Clusterin protects neurons against intracellular proteotoxicity.
Identifieur interne : 000F79 ( PubMed/Checkpoint ); précédent : 000F78; suivant : 000F80Clusterin protects neurons against intracellular proteotoxicity.
Auteurs : Jenna M. Gregory [Royaume-Uni] ; Daniel R. Whiten [Royaume-Uni] ; Rebecca A. Brown [Australie] ; Teresa P. Barros [Royaume-Uni] ; Janet R. Kumita [Royaume-Uni] ; Justin J. Yerbury [Australie] ; Sandeep Satapathy [Australie] ; Karina Mcdade [Royaume-Uni] ; Colin Smith [Royaume-Uni] ; Leila M. Luheshi [Royaume-Uni] ; Christopher M. Dobson [Royaume-Uni] ; Mark R. Wilson [Australie]Source :
- Acta neuropathologica communications [ 2051-5960 ] ; 2017.
Abstract
It is now widely accepted in the field that the normally secreted chaperone clusterin is redirected to the cytosol during endoplasmic reticulum (ER) stress, although the physiological function(s) of this physical relocation remain unknown. We have examined in this study whether or not increased expression of clusterin is able to protect neuronal cells against intracellular protein aggregation and cytotoxicity, characteristics that are strongly implicated in a range of neurodegenerative diseases. We used the amyotrophic lateral sclerosis-associated protein TDP-43 as a primary model to investigate the effects of clusterin on protein aggregation and neurotoxicity in complementary in vitro, neuronal cell and Drosophila systems. We have shown that clusterin directly interacts with TDP-43 in vitro and potently inhibits its aggregation, and observed that in ER stressed neuronal cells, clusterin co-localized with TDP-43 and specifically reduced the numbers of cytoplasmic inclusions. We further showed that the expression of TDP-43 in transgenic Drosophila neurons induced ER stress and that co-expression of clusterin resulted in a dramatic clearance of mislocalized TDP-43 from motor neuron axons, partially rescued locomotor activity and significantly extended lifespan. We also showed that in Drosophila photoreceptor cells, clusterin co-expression gave ER stress-dependent protection against proteotoxicity arising from both Huntingtin-Q128 and mutant (R406W) human tau. We therefore conclude that increased expression of clusterin can provide an important defense against intracellular proteotoxicity under conditions that mimic specific features of neurodegenerative disease.
DOI: 10.1186/s40478-017-0481-1
PubMed: 29115989
Affiliations:
- Australie, Royaume-Uni
- Angleterre, Angleterre de l'Est, Écosse
- Cambridge, Édimbourg
- Université d'Édimbourg, Université de Cambridge
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Gregory</name><affiliation wicri:level="4"><nlm:affiliation>Centre for Clinical Brain Sciences, University of Edinburgh, Chancellor's Building, Edinburgh, EH16 4SB, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Centre for Clinical Brain Sciences, University of Edinburgh, Chancellor's Building, Edinburgh, EH16 4SB</wicri:regionArea><orgName type="university">Université d'Édimbourg</orgName><placeName><settlement type="city">Édimbourg</settlement><region type="country">Écosse</region></placeName></affiliation></author><author><name sortKey="Whiten, Daniel R" sort="Whiten, Daniel R" uniqKey="Whiten D" first="Daniel R" last="Whiten">Daniel R. Whiten</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW</wicri:regionArea><orgName type="university">Université de Cambridge</orgName><placeName><settlement type="city">Cambridge</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Angleterre de l'Est</region></placeName></affiliation></author><author><name sortKey="Brown, Rebecca A" sort="Brown, Rebecca A" uniqKey="Brown R" first="Rebecca A" last="Brown">Rebecca A. Brown</name><affiliation wicri:level="1"><nlm:affiliation>Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522</wicri:regionArea><wicri:noRegion>2522</wicri:noRegion></affiliation></author><author><name sortKey="Barros, Teresa P" sort="Barros, Teresa P" uniqKey="Barros T" first="Teresa P" last="Barros">Teresa P. Barros</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW</wicri:regionArea><orgName type="university">Université de Cambridge</orgName><placeName><settlement type="city">Cambridge</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Angleterre de l'Est</region></placeName></affiliation></author><author><name