Genetic iron chelation protects against proteasome inhibition-induced dopamine neuron degeneration.
Identifieur interne : 000105 ( PubMed/Corpus ); précédent : 000104; suivant : 000106Genetic iron chelation protects against proteasome inhibition-induced dopamine neuron degeneration.
Auteurs : Wen Zhu ; Xuping Li ; Wenjie Xie ; Feifei Luo ; Deepinder Kaur ; Julie. Andersen ; Joseph Jankovic ; Weidong LeSource :
- Neurobiology of disease ; 2010.
English descriptors
- KwdEn :
- Acetylcysteine (analogs & derivatives), Acetylcysteine (pharmacology), Animals, Apoferritins (genetics), Cation Transport Proteins (metabolism), Chelation Therapy (methods), Corpus Striatum (metabolism), Corpus Striatum (physiopathology), Cysteine Proteinase Inhibitors (pharmacology), Cytoprotection (genetics), Dopamine (metabolism), Gene Expression Regulation (genetics), Genetic Therapy (methods), Iron Metabolism Disorders (genetics), Iron Metabolism Disorders (metabolism), Iron Metabolism Disorders (therapy), Mice, Mice, Transgenic, Nerve Degeneration (genetics), Nerve Degeneration (metabolism), Nerve Degeneration (therapy), Neurons (metabolism), Parkinson Disease (genetics), Parkinson Disease (metabolism), Parkinson Disease (therapy), Proteasome Endopeptidase Complex (metabolism), Proteasome Inhibitors, Substantia Nigra (metabolism), Substantia Nigra (physiopathology).
- MESH :
- chemical , analogs & derivatives : Acetylcysteine.
- chemical , genetics : Apoferritins.
- chemical , metabolism : Cation Transport Proteins, Dopamine, Proteasome Endopeptidase Complex.
- chemical , pharmacology : Acetylcysteine, Cysteine Proteinase Inhibitors.
- genetics : Cytoprotection, Gene Expression Regulation, Iron Metabolism Disorders, Nerve Degeneration, Parkinson Disease.
- metabolism : Corpus Striatum, Iron Metabolism Disorders, Nerve Degeneration, Neurons, Parkinson Disease, Substantia Nigra.
- methods : Chelation Therapy, Genetic Therapy.
- physiopathology : Corpus Striatum, Substantia Nigra.
- therapy : Iron Metabolism Disorders, Nerve Degeneration, Parkinson Disease.
- Animals, Mice, Mice, Transgenic, Proteasome Inhibitors.
Abstract
Impairment of the ubiquitin proteasome system (UPS) and iron accumulation in the substantia nigra (SN) have both been implicated in the pathogenesis of Parkinson's disease (PD). We previously reported that chemical iron chelation can protect against proteasome inhibitor lactacystin-induced dopamine (DA) neurodegeneration in vivo. Here, we tested potential neuroprotection via genetic expression of the iron chelator human ferritin heavy chain (H-ferritin). We found that overexpression of H-ferritin in DA neurons significantly reduced lactacystin-induced nigral DA neuron loss and striatal DA depletion. Overexpression of H-ferritin also attenuated elevated levels of total and ferrous iron as well as the divalent metal ion transporter 1 (DMT1) in the SN following lactacystin treatment. In addition, overexpression of H-ferritin alleviated the inhibitory effects of lactacystin on proteasome activity in the nigral tissues. These results suggest that H-ferritin exerts neuroprotection possibly by modulating iron homeostasis and restoring proteasome activity.
