Chemistry of mammalian metallothioneins and their interaction with amyloidogenic peptides and proteins.
Identifieur interne : 001021 ( PubMed/Checkpoint ); précédent : 001020; suivant : 001022Chemistry of mammalian metallothioneins and their interaction with amyloidogenic peptides and proteins.
Auteurs : Elena Atrián-Blasco [France] ; Alice Santoro [France] ; Dean L. Pountney [Australie] ; Gabriele Meloni [États-Unis] ; Christelle Hureau [France] ; Peter Faller [France]Source :
- Chemical Society reviews [ 1460-4744 ] ; 2017.
Abstract
Cu and Zn ions are essential in most living beings. Their metabolism is critical for health and mis-metabolism can be lethal. In the last two decades, a large body of evidence has reported the role of copper, zinc and iron, and oxidative stress in several neurodegenerative diseases like Alzheimer's, Parkinson's, prion diseases, etc. To what extent this mis-metabolism is causative or a consequence of these diseases is still a matter of research. In this context metallothioneins (MTs) appear to play a central gate-keeper role in controlling aberrant metal-protein interactions. MTs are small proteins that can bind high amounts of Zn(ii) and Cu(i) ions in metal-cluster arrangements via their cysteine thiolates. Moreover, MTs are well known antioxidants. The present tutorial outlines the chemistry underlying the interconnection between copper(i/ii) and zinc(ii) coordination to amyloidogenic proteins and MTs, and their redox properties in generation and/or silencing reactive oxygen species (overproduced in oxidative stress) and other reactants. These studies have revealed the coordination chemistry involved in neurodegenerative diseases and the interactions between MTs and amyloidogenic protein metal-complexes (like amyloid-β, α-synuclein and prion-protein). Overall, the protective role of MTs in neurodegenerative processes is emerging, serving as a foundation for exploring MT chemistry as inspiration for therapeutic approaches.
DOI: 10.1039/c7cs00448f
PubMed: 29114657
Affiliations:
- Australie, France, États-Unis
- Alsace (région administrative), Grand Est, Midi-Pyrénées, Occitanie (région administrative), Texas
- Strasbourg, Toulouse
- Université de Strasbourg
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Pascal, 67081 Strasbourg, France. pfaller@unistra.fr and University of Strasbourg Institute for Advanced Study (USIAS), Strasbourg, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Biometals and Biology Chemistry, Institut de Chimie (CNRS UMR7177), Université de Strasbourg, 4 rue B. Pascal, 67081 Strasbourg, France. pfaller@unistra.fr and University of Strasbourg Institute for Advanced Study (USIAS), Strasbourg</wicri:regionArea><placeName><region type="region">Grand Est</region><region type="old region">Alsace (région administrative)</region><settlement type="city">Strasbourg</settlement><settlement type="city">Strasbourg</settlement></placeName><orgName type="university">Université de Strasbourg</orgName></affiliation></author></analytic><series><title level="j">Chemical Society reviews</title><idno type="eISSN">1460-4744</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cu and Zn ions are essential in most living beings. Their metabolism is critical for health and mis-metabolism can be lethal. In the last two decades, a large body of evidence has reported the role of copper, zinc and iron, and oxidative stress in several neurodegenerative diseases like Alzheimer's, Parkinson's, prion diseases, etc. To what extent this mis-metabolism is causative or a consequence of these diseases is still a matter of research. In this context metallothioneins (MTs) appear to play a central gate-keeper role in controlling aberrant metal-protein interactions. MTs are small proteins that can bind high amounts of Zn(ii) and Cu(i) ions in metal-cluster arrangements via their cysteine thiolates. Moreover, MTs are well known antioxidants. The present tutorial outlines the chemistry underlying the interconnection between copper(i/ii) and zinc(ii) coordination to amyloidogenic proteins and MTs, and their redox properties in generation and/or silencing reactive oxygen species (overproduced in oxidative stress) and other reactants. These studies have revealed the coordination chemistry involved in neurodegenerative diseases and the interactions between MTs and amyloidogenic protein metal-complexes (like amyloid-β, α-synuclein and prion-protein). Overall, the protective role of MTs in neurodegenerative processes is emerging, serving as a foundation for exploring MT chemistry as inspiration for therapeutic approaches.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">29114657</PMID><DateCreated><Year>2017</Year><Month>11</Month><Day>08</Day></DateCreated><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-4744</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2017</Year><Month>Nov</Month><Day>08</Day></PubDate></JournalIssue><Title>Chemical Society reviews</Title><ISOAbbreviation>Chem Soc Rev</ISOAbbreviation></Journal><ArticleTitle>Chemistry of mammalian metallothioneins and their interaction with amyloidogenic peptides and proteins.