sortKey="Kumita, Janet R" sort="Kumita, Janet R" uniqKey="Kumita J" first="Janet R" last="Kumita">Janet R. Kumita</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW</wicri:regionArea><orgName type="university">Université de Cambridge</orgName><placeName><settlement type="city">Cambridge</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Angleterre de l'Est</region></placeName></affiliation></author><author><name sortKey="Yerbury, Justin J" sort="Yerbury, Justin J" uniqKey="Yerbury J" first="Justin J" last="Yerbury">Justin J. Yerbury</name><affiliation wicri:level="1"><nlm:affiliation>Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522</wicri:regionArea><wicri:noRegion>2522</wicri:noRegion></affiliation></author><author><name sortKey="Satapathy, Sandeep" sort="Satapathy, Sandeep" uniqKey="Satapathy S" first="Sandeep" last="Satapathy">Sandeep Satapathy</name><affiliation wicri:level="1"><nlm:affiliation>Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522</wicri:regionArea><wicri:noRegion>2522</wicri:noRegion></affiliation></author><author><name sortKey="Mcdade, Karina" sort="Mcdade, Karina" uniqKey="Mcdade K" first="Karina" last="Mcdade">Karina Mcdade</name><affiliation wicri:level="4"><nlm:affiliation>Centre for Clinical Brain Sciences, University of Edinburgh, Chancellor's Building, Edinburgh, EH16 4SB, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Centre for Clinical Brain Sciences, University of Edinburgh, Chancellor's Building, Edinburgh, EH16 4SB</wicri:regionArea><orgName type="university">Université d'Édimbourg</orgName><placeName><settlement type="city">Édimbourg</settlement><region type="country">Écosse</region></placeName></affiliation></author><author><name sortKey="Smith, Colin" sort="Smith, Colin" uniqKey="Smith C" first="Colin" last="Smith">Colin Smith</name><affiliation wicri:level="4"><nlm:affiliation>Centre for Clinical Brain Sciences, University of Edinburgh, Chancellor's Building, Edinburgh, EH16 4SB, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Centre for Clinical Brain Sciences, University of Edinburgh, Chancellor's Building, Edinburgh, EH16 4SB</wicri:regionArea><orgName type="university">Université d'Édimbourg</orgName><placeName><settlement type="city">Édimbourg</settlement><region type="country">Écosse</region></placeName></affiliation></author><author><name sortKey="Luheshi, Leila M" sort="Luheshi, Leila M" uniqKey="Luheshi L" first="Leila M" last="Luheshi">Leila M. Luheshi</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW</wicri:regionArea><orgName type="university">Université de Cambridge</orgName><placeName><settlement type="city">Cambridge</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Angleterre de l'Est</region></placeName></affiliation></author><author><name sortKey="Dobson, Christopher M" sort="Dobson, Christopher M" uniqKey="Dobson C" first="Christopher M" last="Dobson">Christopher M. Dobson</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK. cmd44@cam.ac.uk.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW</wicri:regionArea><orgName type="university">Université de Cambridge</orgName><placeName><settlement type="city">Cambridge</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Angleterre de l'Est</region></placeName></affiliation></author><author><name sortKey="Wilson, Mark R" sort="Wilson, Mark R" uniqKey="Wilson M" first="Mark R" last="Wilson">Mark R. Wilson</name><affiliation wicri:level="1"><nlm:affiliation>Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522, Australia. mrw@uow.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522</wicri:regionArea><wicri:noRegion>2522</wicri:noRegion></affiliation></author></analytic><series><title level="j">Acta neuropathologica communications</title><idno type="eISSN">2051-5960</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">It is now widely accepted in the field that the normally secreted chaperone clusterin is redirected to the cytosol during endoplasmic reticulum (ER) stress, although the physiological function(s) of this physical relocation remain unknown. We have examined in this study whether or not increased expression of clusterin is able to protect neuronal cells against intracellular protein aggregation and cytotoxicity, characteristics that are strongly implicated in a range of neurodegenerative diseases. We used the