Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress.
Identifieur interne : 000F96 ( Main/Exploration ); précédent : 000F95; suivant : 000F97Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress.
Auteurs : Chad R. Borges [États-Unis] ; Timothy Geddes ; J Throck Watson ; Donald M. KuhnSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2002.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Données de séquences moléculaires (MeSH), Dopamine (biosynthèse), Glutathion (métabolisme), RT-PCR (MeSH), Rats (MeSH), Spectrométrie de masse MALDI (MeSH), Stress oxydatif (MeSH), Séquence d'acides aminés (MeSH), Tyrosine 3-monooxygenase (antagonistes et inhibiteurs), Tétraméthyl-diazènedicarboxamide (pharmacologie).
- MESH :
- antagonistes et inhibiteurs : Tyrosine 3-monooxygenase.
- biosynthèse : Dopamine.
- métabolisme : Glutathion.
- pharmacologie : Tétraméthyl-diazènedicarboxamide.
- Animaux, Données de séquences moléculaires, RT-PCR, Rats, Spectrométrie de masse MALDI, Stress oxydatif, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Diamide (pharmacology), Dopamine (biosynthesis), Glutathione (metabolism), Molecular Sequence Data (MeSH), Oxidative Stress (MeSH), Rats (MeSH), Reverse Transcriptase Polymerase Chain Reaction (MeSH), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH), Tyrosine 3-Monooxygenase (antagonists & inhibitors).
- MESH :
- chemical , antagonists & inhibitors : Tyrosine 3-Monooxygenase.
- chemical , biosynthesis : Dopamine.
- chemical , metabolism : Glutathione.
- chemical , pharmacology : Diamide.
- Amino Acid Sequence, Animals, Molecular Sequence Data, Oxidative Stress, Rats, Reverse Transcriptase Polymerase Chain Reaction, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.
Abstract
Tyrosine hydroxylase (TH), the initial and rate-limiting enzyme in the biosynthesis of the neurotransmitter dopamine, is inhibited by the sulfhydryl oxidant diamide in a concentration-dependent manner. The inhibitory effect of diamide on TH catalytic activity is enhanced significantly by GSH. Treatment of TH with diamide in the presence of [(35)S]GSH results in the incorporation of (35)S into the enzyme. The effect of diamide-GSH on TH activity is prevented by dithiothreitol (DTT), as is the binding of [(35)S]GSH, indicating the formation of a disulfide linkage between GSH and TH protein cysteinyls. Loss of TH catalytic activity caused by diamide-GSH is partially recovered by DTT and glutaredoxin, whereas the disulfide linkage of GSH with TH is completely reversed by both. Treatment of intact PC12 cells with diamide results in a concentration-dependent inhibition of TH activity. Incubation of cells with [(35)S]cysteine, to label cellular GSH prior to diamide treatment, followed by immunoprecipitation of TH shows that the loss of TH catalytic activity is associated with a DTT-reversible incorporation of [(35)S]GSH into the enzyme. A combination of matrix-assisted laser desorption/ionization/mass spectrometry and liquid chromatography/tandem mass spectrometry was used to identify the sites of S-glutathionylation in TH. Six cysteines (177, 249, 263, 329, 330, and 380) of the seven cysteine residues in TH were confirmed as substrates for modification. Only Cys-311 was not S-glutathionylated. These results establish that TH activity is influenced in a reversible manner by S-glutathionylation and suggest that cellular GSH may regulate dopamine biosynthesis under conditions of oxidative stress or drug-induced toxicity.
