Sesamin modulates tyrosine hydroxylase, superoxide dismutase, catalase, inducible NO synthase and interleukin-6 expression in dopaminergic cells under MPP+-induced oxidative stress.
Identifieur interne : 000F45 ( PubMed/Corpus ); précédent : 000F44; suivant : 000F46Sesamin modulates tyrosine hydroxylase, superoxide dismutase, catalase, inducible NO synthase and interleukin-6 expression in dopaminergic cells under MPP+-induced oxidative stress.
Auteurs : Vicky Lahaie-Collins ; Julie Bournival ; Marilyn Plouffe ; Julie Carange ; Maria-Grazia MartinoliSource :
- Oxidative medicine and cellular longevity [ 1942-0994 ]
English descriptors
- KwdEn :
- 1-Methyl-4-phenylpyridinium (pharmacology), Animals, Antioxidants (pharmacology), Catalase (biosynthesis), Catalase (metabolism), Dioxoles (pharmacology), Dopamine (metabolism), Dopamine Plasma Membrane Transport Proteins (metabolism), Interleukin-6 (biosynthesis), Interleukin-6 (metabolism), Lignans (pharmacology), Neurons (drug effects), Neurons (enzymology), Neurons (metabolism), Nitric Oxide Synthase Type II (biosynthesis), Nitric Oxide Synthase Type II (metabolism), Oxidative Stress (drug effects), Oxidative Stress (physiology), PC12 Cells, Rats, Reactive Oxygen Species (metabolism), Superoxide Dismutase (biosynthesis), Superoxide Dismutase (metabolism), Tyrosine 3-Monooxygenase (biosynthesis), Tyrosine 3-Monooxygenase (metabolism).
- MESH :
- chemical , biosynthesis : Catalase, Interleukin-6, Nitric Oxide Synthase Type II, Superoxide Dismutase, Tyrosine 3-Monooxygenase.
- chemical , metabolism : Catalase, Dopamine, Dopamine Plasma Membrane Transport Proteins, Interleukin-6, Nitric Oxide Synthase Type II, Reactive Oxygen Species, Superoxide Dismutase, Tyrosine 3-Monooxygenase.
- chemical , pharmacology : 1-Methyl-4-phenylpyridinium, Antioxidants, Dioxoles, Lignans.
- drug effects : Neurons, Oxidative Stress.
- enzymology : Neurons.
- metabolism : Neurons.
- physiology : Oxidative Stress.
- Animals, PC12 Cells, Rats.
Abstract
Oxidative stress is regarded as a mediator of nerve cell death in several neurodegenerative disorders, such as Parkinson's disease. Sesamin, a lignan mainly found in sesame oil, is currently under study for its anti-oxidative and possible neuroprotective properties. We used 1-methyl-4-phenyl-pyridine (MPP(+)) ion, the active metabolite of the potent parkinsonism-causing toxin 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine, to produce oxidative stress and neurodegeneration in neuronal PC12 cells, which express dopamine, as well as neurofilaments. Our results show that picomolar doses of sesamin protected neuronal PC12 cells from MPP(+)-induced cellular death, as revealed by colorimetric measurements and production of reactive oxygen species. We also demonstrated that sesamin acted by rescuing tyrosine hydroxylase levels from MPP(+)-induced depletion. Sesamin, however, did not modulate dopamine transporter levels, and estrogen receptor-alpha and -beta protein expression. By examining several parameters of cell distress, we found that sesamin also elicited a strong increase in superoxide dismutase activity as well as protein expression and decreased catalase activity and the MPP(+) stimulated inducible nitric oxide synthase protein expression, in neuronal PC12 cells. Finally, sesamin possessed significant anti-inflammatory properties, as disclosed by its potential to reduce MPP(+)-induced interleukin-6 mRNA levels in microglia. From these studies, we determined the importance of the lignan sesamin as a neuroprotective molecule and its possible role in complementary and/or preventive therapies of neurodegenerative diseases.