amyotrophic lateral sclerosis-associated protein TDP-43 as a primary model to investigate the effects of clusterin on protein aggregation and neurotoxicity in complementary in vitro, neuronal cell and Drosophila systems. We have shown that clusterin directly interacts with TDP-43 in vitro and potently inhibits its aggregation, and observed that in ER stressed neuronal cells, clusterin co-localized with TDP-43 and specifically reduced the numbers of cytoplasmic inclusions. We further showed that the expression of TDP-43 in transgenic Drosophila neurons induced ER stress and that co-expression of clusterin resulted in a dramatic clearance of mislocalized TDP-43 from motor neuron axons, partially rescued locomotor activity and significantly extended lifespan. We also showed that in Drosophila photoreceptor cells, clusterin co-expression gave ER stress-dependent protection against proteotoxicity arising from both Huntingtin-Q128 and mutant (R406W) human tau. We therefore conclude that increased expression of clusterin can provide an important defense against intracellular proteotoxicity under conditions that mimic specific features of neurodegenerative disease.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">29115989</PMID><DateCreated><Year>2017</Year><Month>11</Month><Day>08</Day></DateCreated><DateRevised><Year>2017</Year><Month>11</Month><Day>18</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2051-5960</ISSN><JournalIssue CitedMedium="Internet"><Volume>5</Volume><Issue>1</Issue><PubDate><Year>2017</Year><Month>Nov</Month><Day>07</Day></PubDate></JournalIssue><Title>Acta neuropathologica communications</Title><ISOAbbreviation>Acta Neuropathol Commun</ISOAbbreviation></Journal><ArticleTitle>Clusterin protects neurons against intracellular proteotoxicity.</ArticleTitle><Pagination><MedlinePgn>81</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1186/s40478-017-0481-1</ELocationID><Abstract><AbstractText>It is now widely accepted in the field that the normally secreted chaperone clusterin is redirected to the cytosol during endoplasmic reticulum (ER) stress, although the physiological function(s) of this physical relocation remain unknown. We have examined in this study whether or not increased expression of clusterin is able to protect neuronal cells against intracellular protein aggregation and cytotoxicity, characteristics that are strongly implicated in a range of neurodegenerative diseases. We used the amyotrophic lateral sclerosis-associated protein TDP-43 as a primary model to investigate the effects of clusterin on protein aggregation and neurotoxicity in complementary in vitro, neuronal cell and Drosophila systems. We have shown that clusterin directly interacts with TDP-43 in vitro and potently inhibits its aggregation, and observed that in ER stressed neuronal cells, clusterin co-localized with TDP-43 and specifically reduced the numbers of cytoplasmic inclusions. We further showed that the expression of TDP-43 in transgenic Drosophila neurons induced ER stress and that co-expression of clusterin resulted in a dramatic clearance of mislocalized TDP-43 from motor neuron axons, partially rescued locomotor activity and significantly extended lifespan. We also showed that in Drosophila photoreceptor cells, clusterin co-expression gave ER stress-dependent protection against proteotoxicity arising from both Huntingtin-Q128 and mutant (R406W) human tau. We therefore conclude that increased expression of clusterin can provide an important defense against intracellular proteotoxicity under conditions that mimic specific features of neurodegenerative disease.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gregory</LastName><ForeName>Jenna M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Centre for Clinical Brain Sciences, University of Edinburgh, Chancellor's Building, Edinburgh, EH16 4SB, UK.