DOI: 10.1074/jbc.M209042200
PubMed: 12376535
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress.</title><author><name sortKey="Borges, Chad R" sort="Borges, Chad R" uniqKey="Borges C" first="Chad R" last="Borges">Chad R. Borges</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, Michigan State University, East Lansing 48824</wicri:regionArea><orgName type="university">Université d'État du Michigan</orgName><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="Geddes, Timothy" sort="Geddes, Timothy" uniqKey="Geddes T" first="Timothy" last="Geddes">Timothy Geddes</name></author><author><name sortKey="Watson, J Throck" sort="Watson, J Throck" uniqKey="Watson J" first="J Throck" last="Watson">J Throck Watson</name></author><author><name sortKey="Kuhn, Donald M" sort="Kuhn, Donald M" uniqKey="Kuhn D" first="Donald M" last="Kuhn">Donald M. Kuhn</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:12376535</idno><idno type="pmid">12376535</idno><idno type="doi">10.1074/jbc.M209042200</idno><idno type="wicri:Area/Main/Corpus">000F63</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000F63</idno><idno type="wicri:Area/Main/Curation">000F63</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000F63</idno><idno type="wicri:Area/Main/Exploration">000F63</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress.</title><author><name sortKey="Borges, Chad R" sort="Borges, Chad R" uniqKey="Borges C" first="Chad R" last="Borges">Chad R. Borges</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, Michigan State University, East Lansing 48824</wicri:regionArea><orgName type="university">Université d'État du Michigan</orgName><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="Geddes, Timothy" sort="Geddes, Timothy" uniqKey="Geddes T" first="Timothy" last="Geddes">Timothy Geddes</name></author><author><name sortKey="Watson, J Throck" sort="Watson, J Throck" uniqKey="Watson J" first="J Throck" last="Watson">J Throck Watson</name></author><author><name sortKey="Kuhn, Donald M" sort="Kuhn, Donald M" uniqKey="Kuhn D" first="Donald M" last="Kuhn">Donald M. Kuhn</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Diamide (pharmacology)</term><term>Dopamine (biosynthesis)</term><term>Glutathione (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Rats (MeSH)</term><term>Reverse Transcriptase Polymerase Chain Reaction (MeSH)</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH)</term><term>Tyrosine 3-Monooxygenase (antagonists & inhibitors)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Dopamine (biosynthèse)</term><term>Glutathion (métabolisme)</term><term>RT-PCR (MeSH)</term><term>Rats (MeSH)</term><term>Spectrométrie de masse MALDI (MeSH)</term><term>Stress oxydatif (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Tyrosine 3-monooxygenase (antagonistes et inhibiteurs)</term><term>Tétraméthyl-diazènedicarboxamide (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Tyrosine 3-Monooxygenase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Dopamine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Diamide</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Tyrosine 3-monooxygenase</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Dopamine</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Tétraméthyl-diazènedicarboxamide</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Molecular Sequence Data</term><term>Oxidative Stress</term><term>Rats</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Données de séquences moléculaires</term><term>RT-PCR</term><term>Rats</term><term>Spectrométrie de masse MALDI</term><term>Stress oxydatif</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Tyrosine hydroxylase (TH), the initial and rate-limiting enzyme in the biosynthesis of the neurotransmitter dopamine, is inhibited by the sulfhydryl oxidant diamide in a concentration-dependent manner. The inhibitory effect of diamide on TH catalytic activity is enhanced significantly by GSH. Treatment of TH with diamide in the presence of [(35)S]GSH results in the incorporation of (35)S into the enzyme. The effect of diamide-GSH on TH activity is prevented by dithiothreitol (DTT), as is the binding of [(35)S]GSH, indicating the formation of a disulfide linkage between GSH and TH protein cysteinyls. Loss of TH catalytic activity caused by diamide-GSH is partially recovered by DTT and glutaredoxin, whereas the disulfide linkage of GSH with TH is completely reversed by both. Treatment of intact PC12 cells with diamide results in a concentration-dependent inhibition of TH activity. Incubation of cells with [(35)S]cysteine, to label cellular GSH prior to diamide treatment, followed by immunoprecipitation of TH shows that the loss of TH catalytic activity is associated with a DTT-reversible incorporation of [(35)S]GSH into the enzyme. A combination of matrix-assisted laser desorption/ionization/mass spectrometry and liquid chromatography/tandem mass spectrometry was used to identify the sites of S-glutathionylation in TH. Six cysteines (177, 249, 263, 329, 330, and 380) of the seven cysteine residues in TH were confirmed as substrates for modification. Only Cys-311 was not S-glutathionylated. These results establish that TH activity is influenced in a reversible manner by S-glutathionylation and suggest that cellular GSH may regulate dopamine biosynthesis under conditions of oxidative stress or drug-induced toxicity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12376535</PMID><DateCompleted><Year>2003</Year><Month>01</Month><Day>28</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>277</Volume><Issue>50</Issue><PubDate><Year>2002</Year><Month>Dec</Month><Day>13</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress.</ArticleTitle><Pagination><MedlinePgn>48295-302</MedlinePgn></Pagination><Abstract><AbstractText>Tyrosine hydroxylase (TH), the initial and rate-limiting enzyme in the biosynthesis of the neurotransmitter dopamine, is inhibited by the sulfhydryl oxidant diamide in a concentration-dependent manner. The inhibitory effect of diamide on TH catalytic activity is enhanced significantly by GSH. Treatment of TH with diamide in the presence of [(35)S]GSH results in the incorporation of (35)S into the enzyme. The effect of diamide-GSH on TH activity is prevented by dithiothreitol (DTT), as is the binding of [(35)S]GSH, indicating the formation of a disulfide linkage between GSH and TH protein cysteinyls. Loss of TH catalytic activity caused by diamide-GSH is partially recovered by DTT and glutaredoxin, whereas the disulfide linkage of GSH with TH is completely reversed by both. Treatment of intact PC12 cells with diamide results in a concentration-dependent inhibition of TH activity. Incubation of cells with [(35)S]cysteine, to label cellular GSH prior to diamide treatment, followed by immunoprecipitation of TH shows that the loss of TH catalytic activity is associated with a DTT-reversible incorporation of [(35)S]GSH into the enzyme. A combination of matrix-assisted laser desorption/ionization/mass spectrometry and liquid chromatography/tandem mass spectrometry was used to identify the sites of S-glutathionylation in TH. Six cysteines (177, 249, 263, 329, 330, and 380) of the seven cysteine residues in TH were confirmed as substrates for modification. Only Cys-311 was not S-glutathionylated. These results establish that TH activity is influenced in a reversible manner by S-glutathionylation and suggest that cellular GSH may regulate dopamine biosynthesis under conditions of oxidative stress or drug-induced toxicity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Borges</LastName><ForeName>Chad R</ForeName><Initials>CR</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Geddes</LastName><ForeName>Timothy</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Watson</LastName><ForeName>J Throck</ForeName><Initials>JT</Initials></Author><Author ValidYN="Y"><LastName>Kuhn</LastName><ForeName>Donald M</ForeName><Initials>DM</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>DA10756</GrantID><Acronym>DA</Acronym><Agency>NIDA NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2002</Year><Month>10</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>10465-78-8</RegistryNumber><NameOfSubstance UI="D003958">Diamide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.16.2</RegistryNumber><NameOfSubstance UI="D014446">Tyrosine 3-Monooxygenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>VTD58H1Z2X</RegistryNumber><NameOfSubstance UI="D004298">Dopamine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>J Biol Chem. 2003 Jan 31;278(5):3407</RefSource></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003958" MajorTopicYN="N">Diamide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004298" MajorTopicYN="N">Dopamine</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="Y">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020133" MajorTopicYN="N">Reverse Transcriptase Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019032" MajorTopicYN="N">Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014446" MajorTopicYN="N">Tyrosine 3-Monooxygenase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>10</Month><Day>12</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>1</Month><Day>29</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>10</Month><Day>12</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12376535</ArticleId><ArticleId IdType="doi">10.1074/jbc.M209042200</ArticleId><ArticleId IdType="pii">M209042200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li></region><settlement><li>East Lansing</li></settlement><orgName><li>Université d'État du Michigan</li></orgName></list><tree><noCountry><name sortKey="Geddes, Timothy" sort="Geddes, Timothy" uniqKey="Geddes T" first="Timothy" last="Geddes">Timothy Geddes</name><name sortKey="Kuhn, Donald M" sort="Kuhn, Donald M" uniqKey="Kuhn D" first="Donald M" last="Kuhn">Donald M. Kuhn</name><name sortKey="Watson, J Throck" sort="Watson, J Throck" uniqKey="Watson J" first="J Throck" last="Watson">J Throck Watson</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Borges, Chad R" sort="Borges, Chad R" uniqKey="Borges C" first="Chad R" last="Borges">Chad R. Borges</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000F96 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000F96 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= GlutaredoxinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:12376535
|texte= Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:12376535" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |