Current status of tyrosine hydroxylase in management of Parkinson's disease.
Identifieur interne : 000862 ( PubMed/Corpus ); précédent : 000861; suivant : 000863Current status of tyrosine hydroxylase in management of Parkinson's disease.
Auteurs : Annaik Petithomme FeveSource :
- CNS & neurological disorders drug targets [ 1996-3181 ] ; 2012.
English descriptors
- KwdEn :
- Animals, Antiparkinson Agents (therapeutic use), Dopamine (metabolism), Gene Expression Regulation, Humans, Parkinson Disease (enzymology), Parkinson Disease (genetics), Parkinson Disease (physiopathology), Parkinson Disease (therapy), Tyrosine 3-Monooxygenase (genetics), Tyrosine 3-Monooxygenase (metabolism), alpha-Synuclein (genetics), alpha-Synuclein (metabolism).
- MESH :
- chemical , genetics : Tyrosine 3-Monooxygenase, alpha-Synuclein.
- chemical , metabolism : Dopamine, Tyrosine 3-Monooxygenase, alpha-Synuclein.
- chemical , therapeutic use : Antiparkinson Agents.
- enzymology : Parkinson Disease.
- genetics : Parkinson Disease.
- physiopathology : Parkinson Disease.
- therapy : Parkinson Disease.
- Animals, Gene Expression Regulation, Humans.
Abstract
Tyrosine hydroxylase (TH) is the rate limiting enzyme responsible for converting tyrosine to L-DOPA in the dopamine synthesis pathway. The pathophysiology of Parkinson's disease (PD) is largely due to the nigrostriatal dopaminergic system, with a decrease in TH activity, TH synthesis and TH mRNA in the striatum of PD and animal experimental models. TH is thus one of the main targets for gene therapy in PD. TH activity variations during L-DOPA and new antiparkinsonian treatments have been extensively studied. Pharmacological trials with neuroprotective treatments could modify these variations, suggesting a direct involvement of TH cells in the neurodegenerative process. α- Synuclein, the main component of Lewy bodies regulates the production of dopamine through its interaction with TH. Over-expression of α-synuclein reduces the levels of TH mRNA and protein in the brain and in this way links the histological description of PD and its pathological biochemistry.
PubMed: 22583428
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pubmed:22583428Le document en format XML
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The pathophysiology of Parkinson's disease (PD) is largely due to the nigrostriatal dopaminergic system, with a decrease in TH activity, TH synthesis and TH mRNA in the striatum of PD and animal experimental models. TH is thus one of the main targets for gene therapy in PD. TH activity variations during L-DOPA and new antiparkinsonian treatments have been extensively studied. Pharmacological trials with neuroprotective treatments could modify these variations, suggesting a direct involvement of TH cells in the neurodegenerative process. α- Synuclein, the main component of Lewy bodies regulates the production of dopamine through its interaction with TH. Over-expression of α-synuclein reduces the levels of TH mRNA and protein in the brain and in this way links the histological description of PD and its pathological biochemistry.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22583428</PMID><DateCreated><Year>2012</Year><Month>06</Month><Day>25</Day></DateCreated><DateCompleted><Year>2012</Year><Month>12</Month><Day>03</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1996-3181</ISSN><JournalIssue CitedMedium="Internet"><Volume>11</Volume><Issue>4</Issue><PubDate><Year>2012</Year><Month>Jun</Month><Day>01</Day></PubDate></JournalIssue><Title>CNS & neurological disorders drug targets</Title><ISOAbbreviation>CNS Neurol Disord Drug Targets</ISOAbbreviation></Journal><ArticleTitle>Current status of tyrosine hydroxylase in management of Parkinson's disease.</ArticleTitle><Pagination><MedlinePgn>450-5</MedlinePgn></Pagination><Abstract><AbstractText>Tyrosine hydroxylase (TH) is the rate limiting enzyme responsible for converting tyrosine to L-DOPA in the dopamine synthesis pathway. 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Over-expression of α-synuclein reduces the levels of TH mRNA and protein in the brain and in this way links the histological description of PD and its pathological biochemistry.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Feve</LastName><ForeName>Annaik Petithomme</ForeName><Initials>AP</Initials><AffiliationInfo><Affiliation>Neurology Department, Parkinson Unit, Leopold Bellan Hospital, Paris, France. afeve@aol.com</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United Arab Emirates</Country><MedlineTA>CNS Neurol Disord Drug Targets</MedlineTA><NlmUniqueID>101269155</NlmUniqueID><ISSNLinking>1871-5273</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000978">Antiparkinson Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.16.2</RegistryNumber><NameOfSubstance UI="D014446">Tyrosine 3-Monooxygenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>VTD58H1Z2X</RegistryNumber><NameOfSubstance UI="D004298">Dopamine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000978" MajorTopicYN="N">Antiparkinson Agents</DescriptorName><QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004298" MajorTopicYN="N">Dopamine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005786" MajorTopicYN="N">Gene Expression Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000503" MajorTopicYN="Y">physiopathology</QualifierName><QualifierName UI="Q000628" MajorTopicYN="N">therapy</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014446" MajorTopicYN="N">Tyrosine 3-Monooxygenase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>02</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>04</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>04</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>5</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>5</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>12</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22583428</ArticleId><ArticleId IdType="pii">CDTCNSND-EPUB-20120511-1</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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