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Euan MacDonald Centre for MND Research, 49 Little France Crescent-Chancellor, Edinburgh, EH16 4SB, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Whiten</LastName><ForeName>Daniel R</ForeName><Initials>DR</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Brown</LastName><ForeName>Rebecca A</ForeName><Initials>RA</Initials><AffiliationInfo><Affiliation>Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Barros</LastName><ForeName>Teresa P</ForeName><Initials>TP</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kumita</LastName><ForeName>Janet R</ForeName><Initials>JR</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yerbury</LastName><ForeName>Justin J</ForeName><Initials>JJ</Initials><AffiliationInfo><Affiliation>Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Satapathy</LastName><ForeName>Sandeep</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>McDade</LastName><ForeName>Karina</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Centre for Clinical Brain Sciences, University of Edinburgh, Chancellor's Building, Edinburgh, EH16 4SB, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Smith</LastName><ForeName>Colin</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Centre for Clinical Brain Sciences, University of Edinburgh, Chancellor's Building, Edinburgh, EH16 4SB, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Luheshi</LastName><ForeName>Leila M</ForeName><Initials>LM</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dobson</LastName><ForeName>Christopher M</ForeName><Initials>CM</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK. cmd44@cam.ac.uk.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wilson</LastName><ForeName>Mark R</ForeName><Initials>MR</Initials><AffiliationInfo><Affiliation>Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522, Australia. mrw@uow.edu.au.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>11</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Acta Neuropathol Commun</MedlineTA><NlmUniqueID>101610673</NlmUniqueID><ISSNLinking>2051-5960</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Chaperone translocation</Keyword><Keyword MajorTopicYN="N">Cytoplasmic inclusions</Keyword><Keyword MajorTopicYN="N">Proteotoxicity</Keyword><Keyword MajorTopicYN="N">TDP-43</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>10</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>10</Month><Day>11</Day></PubMedPubDate><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>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29115989</ArticleId><ArticleId IdType="doi">10.1186/s40478-017-0481-1</ArticleId><ArticleId IdType="pii">10.1186/s40478-017-0481-1</ArticleId><ArticleId IdType="pmc">PMC5678579</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Angleterre de l'Est</li><li>Écosse</li></region><settlement><li>Cambridge</li><li>Édimbourg</li></settlement><orgName><li>Université d'Édimbourg</li><li>Université de Cambridge</li></orgName></list><tree><country name="Royaume-Uni"><region name="Écosse"><name sortKey="Gregory, Jenna M" sort="Gregory, Jenna M" uniqKey="Gregory J" first="Jenna M" last="Gregory">Jenna M. Gregory</name></region><name sortKey="Barros, Teresa P" sort="Barros, Teresa P" uniqKey="Barros T" first="Teresa P" last="Barros">Teresa P. Barros</name><name sortKey="Dobson, Christopher M" sort="Dobson, Christopher M" uniqKey="Dobson C" first="Christopher M" last="Dobson">Christopher M. Dobson</name><name sortKey="Kumita, Janet R" sort="Kumita, Janet R" uniqKey="Kumita J" first="Janet R" last="Kumita">Janet R. Kumita</name><name sortKey="Luheshi, Leila M" sort="Luheshi, Leila M" uniqKey="Luheshi L" first="Leila M" last="Luheshi">Leila M. Luheshi</name><name sortKey="Mcdade, Karina" sort="Mcdade, Karina" uniqKey="Mcdade K" first="Karina" last="Mcdade">Karina Mcdade</name><name sortKey="Smith, Colin" sort="Smith, Colin" uniqKey="Smith C" first="Colin" last="Smith">Colin Smith</name><name sortKey="Whiten, Daniel R" sort="Whiten, Daniel R" uniqKey="Whiten D" first="Daniel R" last="Whiten">Daniel R. Whiten</name></country><country name="Australie"><noRegion><name sortKey="Brown, Rebecca A" sort="Brown, Rebecca A" uniqKey="Brown R" first="Rebecca A" last="Brown">Rebecca A. Brown</name></noRegion><name sortKey="Satapathy, Sandeep" sort="Satapathy, Sandeep" uniqKey="Satapathy S" first="Sandeep" last="Satapathy">Sandeep Satapathy</name><name sortKey="Wilson, Mark R" sort="Wilson, Mark R" uniqKey="Wilson M" first="Mark R" last="Wilson">Mark R. Wilson</name><name sortKey="Yerbury, Justin J" sort="Yerbury, Justin J" uniqKey="Yerbury J" first="Justin J" last="Yerbury">Justin J. Yerbury</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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