The roles of redox enzymes in Parkinson's disease: Focus on glutaredoxin.
Identifieur interne : 000498 ( Main/Exploration ); précédent : 000497; suivant : 000499The roles of redox enzymes in Parkinson's disease: Focus on glutaredoxin.
Auteurs : William M. Johnson [États-Unis] ; Amy L. Wilson-Delfosse [États-Unis] ; Shu G. Chen [États-Unis] ; John J. Mieyal [États-Unis]Source :
- Therapeutic targets for neurological diseases [ 2376-0478 ]
Abstract
Parkinson's disease (PD) results from the loss of dopaminergic neurons in the substantia nigra portion of the midbrain, and represents the second most common neurodegenerative disease in the world. Although the etiology of PD is currently unclear, oxidative stress and redox dysfunction are generally understood to play key roles in PD pathogenesis and progression. Aging and environmental factors predispose cells to adverse effects of redox changes. In addition to these factors, genetic mutations linked to PD have been observed to disrupt the redox balance. Mutations in leucine-rich repeat kinase 2 (LRRK2) are associated with autosomal dominant PD, and several of these mutations have also been shown to increase the levels of reactive oxygen species in cells. Anti-oxidant proteins are necessary to restore the redox balance and maintain cell viability. Over the past decade studies have started to demonstrate the critical importance for redox proteins mediating neuronal protection in models of PD. This commentary briefly describes some of the factors hypothesized to contribute to PD, specifically regarding the redox changes that occur in PD. Dysregulation of redox proteins in PD is highlighted by some of the work detailing the roles of peroxiredoxin-3 and thioredoxin-1 in models of PD. In an attempt to generate novel therapies for PD, several potent inhibitors of LRRK2 have been developed. The use of these compounds, both as tools to understand the biology of LRRK2 and as potential therapeutic strategies is also discussed. This mini-review then provides a historical prospective on the discovery and characterization of glutaredoxin (Grx1), and briefly describes current understanding of the role of Grx1 in PD. The review concludes by highlighting our recent publication describing the novel role for Grx1 in mediating dopaminergic neuronal protection both in vitro and in vivo.
PubMed: 26097894
PubMed Central: PMC4474481
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Wilson-Delfosse</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pharmacology, Case Western Reserve University, 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="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="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, Case Western Reserve University, Cleveland, OH 44106, USA ; Louis B. Stokes Veterans Affairs Medical Research Center, Cleveland, OH 44106, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, USA ; Louis B. 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Johnson</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</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 wicri:level="2"><nlm:affiliation>Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pharmacology, Case Western Reserve University, 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="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="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, Case Western Reserve University, Cleveland, OH 44106, USA ; Louis B. Stokes Veterans Affairs Medical Research Center, Cleveland, OH 44106, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, USA ; Louis B. Stokes Veterans Affairs Medical Research Center, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author></analytic><series><title level="j">Therapeutic targets for neurological diseases</title><idno type="ISSN">2376-0478</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Parkinson's disease (PD) results from the loss of dopaminergic neurons in the <i>substantia nigra</i> portion of the midbrain, and represents the second most common neurodegenerative disease in the world. Although the etiology of PD is currently unclear, oxidative stress and redox dysfunction are generally understood to play key roles in PD pathogenesis and progression. Aging and environmental factors predispose cells to adverse effects of redox changes. In addition to these factors, genetic mutations linked to PD have been observed to disrupt the redox balance. Mutations in leucine-rich repeat kinase 2 (<i>LRRK2</i>) are associated with autosomal dominant PD, and several of these mutations have also been shown to increase the levels of reactive oxygen species in cells. Anti-oxidant proteins are necessary to restore the redox balance and maintain cell viability. Over the past decade studies have started to demonstrate the critical importance for redox proteins mediating neuronal protection in models of PD. This commentary briefly describes some of the factors hypothesized to contribute to PD, specifically regarding the redox changes that occur in PD. Dysregulation of redox proteins in PD is highlighted by some of the work detailing the roles of peroxiredoxin-3 and thioredoxin-1 in models of PD. In an attempt to generate novel therapies for PD, several potent inhibitors of LRRK2 have been developed. The use of these compounds, both as tools to understand the biology of LRRK2 and as potential therapeutic strategies is also discussed. This mini-review then provides a historical prospective on the discovery and characterization of glutaredoxin (Grx1), and briefly describes current understanding of the role of Grx1 in PD. The review concludes by highlighting our recent publication describing the novel role for Grx1 in mediating dopaminergic neuronal protection both <i>in vitro</i> and <i>in vivo</i>.