DOI: 10.1016/j.nbd.2009.09.024
PubMed: 19818853
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pubmed:19818853Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Genetic iron chelation protects against proteasome inhibition-induced dopamine neuron degeneration.</title><author><name sortKey="Zhu, Wen" sort="Zhu, Wen" uniqKey="Zhu W" first="Wen" last="Zhu">Wen Zhu</name><affiliation><nlm:affiliation>Department of Neurology, NB 205, Baylor College of Medicine, Houston, TX 77030, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Li, Xuping" sort="Li, Xuping" uniqKey="Li X" first="Xuping" last="Li">Xuping Li</name></author><author><name sortKey="Xie, Wenjie" sort="Xie, Wenjie" uniqKey="Xie W" first="Wenjie" last="Xie">Wenjie Xie</name></author><author><name sortKey="Luo, Feifei" sort="Luo, Feifei" uniqKey="Luo F" first="Feifei" last="Luo">Feifei Luo</name></author><author><name sortKey="Kaur, Deepinder" sort="Kaur, Deepinder" uniqKey="Kaur D" first="Deepinder" last="Kaur">Deepinder Kaur</name></author><author><name sortKey="Andersen, Julie K" sort="Andersen, Julie K" uniqKey="Andersen J" first="Julie" last="Andersen">Julie. Andersen</name></author><author><name sortKey="Jankovic, Joseph" sort="Jankovic, Joseph" uniqKey="Jankovic J" first="Joseph" last="Jankovic">Joseph Jankovic</name></author><author><name sortKey="Le, Weidong" sort="Le, Weidong" uniqKey="Le W" first="Weidong" last="Le">Weidong Le</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="doi">10.1016/j.nbd.2009.09.024</idno><idno type="RBID">pubmed:19818853</idno><idno type="pmid">19818853</idno><idno type="wicri:Area/PubMed/Corpus">000105</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Genetic iron chelation protects against proteasome inhibition-induced dopamine neuron degeneration.</title><author><name sortKey="Zhu, Wen" sort="Zhu, Wen" uniqKey="Zhu W" first="Wen" last="Zhu">Wen Zhu</name><affiliation><nlm:affiliation>Department of Neurology, NB 205, Baylor College of Medicine, Houston, TX 77030, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Li, Xuping" sort="Li, Xuping" uniqKey="Li X" first="Xuping" last="Li">Xuping Li</name></author><author><name sortKey="Xie, Wenjie" sort="Xie, Wenjie" uniqKey="Xie W" first="Wenjie" last="Xie">Wenjie Xie</name></author><author><name sortKey="Luo, Feifei" sort="Luo, Feifei" uniqKey="Luo F" first="Feifei" last="Luo">Feifei Luo</name></author><author><name sortKey="Kaur, Deepinder" sort="Kaur, Deepinder" uniqKey="Kaur D" first="Deepinder" last="Kaur">Deepinder Kaur</name></author><author><name sortKey="Andersen, Julie K" sort="Andersen, Julie K" uniqKey="Andersen J" first="Julie" last="Andersen">Julie. Andersen</name></author><author><name sortKey="Jankovic, Joseph" sort="Jankovic, Joseph" uniqKey="Jankovic J" first="Joseph" last="Jankovic">Joseph Jankovic</name></author><author><name sortKey="Le, Weidong" sort="Le, Weidong" uniqKey="Le W" first="Weidong" last="Le">Weidong Le</name></author></analytic><series><title level="j">Neurobiology of disease</title><idno type="e-ISSN">1095-953X</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetylcysteine (analogs & derivatives)</term><term>Acetylcysteine (pharmacology)</term><term>Animals</term><term>Apoferritins (genetics)</term><term>Cation Transport Proteins (metabolism)</term><term>Chelation Therapy (methods)</term><term>Corpus Striatum (metabolism)</term><term>Corpus Striatum (physiopathology)</term><term>Cysteine Proteinase Inhibitors (pharmacology)</term><term>Cytoprotection (genetics)</term><term>Dopamine (metabolism)</term><term>Gene Expression Regulation (genetics)</term><term>Genetic Therapy (methods)</term><term>Iron Metabolism Disorders (genetics)</term><term>Iron Metabolism Disorders (metabolism)</term><term>Iron Metabolism Disorders (therapy)</term><term>Mice</term><term>Mice, Transgenic</term><term>Nerve Degeneration (genetics)</term><term>Nerve Degeneration (metabolism)</term><term>Nerve Degeneration (therapy)</term><term>Neurons (metabolism)</term><term>Parkinson Disease (genetics)</term><term>Parkinson Disease (metabolism)</term><term>Parkinson Disease (therapy)</term><term>Proteasome Endopeptidase Complex (metabolism)</term><term>Proteasome Inhibitors</term><term>Substantia Nigra (metabolism)</term><term>Substantia Nigra (physiopathology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Acetylcysteine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Apoferritins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cation Transport Proteins</term><term>Dopamine</term><term>Proteasome Endopeptidase Complex</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Acetylcysteine</term><term>Cysteine Proteinase Inhibitors</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Cytoprotection</term><term>Gene Expression Regulation</term><term>Iron Metabolism Disorders</term><term>Nerve Degeneration</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Corpus Striatum</term><term>Iron Metabolism Disorders</term><term>Nerve Degeneration</term><term>Neurons</term><term>Parkinson Disease</term><term>Substantia Nigra</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Chelation Therapy</term><term>Genetic Therapy</term></keywords><keywords scheme="MESH" qualifier="physiopathology" xml:lang="en"><term>Corpus Striatum</term><term>Substantia Nigra</term></keywords><keywords scheme="MESH" qualifier="therapy" xml:lang="en"><term>Iron Metabolism Disorders</term><term>Nerve Degeneration</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Mice</term><term>Mice, Transgenic</term><term>Proteasome