Glutaredoxin deficiency exacerbates neurodegeneration in C. elegans models of Parkinson's disease.
Identifieur interne : 000548 ( Main/Exploration ); précédent : 000547; suivant : 000549Glutaredoxin deficiency exacerbates neurodegeneration in C. elegans models of Parkinson's disease.
Auteurs : William M. Johnson ; Chen Yao [États-Unis] ; Sandra L. Siedlak [États-Unis] ; Wenzhang Wang [États-Unis] ; Xiongwei Zhu [États-Unis] ; Guy A. Caldwell [États-Unis] ; Amy L. Wilson-Delfosse ; John J. Mieyal [États-Unis] ; Shu G. Chen [États-Unis]Source :
- Human molecular genetics [ 1460-2083 ] ; 2015.
Descripteurs français
- KwdFr :
- ARN messager (génétique), ARN messager (métabolisme), Animaux (MeSH), Caenorhabditis elegans (génétique), Cystéine (métabolisme), Glutarédoxines (déficit), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Homéostasie (MeSH), Humains (MeSH), Leucine-rich repeat serine-threonine protein kinase-2 (MeSH), Maladie de Parkinson (génétique), Modèles animaux de maladie humaine (MeSH), Mésencéphale (métabolisme), Neurones dopaminergiques (métabolisme), Phénotype (MeSH), Protein-Serine-Threonine Kinases (génétique), Protein-Serine-Threonine Kinases (métabolisme), Protéines d'helminthes (génétique), Protéines d'helminthes (métabolisme), Régulation de l'expression des gènes (MeSH), Stress oxydatif (MeSH), Survie cellulaire (MeSH), Tyrosine 3-monooxygenase (génétique), Tyrosine 3-monooxygenase (métabolisme), alpha-Synucléine (génétique), alpha-Synucléine (métabolisme), Évolution moléculaire (MeSH).
- MESH :
- déficit : Glutarédoxines.
- génétique : ARN messager, Caenorhabditis elegans, Glutarédoxines, Maladie de Parkinson, Protein-Serine-Threonine Kinases, Protéines d'helminthes, Tyrosine 3-monooxygenase, alpha-Synucléine.
- métabolisme : ARN messager, Cystéine, Glutarédoxines, Mésencéphale, Neurones dopaminergiques, Protein-Serine-Threonine Kinases, Protéines d'helminthes, Tyrosine 3-monooxygenase, alpha-Synucléine.
- Animaux, Homéostasie, Humains, Leucine-rich repeat serine-threonine protein kinase-2, Modèles animaux de maladie humaine, Phénotype, Régulation de l'expression des gènes, Stress oxydatif, Survie cellulaire, Évolution moléculaire.
English descriptors
- KwdEn :
- Animals (MeSH), Caenorhabditis elegans (genetics), Cell Survival (MeSH), Cysteine (metabolism), Disease Models, Animal (MeSH), Dopaminergic Neurons (metabolism), Evolution, Molecular (MeSH), Gene Expression Regulation (MeSH), Glutaredoxins (deficiency), Glutaredoxins (genetics), Glutaredoxins (metabolism), Helminth Proteins (genetics), Helminth Proteins (metabolism), Homeostasis (MeSH), Humans (MeSH), Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 (MeSH), Mesencephalon (metabolism), Oxidative Stress (MeSH), Parkinson Disease (genetics), Phenotype (MeSH), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), RNA, Messenger (genetics), RNA, Messenger (metabolism), Tyrosine 3-Monooxygenase (genetics), Tyrosine 3-Monooxygenase (metabolism), alpha-Synuclein (genetics), alpha-Synuclein (metabolism).
- MESH :
- chemical , deficiency : Glutaredoxins.
- chemical , genetics : Glutaredoxins, Helminth Proteins, Protein-Serine-Threonine Kinases, RNA, Messenger, Tyrosine 3-Monooxygenase, alpha-Synuclein.
- chemical , metabolism : Cysteine, Glutaredoxins, Helminth Proteins, Protein-Serine-Threonine Kinases, RNA, Messenger, Tyrosine 3-Monooxygenase, alpha-Synuclein.
- genetics : Caenorhabditis elegans, Parkinson Disease.
- metabolism : Dopaminergic Neurons, Mesencephalon.
- Animals, Cell Survival, Disease Models, Animal, Evolution, Molecular, Gene Expression Regulation, Homeostasis, Humans, Leucine-Rich Repeat Serine-Threonine Protein Kinase-2, Oxidative Stress, Phenotype.
Abstract
Parkinson's disease (PD) is characterized by selective degeneration of dopaminergic neurons. Although the etiology of PD remains incompletely understood, oxidative stress has been implicated as an important contributor in the development of PD. Oxidative stress can lead to oxidation and functional perturbation of proteins critical to neuronal survival. Glutaredoxin 1 (Grx1) is an evolutionally conserved antioxidant enzyme that repairs protein oxidation by reversing the oxidative modification of cysteine known as S-glutathionylation. We aimed to explore the regulatory role of Grx1 in PD. We first examined the levels of Grx1 in postmortem midbrain samples from PD patients, and observed that Grx1 content is decreased in PD, specifically within the dopaminergic neurons. We subsequently investigated the potential role of Grx1 deficiency in PD pathogenesis by examining the consequences of loss of the Caenorhabditis elegans Grx1 homolog in well-established worm models of familial PD caused by overexpression of pathogenic human LRRK2 mutants G2019S or R1441C. We found that loss of the Grx1 homolog led to significant exacerbation of the neurodegenerative phenotype in C. elegans overexpressing the human LRRK2 mutants. Re-expression in the dopaminergic neurons of the active, but not a catalytically inactive form of the Grx1 homolog rescued the exacerbated phenotype. Loss of the Grx1 homolog also exacerbated the neurodegenerative phenotype in other C. elegans models, including overexpression of human α-synuclein and overexpression of tyrosine hydroxylase (a model of sporadic PD). Therefore, our results reveal a novel neuroprotective role of glutaredoxin against dopaminergic neurodegeneration in models of familial and sporadic PD.
DOI: 10.1093/hmg/ddu542
PubMed: 25355420
PubMed Central: PMC4321441
Affiliations:
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Johnson</name><affiliation><nlm:affiliation>Department of Pharmacology and.</nlm:affiliation><wicri:noCountry code="no comma">Department of Pharmacology and.</wicri:noCountry></affiliation></author><author><name sortKey="Yao, Chen" sort="Yao, Chen" uniqKey="Yao C" first="Chen" last="Yao">Chen Yao</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Siedlak, Sandra L" sort="Siedlak, Sandra L" uniqKey="Siedlak S" first="Sandra L" last="Siedlak">Sandra L. 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Caldwell</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biological Sciences, The University of Alabama, Tuscaloosa, AL 35487, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, The University of Alabama, Tuscaloosa, AL 35487</wicri:regionArea><placeName><region type="state">Alabama</region></placeName></affiliation></author><author><name sortKey="Wilson Delfosse, Amy L" sort="Wilson Delfosse, Amy L" uniqKey="Wilson Delfosse A" first="Amy L" last="Wilson-Delfosse">Amy L. Wilson-Delfosse</name><affiliation><nlm:affiliation>Department of Pharmacology and.</nlm:affiliation><wicri:noCountry code="no comma">Department of Pharmacology and.</wicri:noCountry></affiliation></author><author><name sortKey="Mieyal, John J" sort="Mieyal, John J" uniqKey="Mieyal J" first="John J" last="Mieyal">John J. Mieyal</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pharmacology and Louis B. Stokes Veterans Affairs Medical Research Center, Cleveland, OH 44106, USA jjm5@case.edu shu.chen@case.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Pharmacology and Louis B. Stokes Veterans Affairs Medical Research Center, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Chen, Shu G" sort="Chen, Shu G" uniqKey="Chen S" first="Shu G" last="Chen">Shu G. 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Johnson</name><affiliation><nlm:affiliation>Department of Pharmacology and.</nlm:affiliation><wicri:noCountry code="no comma">Department of Pharmacology and.