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">26097894</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">2376-0478</ISSN><JournalIssue CitedMedium="Print"><Volume>2</Volume><Issue>2</Issue><PubDate><MedlineDate>2015</MedlineDate></PubDate></JournalIssue><Title>Therapeutic targets for neurological diseases</Title><ISOAbbreviation>Ther Targets Neurol Dis</ISOAbbreviation></Journal><ArticleTitle>The roles of redox enzymes in Parkinson's disease: Focus on glutaredoxin.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">e790</ELocationID><Abstract><AbstractText>Parkinson's disease (PD) results from the loss of dopaminergic neurons in the <i>substantia nigra</i> portion of the midbrain, and represents the second most common neurodegenerative disease in the world. Although the etiology of PD is currently unclear, oxidative stress and redox dysfunction are generally understood to play key roles in PD pathogenesis and progression. Aging and environmental factors predispose cells to adverse effects of redox changes. In addition to these factors, genetic mutations linked to PD have been observed to disrupt the redox balance. Mutations in leucine-rich repeat kinase 2 (<i>LRRK2</i>) are associated with autosomal dominant PD, and several of these mutations have also been shown to increase the levels of reactive oxygen species in cells. Anti-oxidant proteins are necessary to restore the redox balance and maintain cell viability. Over the past decade studies have started to demonstrate the critical importance for redox proteins mediating neuronal protection in models of PD. This commentary briefly describes some of the factors hypothesized to contribute to PD, specifically regarding the redox changes that occur in PD. Dysregulation of redox proteins in PD is highlighted by some of the work detailing the roles of peroxiredoxin-3 and thioredoxin-1 in models of PD. In an attempt to generate novel therapies for PD, several potent inhibitors of LRRK2 have been developed. The use of these compounds, both as tools to understand the biology of LRRK2 and as potential therapeutic strategies is also discussed. This mini-review then provides a historical prospective on the discovery and characterization of glutaredoxin (Grx1), and briefly describes current understanding of the role of Grx1 in PD. The review concludes by highlighting our recent publication describing the novel role for Grx1 in mediating dopaminergic neuronal protection both <i>in vitro</i> and <i>in vivo</i>.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Johnson</LastName><ForeName>William M</ForeName><Initials>WM</Initials><AffiliationInfo><Affiliation>Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wilson-Delfosse</LastName><ForeName>Amy L</ForeName><Initials>AL</Initials><AffiliationInfo><Affiliation>Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, USA.</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.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mieyal</LastName><ForeName>John J</ForeName><Initials>JJ</Initials><AffiliationInfo><Affiliation>Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, USA ; Louis B. Stokes Veterans Affairs Medical Research Center, Cleveland, OH 44106, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>I01 BX000290</GrantID><Acronym>BX</Acronym><Agency>BLRD VA</Agency><Country>United States</Country></Grant><Grant><GrantID>R21 NS073170</GrantID><Acronym>NS</Acronym><Agency>NINDS 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></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Ther Targets Neurol Dis</MedlineTA><NlmUniqueID>101645414</NlmUniqueID><ISSNLinking>2376-0478</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">C. elegans</Keyword><Keyword MajorTopicYN="N">Glutaredoxin</Keyword><Keyword MajorTopicYN="N">LRRK2</Keyword><Keyword MajorTopicYN="N">Parkinson’s disease</Keyword><Keyword MajorTopicYN="N">redox</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>6</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>6</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>6</Month><Day>23</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26097894</ArticleId><ArticleId IdType="pmc">PMC4474481</ArticleId><ArticleId IdType="mid">NIHMS689460</ArticleId></ArticleIdList><pmc-dir>nihms</pmc-dir>
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Johnson</name></region><name sortKey="Chen, Shu G" sort="Chen, Shu G" uniqKey="Chen S" first="Shu G" last="Chen">Shu G. Chen</name><name sortKey="Mieyal, John J" sort="Mieyal, John J" uniqKey="Mieyal J" first="John J" last="Mieyal">John J. Mieyal</name><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></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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