term>Anthocyanes (pharmacologie)</term><term>Antioxydants (métabolisme)</term><term>Cytométrie en flux (MeSH)</term><term>Extraits de plantes (pharmacologie)</term><term>Facteur-2 apparenté à NF-E2 (métabolisme)</term><term>Glucosides (pharmacologie)</term><term>Hippocampe (cytologie)</term><term>Lignée cellulaire (MeSH)</term><term>Neurones (effets des médicaments et des substances chimiques)</term><term>Neuroprotecteurs (pharmacologie)</term><term>Souris (MeSH)</term><term>Stress du réticulum endoplasmique (effets des médicaments et des substances chimiques)</term><term>Structure moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antioxidants</term><term>NF-E2-Related Factor 2</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Anthocyanins</term><term>Glucosides</term><term>Neuroprotective Agents</term><term>Plant Extracts</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Hippocampe</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Hippocampus</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Endoplasmic Reticulum Stress</term><term>Neurons</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Neurones</term><term>Stress du réticulum endoplasmique</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antioxydants</term><term>Facteur-2 apparenté à NF-E2</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Anthocyanes</term><term>Extraits de plantes</term><term>Glucosides</term><term>Neuroprotecteurs</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Flow Cytometry</term><term>Glutamic Acid</term><term>Mice</term><term>Molecular Structure</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acide glutamique</term><term>Animaux</term><term>Cytométrie en flux</term><term>Lignée cellulaire</term><term>Souris</term><term>Structure moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b></p><p>Cyanidin-3-glucoside (C3G), a major anthocyanin present in berries, exhibits a strong antioxidant and has been shown to possess a neuroprotection. Prolonged exposure to glutamate will lead to oxidative damage and endoplasmic reticulum stress which could play a key detrimental role in the development of neurodegenerative disorders (NDs). In the present study, we investigated the neuroprotective effect and underlying mechanisms of C3G on the reduction of oxidative/ER stress-induced apoptosis by glutamate in HT22 mouse hippocampal neuronal cells.</p></div><div type="abstract" xml:lang="en"><p><b>METHOD</b></p><p>Cells were pre-treated with C3G in various concentrations, followed by glutamate. Cell viability and toxicity were examined using MTT and LDH assays. The apoptotic and necrotic cell death were carried out by Annexin V-FITC/propidium iodide co-staining assays. Generation of intracellular reactive oxygen species (ROS) in cells was measured by flow cytometry using DCFH-DA probe. Expression of antioxidant genes was evaluated by Real-time polymerase chain reaction analysis. The possible signaling pathways and proteins involved were subsequently demonstrated by Western blot analysis.</p></div><div type="abstract" xml:lang="en"><p><b>RESULT</b></p><p>The pretreatment of the HT22 cells with C3G protected cell death from oxidative toxicity induced by glutamate. We demonstrated that treatment cells with glutamate caused several radical forms of ROS formation, and they were abolished by specific ROS inhibitors. Interestingly, C3G directly scavenged radical activity and inhibited intracellular ROS generation in our cell-based system. In addition, C3G pretreatment suppressed the up-regulation of specific ER proteins namely calpain, caspase-12 and C/EBP homologous proteins (CHOP) induced by glutamate-mediated oxidative and ER stress signal by up-regulating the expressions of survival proteins, including extracellular regulated protein kinase (ERK) and nuclear factor E2-related factor 2 (Nrf2). Furthermore, dramatically activated gene expression of endogenous antioxidant enzymes (i.e. superoxide dismutases (SODs), catalase (CAT) and glutathione peroxidase (GPx)), and phase II enzymes (glutathione-S-transferases (GSTs)) was found in C3G-treated with cells.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b></p><p>Our finding suggest that C3G could be a promising neuroprotectant via inhibition of glutamate-induced oxidative and ER stress signal and activation of ERK/Nrf2 antioxidant mechanism pathways.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32046712</PMID><DateCompleted><Year>2020</Year><Month>08</Month><Day>17</Day></DateCompleted><DateRevised><Year>2020</Year><Month>08</Month><Day>17</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2662-7671</ISSN><JournalIssue CitedMedium="Internet"><Volume>20</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>Feb</Month><Day>11</Day></PubDate></JournalIssue><Title>BMC complementary medicine and therapies</Title><ISOAbbreviation>BMC Complement Med Ther</ISOAbbreviation></Journal><ArticleTitle>Cyanidin-3-glucoside activates Nrf2-antioxidant response element and protects against glutamate-induced oxidative and endoplasmic reticulum stress in HT22 hippocampal neuronal cells.</ArticleTitle><Pagination><MedlinePgn>46</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1186/s12906-020-2819-7</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Cyanidin-3-glucoside (C3G), a major anthocyanin present in berries, exhibits a strong antioxidant and has been shown to possess a neuroprotection. Prolonged exposure to glutamate will lead to oxidative damage and endoplasmic reticulum stress which could play a key detrimental role in the development of neurodegenerative disorders (NDs). In the present study, we investigated the neuroprotective effect and underlying mechanisms of C3G on the reduction of oxidative/ER stress-induced apoptosis by glutamate in HT22 mouse hippocampal neuronal cells.