</wicri:noCountry></affiliation></author><author><name sortKey="Yao, Chen" sort="Yao, Chen" uniqKey="Yao C" first="Chen" last="Yao">Chen Yao</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Siedlak, Sandra L" sort="Siedlak, Sandra L" uniqKey="Siedlak S" first="Sandra L" last="Siedlak">Sandra L. Siedlak</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Wang, Wenzhang" sort="Wang, Wenzhang" uniqKey="Wang W" first="Wenzhang" last="Wang">Wenzhang Wang</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Zhu, Xiongwei" sort="Zhu, Xiongwei" uniqKey="Zhu X" first="Xiongwei" last="Zhu">Xiongwei Zhu</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Caldwell, Guy A" sort="Caldwell, Guy A" uniqKey="Caldwell G" first="Guy A" last="Caldwell">Guy A. Caldwell</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biological Sciences, The University of Alabama, Tuscaloosa, AL 35487, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, The University of Alabama, Tuscaloosa, AL 35487</wicri:regionArea><placeName><region type="state">Alabama</region></placeName></affiliation></author><author><name sortKey="Wilson Delfosse, Amy L" sort="Wilson Delfosse, Amy L" uniqKey="Wilson Delfosse A" first="Amy L" last="Wilson-Delfosse">Amy L. Wilson-Delfosse</name><affiliation><nlm:affiliation>Department of Pharmacology and.</nlm:affiliation><wicri:noCountry code="no comma">Department of Pharmacology and.</wicri:noCountry></affiliation></author><author><name sortKey="Mieyal, John J" sort="Mieyal, John J" uniqKey="Mieyal J" first="John J" last="Mieyal">John J. Mieyal</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pharmacology and Louis B. Stokes Veterans Affairs Medical Research Center, Cleveland, OH 44106, USA jjm5@case.edu shu.chen@case.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Pharmacology and Louis B. Stokes Veterans Affairs Medical Research Center, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Chen, Shu G" sort="Chen, Shu G" uniqKey="Chen S" first="Shu G" last="Chen">Shu G. Chen</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA, jjm5@case.edu shu.chen@case.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA</wicri:regionArea><wicri:noRegion>USA</wicri:noRegion></affiliation></author></analytic><series><title level="j">Human molecular genetics</title><idno type="eISSN">1460-2083</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Caenorhabditis elegans (genetics)</term><term>Cell Survival (MeSH)</term><term>Cysteine (metabolism)</term><term>Disease Models, Animal (MeSH)</term><term>Dopaminergic Neurons (metabolism)</term><term>Evolution, Molecular (MeSH)</term><term>Gene Expression Regulation (MeSH)</term><term>Glutaredoxins (deficiency)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Helminth Proteins (genetics)</term><term>Helminth Proteins (metabolism)</term><term>Homeostasis (MeSH)</term><term>Humans (MeSH)</term><term>Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 (MeSH)</term><term>Mesencephalon (metabolism)</term><term>Oxidative Stress (MeSH)</term><term>Parkinson Disease (genetics)</term><term>Phenotype (MeSH)</term><term>Protein-Serine-Threonine Kinases (genetics)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>RNA, Messenger (genetics)</term><term>RNA, Messenger (metabolism)</term><term>Tyrosine 3-Monooxygenase (genetics)</term><term>Tyrosine 3-Monooxygenase (metabolism)</term><term>alpha-Synuclein (genetics)</term><term>alpha-Synuclein (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (génétique)</term><term>ARN messager (métabolisme)</term><term>Animaux (MeSH)</term><term>Caenorhabditis elegans (génétique)</term><term>Cystéine (métabolisme)</term><term>Glutarédoxines (déficit)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Homéostasie (MeSH)</term><term>Humains (MeSH)</term><term>Leucine-rich repeat serine-threonine protein kinase-2 (MeSH)</term><term>Maladie de Parkinson (génétique)</term><term>Modèles animaux de maladie humaine (MeSH)</term><term>Mésencéphale (métabolisme)</term><term>Neurones dopaminergiques (métabolisme)</term><term>Phénotype (MeSH)</term><term>Protein-Serine-Threonine Kinases (génétique)</term><term>Protein-Serine-Threonine Kinases (métabolisme)</term><term>Protéines d'helminthes (génétique)</term><term>Protéines d'helminthes (métabolisme)</term><term>Régulation de l'expression des gènes (MeSH)</term><term>Stress oxydatif (MeSH)</term><term>Survie cellulaire (MeSH)</term><term>Tyrosine 3-monooxygenase (génétique)</term><term>Tyrosine 3-monooxygenase (métabolisme)</term><term>alpha-Synucléine (génétique)</term><term>alpha-Synucléine (métabolisme)</term><term>Évolution moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="deficiency" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Helminth Proteins</term><term>Protein-Serine-Threonine Kinases</term><term>RNA, Messenger</term><term>Tyrosine 3-Monooxygenase</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term><term>Glutaredoxins</term><term>Helminth Proteins</term><term>Protein-Serine-Threonine Kinases</term><term>RNA, Messenger</term><term>Tyrosine 3-Monooxygenase</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" qualifier="déficit" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Caenorhabditis elegans</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ARN messager</term><term>Caenorhabditis elegans</term><term>Glutarédoxines</term><term>Maladie de Parkinson</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines d'helminthes</term><term>Tyrosine 3-monooxygenase</term><term>alpha-Synucléine</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Dopaminergic Neurons</term><term>Mesencephalon</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN messager</term><term>Cystéine</term><term>Glutarédoxines</term><term>Mésencéphale</term><term>Neurones dopaminergiques</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines d'helminthes</term><term>Tyrosine 3-monooxygenase</term><term>alpha-Synucléine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Survival</term><term>Disease Models, Animal</term><term>Evolution, Molecular</term><term>Gene Expression Regulation</term><term>Homeostasis</term><term>Humans</term><term>Leucine-Rich Repeat Serine-Threonine Protein Kinase-2</term><term>Oxidative Stress</term><term>Phenotype</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Homéostasie</term><term>Humains</term><term>Leucine-rich repeat serine-threonine protein kinase-2</term><term>Modèles animaux de maladie humaine</term><term>Phénotype</term><term>Régulation de l'expression des gènes</term><term>Stress oxydatif</term><term>Survie cellulaire</term><term>Évolution moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Parkinson's disease (PD) is characterized by selective degeneration of dopaminergic neurons. Although the etiology of PD remains incompletely understood, oxidative stress has been implicated as an important contributor in the development of PD. Oxidative stress can lead to oxidation and functional perturbation of proteins critical to neuronal survival. Glutaredoxin 1 (Grx1) is an evolutionally conserved antioxidant enzyme that repairs protein oxidation by reversing the oxidative modification of cysteine known as S-glutathionylation. We aimed to explore the regulatory role of Grx1 in PD. We first examined the levels of Grx1 in postmortem midbrain samples from PD patients, and observed that Grx1 content is decreased in PD, specifically within the dopaminergic neurons. We subsequently investigated the potential role of Grx1 deficiency in PD pathogenesis by examining the consequences of loss of the Caenorhabditis elegans Grx1 homolog in well-established worm models of familial PD caused by overexpression of pathogenic human LRRK2 mutants G2019S or R1441C. We found that loss of the Grx1 homolog led to significant exacerbation of the neurodegenerative phenotype in C. elegans overexpressing the human LRRK2 mutants. Re-expression in the dopaminergic neurons of the active, but not a catalytically inactive form of the Grx1 homolog rescued the exacerbated phenotype. Loss of the Grx1 homolog also exacerbated the neurodegenerative phenotype in other C. elegans models, including overexpression of human α-synuclein and overexpression of tyrosine hydroxylase (a model of sporadic PD). Therefore, our results reveal a novel neuroprotective role of glutaredoxin against dopaminergic neurodegeneration in models of familial and sporadic PD. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25355420</PMID><DateCompleted><Year>2015</Year><Month>11</Month><Day>16</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2083</ISSN><JournalIssue CitedMedium="Internet"><Volume>24</Volume><Issue>5</Issue><PubDate><Year>2015</Year><Month>Mar</Month><Day>01</Day></PubDate></JournalIssue><Title>Human molecular genetics</Title><ISOAbbreviation>Hum Mol Genet</ISOAbbreviation></Journal><ArticleTitle>Glutaredoxin deficiency exacerbates neurodegeneration in C. elegans models of Parkinson's disease.