Inhibitors</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Impairment of the ubiquitin proteasome system (UPS) and iron accumulation in the substantia nigra (SN) have both been implicated in the pathogenesis of Parkinson's disease (PD). We previously reported that chemical iron chelation can protect against proteasome inhibitor lactacystin-induced dopamine (DA) neurodegeneration in vivo. Here, we tested potential neuroprotection via genetic expression of the iron chelator human ferritin heavy chain (H-ferritin). We found that overexpression of H-ferritin in DA neurons significantly reduced lactacystin-induced nigral DA neuron loss and striatal DA depletion. Overexpression of H-ferritin also attenuated elevated levels of total and ferrous iron as well as the divalent metal ion transporter 1 (DMT1) in the SN following lactacystin treatment. In addition, overexpression of H-ferritin alleviated the inhibitory effects of lactacystin on proteasome activity in the nigral tissues. These results suggest that H-ferritin exerts neuroprotection possibly by modulating iron homeostasis and restoring proteasome activity.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">19818853</PMID><DateCreated><Year>2010</Year><Month>02</Month><Day>03</Day></DateCreated><DateCompleted><Year>2010</Year><Month>06</Month><Day>15</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1095-953X</ISSN><JournalIssue CitedMedium="Internet"><Volume>37</Volume><Issue>2</Issue><PubDate><Year>2010</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Neurobiology of disease</Title><ISOAbbreviation>Neurobiol. Dis.</ISOAbbreviation></Journal><ArticleTitle>Genetic iron chelation protects against proteasome inhibition-induced dopamine neuron degeneration.</ArticleTitle><Pagination><MedlinePgn>307-13</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.nbd.2009.09.024</ELocationID><Abstract><AbstractText>Impairment of the ubiquitin proteasome system (UPS) and iron accumulation in the substantia nigra (SN) have both been implicated in the pathogenesis of Parkinson's disease (PD). We previously reported that chemical iron chelation can protect against proteasome inhibitor lactacystin-induced dopamine (DA) neurodegeneration in vivo. Here, we tested potential neuroprotection via genetic expression of the iron chelator human ferritin heavy chain (H-ferritin). We found that overexpression of H-ferritin in DA neurons significantly reduced lactacystin-induced nigral DA neuron loss and striatal DA depletion. Overexpression of H-ferritin also attenuated elevated levels of total and ferrous iron as well as the divalent metal ion transporter 1 (DMT1) in the SN following lactacystin treatment. In addition, overexpression of H-ferritin alleviated the inhibitory effects of lactacystin on proteasome activity in the nigral tissues. These results suggest that H-ferritin exerts neuroprotection possibly by modulating iron homeostasis and restoring proteasome activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhu</LastName><ForeName>Wen</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Department of Neurology, NB 205, Baylor College of Medicine, Houston, TX 77030, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Xuping</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Xie</LastName><ForeName>Wenjie</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Luo</LastName><ForeName>Feifei</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Kaur</LastName><ForeName>Deepinder</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Andersen</LastName><ForeName>Julie K</ForeName><Initials>JK</Initials></Author><Author ValidYN="Y"><LastName>Jankovic</LastName><ForeName>Joseph</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Le</LastName><ForeName>Weidong</ForeName><Initials>W</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>NS41264</GrantID><Acronym>NS</Acronym><Agency>NINDS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>10</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Neurobiol Dis</MedlineTA><NlmUniqueID>9500169</NlmUniqueID><ISSNLinking>0969-9961</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D027682">Cation Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015853">Cysteine Proteinase Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D061988">Proteasome Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C436204">solute carrier family 11- (proton-coupled divalent metal ion transporters), member 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>133343-34-7</RegistryNumber><NameOfSubstance UI="C067713">lactacystin</NameOfSubstance></Chemical><Chemical><RegistryNumber>9013-31-4</RegistryNumber><NameOfSubstance UI="D001052">Apoferritins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.25.1</RegistryNumber><NameOfSubstance UI="D046988">Proteasome Endopeptidase Complex</NameOfSubstance></Chemical><Chemical><RegistryNumber>VTD58H1Z2X</RegistryNumber><NameOfSubstance UI="D004298">Dopamine</NameOfSubstance></Chemical><Chemical><RegistryNumber>WYQ7N0BPYC</RegistryNumber><NameOfSubstance UI="D000111">Acetylcysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N" UI="D000111">Acetylcysteine</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000031">analogs & derivatives</QualifierName><QualifierName MajorTopicYN="N" UI="Q000494">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D000818">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D001052">Apoferritins</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000235">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName 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