</AbstractText><AbstractText Label="METHOD" NlmCategory="METHODS">Cells were pre-treated with C3G in various concentrations, followed by glutamate. Cell viability and toxicity were examined using MTT and LDH assays. The apoptotic and necrotic cell death were carried out by Annexin V-FITC/propidium iodide co-staining assays. Generation of intracellular reactive oxygen species (ROS) in cells was measured by flow cytometry using DCFH-DA probe. Expression of antioxidant genes was evaluated by Real-time polymerase chain reaction analysis. The possible signaling pathways and proteins involved were subsequently demonstrated by Western blot analysis.</AbstractText><AbstractText Label="RESULT" NlmCategory="RESULTS">The pretreatment of the HT22 cells with C3G protected cell death from oxidative toxicity induced by glutamate. We demonstrated that treatment cells with glutamate caused several radical forms of ROS formation, and they were abolished by specific ROS inhibitors. Interestingly, C3G directly scavenged radical activity and inhibited intracellular ROS generation in our cell-based system. In addition, C3G pretreatment suppressed the up-regulation of specific ER proteins namely calpain, caspase-12 and C/EBP homologous proteins (CHOP) induced by glutamate-mediated oxidative and ER stress signal by up-regulating the expressions of survival proteins, including extracellular regulated protein kinase (ERK) and nuclear factor E2-related factor 2 (Nrf2). Furthermore, dramatically activated gene expression of endogenous antioxidant enzymes (i.e. superoxide dismutases (SODs), catalase (CAT) and glutathione peroxidase (GPx)), and phase II enzymes (glutathione-S-transferases (GSTs)) was found in C3G-treated with cells.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">Our finding suggest that C3G could be a promising neuroprotectant via inhibition of glutamate-induced oxidative and ER stress signal and activation of ERK/Nrf2 antioxidant mechanism pathways.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sukprasansap</LastName><ForeName>Monruedee</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Food Toxicology Unit, Institute of Nutrition, Mahidol University, Salaya campus, 25/25 Phuttamonthon 4 Road, Salaya, Nakhon Pathom, 73170, Thailand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chanvorachote</LastName><ForeName>Pithi</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Pharmacology and Physiology, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, 10330, Thailand.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Cell-based Drug and Health Products Development Research Unit, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, 10330, Thailand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tencomnao</LastName><ForeName>Tewin</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Age-Related Inflammation and Degeneration Research Unit, Department of Clinical Chemistry, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok, 10330, Thailand. tewin.t@chula.ac.th.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>TT</GrantID><Agency>Thailand Research Fund</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>02</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>BMC Complement Med Ther</MedlineTA><NlmUniqueID>101761232</NlmUniqueID><ISSNLinking>2662-7671</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000872">Anthocyanins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000975">Antioxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005960">Glucosides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051267">NF-E2-Related Factor 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018696">Neuroprotective Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C495636">Nfe2l2 protein, mouse</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010936">Plant Extracts</NameOfSubstance></Chemical><Chemical><RegistryNumber>3KX376GY7L</RegistryNumber><NameOfSubstance UI="D018698">Glutamic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>7084-24-4</RegistryNumber><NameOfSubstance UI="C114438">cyanidin 3-O-glucoside</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000872" MajorTopicYN="N">Anthocyanins</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000975" MajorTopicYN="N">Antioxidants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D059865" MajorTopicYN="N">Endoplasmic Reticulum Stress</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005434" MajorTopicYN="N">Flow Cytometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005960" MajorTopicYN="N">Glucosides</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018698" MajorTopicYN="N">Glutamic Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006624" MajorTopicYN="N">Hippocampus</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051267" MajorTopicYN="N">NF-E2-Related Factor 2</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018696" MajorTopicYN="N">Neuroprotective Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010936" MajorTopicYN="N">Plant Extracts</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Anthocyanin</Keyword><Keyword MajorTopicYN="N">Antioxidant enzyme</Keyword><Keyword MajorTopicYN="N">Cyanidin-3-glucoside</Keyword><Keyword MajorTopicYN="N">ER stress</Keyword><Keyword MajorTopicYN="N">Glutamate</Keyword><Keyword MajorTopicYN="N">HT22 cells</Keyword><Keyword MajorTopicYN="N">Neuroprotective effect</Keyword><Keyword MajorTopicYN="N">Nrf2</Keyword><Keyword MajorTopicYN="N">Oxidative stress</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>06</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>01</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>2</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>2</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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