</ArticleTitle><Pagination><MedlinePgn>1322-35</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/hmg/ddu542</ELocationID><Abstract><AbstractText>Parkinson's disease (PD) is characterized by selective degeneration of dopaminergic neurons. Although the etiology of PD remains incompletely understood, oxidative stress has been implicated as an important contributor in the development of PD. Oxidative stress can lead to oxidation and functional perturbation of proteins critical to neuronal survival. Glutaredoxin 1 (Grx1) is an evolutionally conserved antioxidant enzyme that repairs protein oxidation by reversing the oxidative modification of cysteine known as S-glutathionylation. We aimed to explore the regulatory role of Grx1 in PD. We first examined the levels of Grx1 in postmortem midbrain samples from PD patients, and observed that Grx1 content is decreased in PD, specifically within the dopaminergic neurons. We subsequently investigated the potential role of Grx1 deficiency in PD pathogenesis by examining the consequences of loss of the Caenorhabditis elegans Grx1 homolog in well-established worm models of familial PD caused by overexpression of pathogenic human LRRK2 mutants G2019S or R1441C. We found that loss of the Grx1 homolog led to significant exacerbation of the neurodegenerative phenotype in C. elegans overexpressing the human LRRK2 mutants. Re-expression in the dopaminergic neurons of the active, but not a catalytically inactive form of the Grx1 homolog rescued the exacerbated phenotype. Loss of the Grx1 homolog also exacerbated the neurodegenerative phenotype in other C. elegans models, including overexpression of human α-synuclein and overexpression of tyrosine hydroxylase (a model of sporadic PD). Therefore, our results reveal a novel neuroprotective role of glutaredoxin against dopaminergic neurodegeneration in models of familial and sporadic PD. </AbstractText><CopyrightInformation>© The Author 2014. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oup.com.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Johnson</LastName><ForeName>William M</ForeName><Initials>WM</Initials><AffiliationInfo><Affiliation>Department of Pharmacology and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yao</LastName><ForeName>Chen</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Siedlak</LastName><ForeName>Sandra L</ForeName><Initials>SL</Initials><AffiliationInfo><Affiliation>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Wenzhang</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhu</LastName><ForeName>Xiongwei</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Caldwell</LastName><ForeName>Guy A</ForeName><Initials>GA</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences, The University of Alabama, Tuscaloosa, AL 35487, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wilson-Delfosse</LastName><ForeName>Amy L</ForeName><Initials>AL</Initials><AffiliationInfo><Affiliation>Department of Pharmacology and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mieyal</LastName><ForeName>John J</ForeName><Initials>JJ</Initials><AffiliationInfo><Affiliation>Department of Pharmacology and Louis B. Stokes Veterans Affairs Medical Research Center, Cleveland, OH 44106, USA jjm5@case.edu shu.chen@case.edu.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Shu G</ForeName><Initials>SG</Initials><AffiliationInfo><Affiliation>Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA, jjm5@case.edu shu.chen@case.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P40 OD010440</GrantID><Acronym>OD</Acronym><Agency>NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R21 NS085503</GrantID><Acronym>NS</Acronym><Agency>NINDS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32 GM008803</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>NS083498</GrantID><Acronym>NS</Acronym><Agency>NINDS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>NS085503</GrantID><Acronym>NS</Acronym><Agency>NINDS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>NS073170</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><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>10</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Hum Mol Genet</MedlineTA><NlmUniqueID>9208958</NlmUniqueID><ISSNLinking>0964-6906</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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