PubMed: 19794909
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pubmed:19794909Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Sesamin modulates tyrosine hydroxylase, superoxide dismutase, catalase, inducible NO synthase and interleukin-6 expression in dopaminergic cells under MPP+-induced oxidative stress.</title><author><name sortKey="Lahaie Collins, Vicky" sort="Lahaie Collins, Vicky" uniqKey="Lahaie Collins V" first="Vicky" last="Lahaie-Collins">Vicky Lahaie-Collins</name><affiliation><nlm:affiliation>Department of Biochemistry, Neuroscience Research Group, Université du Québec, Trois-Rivières, Québec, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Bournival, Julie" sort="Bournival, Julie" uniqKey="Bournival J" first="Julie" last="Bournival">Julie Bournival</name></author><author><name sortKey="Plouffe, Marilyn" sort="Plouffe, Marilyn" uniqKey="Plouffe M" first="Marilyn" last="Plouffe">Marilyn Plouffe</name></author><author><name sortKey="Carange, Julie" sort="Carange, Julie" uniqKey="Carange J" first="Julie" last="Carange">Julie Carange</name></author><author><name sortKey="Martinoli, Maria Grazia" sort="Martinoli, Maria Grazia" uniqKey="Martinoli M" first="Maria-Grazia" last="Martinoli">Maria-Grazia Martinoli</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="????"><PubDate><MedlineDate>2008 Oct-Dec</MedlineDate></PubDate></date><idno type="RBID">pubmed:19794909</idno><idno type="pmid">19794909</idno><idno type="wicri:Area/PubMed/Corpus">000F45</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000F45</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Sesamin modulates tyrosine hydroxylase, superoxide dismutase, catalase, inducible NO synthase and interleukin-6 expression in dopaminergic cells under MPP+-induced oxidative stress.</title><author><name sortKey="Lahaie Collins, Vicky" sort="Lahaie Collins, Vicky" uniqKey="Lahaie Collins V" first="Vicky" last="Lahaie-Collins">Vicky Lahaie-Collins</name><affiliation><nlm:affiliation>Department of Biochemistry, Neuroscience Research Group, Université du Québec, Trois-Rivières, Québec, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Bournival, Julie" sort="Bournival, Julie" uniqKey="Bournival J" first="Julie" last="Bournival">Julie Bournival</name></author><author><name sortKey="Plouffe, Marilyn" sort="Plouffe, Marilyn" uniqKey="Plouffe M" first="Marilyn" last="Plouffe">Marilyn Plouffe</name></author><author><name sortKey="Carange, Julie" sort="Carange, Julie" uniqKey="Carange J" first="Julie" last="Carange">Julie Carange</name></author><author><name sortKey="Martinoli, Maria Grazia" sort="Martinoli, Maria Grazia" uniqKey="Martinoli M" first="Maria-Grazia" last="Martinoli">Maria-Grazia Martinoli</name></author></analytic><series><title level="j">Oxidative medicine and cellular longevity</title><idno type="eISSN">1942-0994</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>1-Methyl-4-phenylpyridinium (pharmacology)</term><term>Animals</term><term>Antioxidants (pharmacology)</term><term>Catalase (biosynthesis)</term><term>Catalase (metabolism)</term><term>Dioxoles (pharmacology)</term><term>Dopamine (metabolism)</term><term>Dopamine Plasma Membrane Transport Proteins (metabolism)</term><term>Interleukin-6 (biosynthesis)</term><term>Interleukin-6 (metabolism)</term><term>Lignans (pharmacology)</term><term>Neurons (drug effects)</term><term>Neurons (enzymology)</term><term>Neurons (metabolism)</term><term>Nitric Oxide Synthase Type II (biosynthesis)</term><term>Nitric Oxide Synthase Type II (metabolism)</term><term>Oxidative Stress (drug effects)</term><term>Oxidative Stress (physiology)</term><term>PC12 Cells</term><term>Rats</term><term>Reactive Oxygen Species (metabolism)</term><term>Superoxide Dismutase (biosynthesis)</term><term>Superoxide Dismutase (metabolism)</term><term>Tyrosine 3-Monooxygenase (biosynthesis)</term><term>Tyrosine 3-Monooxygenase (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Catalase</term><term>Interleukin-6</term><term>Nitric Oxide Synthase Type II</term><term>Superoxide Dismutase</term><term>Tyrosine 3-Monooxygenase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Catalase</term><term>Dopamine</term><term>Dopamine Plasma Membrane Transport Proteins</term><term>Interleukin-6</term><term>Nitric Oxide Synthase Type II</term><term>Reactive Oxygen Species</term><term>Superoxide Dismutase</term><term>Tyrosine 3-Monooxygenase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>1-Methyl-4-phenylpyridinium</term><term>Antioxidants</term><term>Dioxoles</term><term>Lignans</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Neurons</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Neurons</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Neurons</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Oxidative Stress</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>PC12 Cells</term><term>Rats</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Oxidative stress is regarded as a mediator of nerve cell death in several neurodegenerative disorders, such as Parkinson's disease. Sesamin, a lignan mainly found in sesame oil, is currently under study for its anti-oxidative and possible neuroprotective properties. We used 1-methyl-4-phenyl-pyridine (MPP(+)) ion, the active metabolite of the potent parkinsonism-causing toxin 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine, to produce oxidative stress and neurodegeneration in neuronal PC12 cells, which express dopamine, as well as