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1039/c7cs00448f</ELocationID><Abstract><AbstractText>Cu and Zn ions are essential in most living beings. Their metabolism is critical for health and mis-metabolism can be lethal. In the last two decades, a large body of evidence has reported the role of copper, zinc and iron, and oxidative stress in several neurodegenerative diseases like Alzheimer's, Parkinson's, prion diseases, etc. To what extent this mis-metabolism is causative or a consequence of these diseases is still a matter of research. In this context metallothioneins (MTs) appear to play a central gate-keeper role in controlling aberrant metal-protein interactions. MTs are small proteins that can bind high amounts of Zn(ii) and Cu(i) ions in metal-cluster arrangements via their cysteine thiolates. Moreover, MTs are well known antioxidants. The present tutorial outlines the chemistry underlying the interconnection between copper(i/ii) and zinc(ii) coordination to amyloidogenic proteins and MTs, and their redox properties in generation and/or silencing reactive oxygen species (overproduced in oxidative stress) and other reactants. These studies have revealed the coordination chemistry involved in neurodegenerative diseases and the interactions between MTs and amyloidogenic protein metal-complexes (like amyloid-β, α-synuclein and prion-protein). Overall, the protective role of MTs in neurodegenerative processes is emerging, serving as a foundation for exploring MT chemistry as inspiration for therapeutic approaches.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Atrián-Blasco</LastName><ForeName>Elena</ForeName><Initials>E</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-3830-7847</Identifier><AffiliationInfo><Affiliation>LCC (Laboratoire de Chimie de Coordination), CNRS UPR 8241, 205 route de Narbonne, 31062 Toulouse Cedex 09, France and Université de Toulouse, UPS, INPT, 31077 Toulouse, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Santoro</LastName><ForeName>Alice</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Biometals and Biology Chemistry, Institut de Chimie (CNRS UMR7177), Université de Strasbourg, 4 rue B. Pascal, 67081 Strasbourg, France. pfaller@unistra.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pountney</LastName><ForeName>Dean L</ForeName><Initials>DL</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-0653-7832</Identifier><AffiliationInfo><Affiliation>Menzies Health Institute Queensland, Griffith University Gold Coast, 4222, QLD, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Meloni</LastName><ForeName>Gabriele</ForeName><Initials>G</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-4976-1401</Identifier><AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, University of Texas at Dallas, 800 W Campbell Road, Richardson, TX 75080-3021, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hureau</LastName><ForeName>Christelle</ForeName><Initials>C</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-3339-0239</Identifier><AffiliationInfo><Affiliation>LCC (Laboratoire de Chimie de Coordination), CNRS UPR 8241, 205 route de Narbonne, 31062 Toulouse Cedex 09, France and Université de Toulouse, UPS, INPT, 31077 Toulouse, France and University of Strasbourg Institute for Advanced Study (USIAS), Strasbourg, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Faller</LastName><ForeName>Peter</ForeName><Initials>P</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-8013-0806</Identifier><AffiliationInfo><Affiliation>Biometals and Biology Chemistry, Institut de Chimie (CNRS UMR7177), Université de Strasbourg, 4 rue B. Pascal, 67081 Strasbourg, France. pfaller@unistra.fr and University of Strasbourg Institute for Advanced Study (USIAS), Strasbourg, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>638712</GrantID><Agency>European Research Council</Agency><Country>International</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>11</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Chem Soc Rev</MedlineTA><NlmUniqueID>0335405</NlmUniqueID><ISSNLinking>0306-0012</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>11</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>11</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>11</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29114657</ArticleId><ArticleId IdType="doi">10.1039/c7cs00448f</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>France</li><li>États-Unis</li></country><region><li>Alsace (région administrative)</li><li>Grand Est</li><li>Midi-Pyrénées</li><li>Occitanie (région administrative)</li><li>Texas</li></region><settlement><li>Strasbourg</li><li>Toulouse</li></settlement><orgName><li>Université de Strasbourg</li></orgName></list><tree><country name="France"><region name="Occitanie (région administrative)"><name sortKey="Atrian Blasco, Elena" sort="Atrian Blasco, Elena" uniqKey="Atrian Blasco E" first="Elena" last="Atrián-Blasco">Elena Atrián-Blasco</name></region><name sortKey="Faller, Peter" sort="Faller, Peter" uniqKey="Faller P" first="Peter" last="Faller">Peter Faller</name><name sortKey="Hureau, Christelle" sort="Hureau, Christelle" uniqKey="Hureau C" first="Christelle" last="Hureau">Christelle Hureau</name><name sortKey="Santoro, Alice" sort="Santoro, Alice" uniqKey="Santoro A" first="Alice" last="Santoro">Alice Santoro</name></country><country name="Australie"><noRegion><name sortKey="Pountney, Dean L" sort="Pountney, Dean L" uniqKey="Pountney D" first="Dean L" last="Pountney">Dean L. 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