neurofilaments. Our results show that picomolar doses of sesamin protected neuronal PC12 cells from MPP(+)-induced cellular death, as revealed by colorimetric measurements and production of reactive oxygen species. We also demonstrated that sesamin acted by rescuing tyrosine hydroxylase levels from MPP(+)-induced depletion. Sesamin, however, did not modulate dopamine transporter levels, and estrogen receptor-alpha and -beta protein expression. By examining several parameters of cell distress, we found that sesamin also elicited a strong increase in superoxide dismutase activity as well as protein expression and decreased catalase activity and the MPP(+) stimulated inducible nitric oxide synthase protein expression, in neuronal PC12 cells. Finally, sesamin possessed significant anti-inflammatory properties, as disclosed by its potential to reduce MPP(+)-induced interleukin-6 mRNA levels in microglia. From these studies, we determined the importance of the lignan sesamin as a neuroprotective molecule and its possible role in complementary and/or preventive therapies of neurodegenerative diseases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19794909</PMID><DateCreated><Year>2009</Year><Month>10</Month><Day>01</Day></DateCreated><DateCompleted><Year>2011</Year><Month>01</Month><Day>28</Day></DateCompleted><DateRevised><Year>2016</Year><Month>03</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1942-0994</ISSN><JournalIssue CitedMedium="Internet"><Volume>1</Volume><Issue>1</Issue><PubDate><MedlineDate>2008 Oct-Dec</MedlineDate></PubDate></JournalIssue><Title>Oxidative medicine and cellular longevity</Title><ISOAbbreviation>Oxid Med Cell Longev</ISOAbbreviation></Journal><ArticleTitle>Sesamin modulates tyrosine hydroxylase, superoxide dismutase, catalase, inducible NO synthase and interleukin-6 expression in dopaminergic cells under MPP+-induced oxidative stress.</ArticleTitle><Pagination><MedlinePgn>54-62</MedlinePgn></Pagination><Abstract><AbstractText>Oxidative stress is regarded as a mediator of nerve cell death in several neurodegenerative disorders, such as Parkinson's disease. Sesamin, a lignan mainly found in sesame oil, is currently under study for its anti-oxidative and possible neuroprotective properties. We used 1-methyl-4-phenyl-pyridine (MPP(+)) ion, the active metabolite of the potent parkinsonism-causing toxin 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine, to produce oxidative stress and neurodegeneration in neuronal PC12 cells, which express dopamine, as well as neurofilaments. Our results show that picomolar doses of sesamin protected neuronal PC12 cells from MPP(+)-induced cellular death, as revealed by colorimetric measurements and production of reactive oxygen species. We also demonstrated that sesamin acted by rescuing tyrosine hydroxylase levels from MPP(+)-induced depletion. Sesamin, however, did not modulate dopamine transporter levels, and estrogen receptor-alpha and -beta protein expression. By examining several parameters of cell distress, we found that sesamin also elicited a strong increase in superoxide dismutase activity as well as protein expression and decreased catalase activity and the MPP(+) stimulated inducible nitric oxide synthase protein expression, in neuronal PC12 cells. Finally, sesamin possessed significant anti-inflammatory properties, as disclosed by its potential to reduce MPP(+)-induced interleukin-6 mRNA levels in microglia. From these studies, we determined the importance of the lignan sesamin as a neuroprotective molecule and its possible role in complementary and/or preventive therapies of neurodegenerative diseases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lahaie-Collins</LastName><ForeName>Vicky</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Neuroscience Research Group, Université du Québec, Trois-Rivières, Québec, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bournival</LastName><ForeName>Julie</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Plouffe</LastName><ForeName>Marilyn</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Carange</LastName><ForeName>Julie</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Martinoli</LastName><ForeName>Maria-Grazia</ForeName><Initials>MG</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Oxid Med Cell Longev</MedlineTA><NlmUniqueID>101479826</NlmUniqueID><ISSNLinking>1942-0994</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000975">Antioxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004149">Dioxoles</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050483">Dopamine Plasma Membrane Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015850">Interleukin-6</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017705">Lignans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017382">Reactive Oxygen Species</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.6</RegistryNumber><NameOfSubstance UI="D002374">Catalase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.13.39</RegistryNumber><NameOfSubstance UI="D052247">Nitric Oxide Synthase Type II</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.16.2</RegistryNumber><NameOfSubstance UI="D014446">Tyrosine 3-Monooxygenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.15.1.1</RegistryNumber><NameOfSubstance UI="D013482">Superoxide Dismutase</NameOfSubstance></Chemical><Chemical><RegistryNumber>R865A5OY8J</RegistryNumber><NameOfSubstance 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