Identification of brain substrates of transglutaminase by functional proteomics supports its role in neurodegenerative diseases.
Identifieur interne : 000020 ( PubMed/Curation ); précédent : 000019; suivant : 000021Identification of brain substrates of transglutaminase by functional proteomics supports its role in neurodegenerative diseases.
Auteurs : William André [France] ; Isabelle Nondier [France] ; Maud Valensi [France] ; François Guillonneau [France] ; Christian Federici [France] ; Guylaine Hoffner [France] ; Philippe Djian [France]Source :
- Neurobiology of disease [ 1095-953X ] ; 2017.
Abstract
Transglutaminases are calcium-dependent enzymes that catalyze the formation of ε-(γ-glutamyl)lysine isopeptide bonds between specific glutamine and lysine residues. Some transglutaminase isoforms are present in the brain and are thought to participate in the protein aggregation characteristic of neurological diseases such as Huntington, Alzheimer's and Parkinson's disease. We have developed a functional proteomics strategy in which biotinylated amine-donor and amine-acceptor probes were used to identify the transglutaminase substrates present in brain. Bioinformatics analyses revealed that most of the 166 brain substrates identified interacted with huntingtin, the amyloid precursor protein or α-synuclein and that neurological disease was the most significant canonical pathway associated with the substrates. The physiological relevance of the substrates identified by mass spectrometry was confirmed by the fact that three of them (actin, β-tubulin and a neurofilament subunit) were polymerized in neuronal cells when cytosolic calcium concentration was raised. We also showed by in-situ immunolabeling that some of the substrates were part of the protein aggregates found in neurological diseases. These results strongly support the idea that the crosslinking activity of brain transglutaminase participates in the formation of the protein aggregates found in diseases of the central nervous system.
DOI: 10.1016/j.nbd.2017.01.007
PubMed: 28132929
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Electronic address: philippe.djian@parisdescartes.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de physiologie cérébrale, UMR 8118, Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes, Paris</wicri:regionArea></affiliation></author></analytic><series><title level="j">Neurobiology of disease</title><idno type="eISSN">1095-953X</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">Transglutaminases are calcium-dependent enzymes that catalyze the formation of ε-(γ-glutamyl)lysine isopeptide bonds between specific glutamine and lysine residues. Some transglutaminase isoforms are present in the brain and are thought to participate in the protein aggregation characteristic of neurological diseases such as Huntington, Alzheimer's and Parkinson's disease. We have developed a functional proteomics strategy in which biotinylated amine-donor and amine-acceptor probes were used to identify the transglutaminase substrates present in brain. Bioinformatics analyses revealed that most of the 166 brain substrates identified interacted with huntingtin, the amyloid precursor protein or α-synuclein and that neurological disease was the most significant canonical pathway associated with the substrates. The physiological relevance of the substrates identified by mass spectrometry was confirmed by the fact that three of them (actin, β-tubulin and a neurofilament subunit) were polymerized in neuronal cells when cytosolic calcium concentration was raised. We also showed by in-situ immunolabeling that some of the substrates were part of the protein aggregates found in neurological diseases. These results strongly support the idea that the crosslinking activity of brain transglutaminase participates in the formation of the protein aggregates found in diseases of the central nervous system.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">28132929</PMID><DateCreated><Year>2017</Year><Month>01</Month><Day>30</Day></DateCreated><DateRevised><Year>2017</Year><Month>01</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1095-953X</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2017</Year><Month>Jan</Month><Day>26</Day></PubDate></JournalIssue><Title>Neurobiology of disease</Title><ISOAbbreviation>Neurobiol. Dis.</ISOAbbreviation></Journal><ArticleTitle>Identification of brain substrates of transglutaminase by functional proteomics supports its role in neurodegenerative diseases.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">S0969-9961(17)30018-9</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.nbd.2017.01.007</ELocationID><Abstract><AbstractText NlmCategory="UNASSIGNED">Transglutaminases are calcium-dependent enzymes that catalyze the formation of ε-(γ-glutamyl)lysine isopeptide bonds between specific glutamine and lysine residues. Some transglutaminase isoforms are present in the brain and are thought to participate in the protein aggregation characteristic of neurological diseases such as Huntington, Alzheimer's and Parkinson's disease. We have developed a functional proteomics strategy in which biotinylated amine-donor and amine-acceptor probes were used to identify the transglutaminase substrates present in brain. Bioinformatics analyses revealed that most of the 166 brain substrates identified interacted with huntingtin, the amyloid precursor protein or α-synuclein and that neurological disease was the most significant canonical pathway associated with the substrates. The physiological relevance of the substrates identified by mass spectrometry was confirmed by the fact that three of them (actin, β-tubulin and a neurofilament subunit) were polymerized in neuronal cells when cytosolic calcium concentration was raised. We also showed by in-situ immunolabeling that some of the substrates were part of the protein aggregates found in neurological diseases. These results strongly support the idea that the crosslinking activity of brain transglutaminase participates in the formation of the protein aggregates found in diseases of the central nervous system.</AbstractText><CopyrightInformation>Copyright © 2016. Published by Elsevier Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>André</LastName><ForeName>William</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Laboratoire de physiologie cérébrale, UMR 8118, Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nondier</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Laboratoire de physiologie cérébrale, UMR 8118, Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Valensi</LastName><ForeName>Maud</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratoire de physiologie cérébrale, UMR 8118, Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guillonneau</LastName><ForeName>François</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Institut Cochin, INSERM U1016/CNRS UMR8104, Paris, France; 3P5 Plateforme de protéomique, Université Paris Descartes, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Federici</LastName><ForeName>Christian</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Institut Cochin, INSERM U1016/CNRS UMR8104, Paris, France; 3P5 Plateforme de protéomique, Université Paris Descartes, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hoffner</LastName><ForeName>Guylaine</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Laboratoire de physiologie cérébrale, UMR 8118, Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes, Paris, France. Electronic address: guylaine.hoffner@parisdescartes.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Djian</LastName><ForeName>Philippe</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Laboratoire de physiologie cérébrale, UMR 8118, Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes, Paris, France. Electronic address: philippe.djian@parisdescartes.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>01</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Neurobiol Dis</MedlineTA><NlmUniqueID>9500169</NlmUniqueID><ISSNLinking>0969-9961</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Aggregates</Keyword><Keyword MajorTopicYN="N">Alzheimer's disease</Keyword><Keyword MajorTopicYN="N">Amyloid precursor protein</Keyword><Keyword MajorTopicYN="N">Huntingtin</Keyword><Keyword MajorTopicYN="N">Huntington disease</Keyword><Keyword MajorTopicYN="N">Inclusions</Keyword><Keyword MajorTopicYN="N">Oligomers</Keyword><Keyword MajorTopicYN="N">Parkinson's disease</Keyword><Keyword MajorTopicYN="N">Polyglutamine</Keyword><Keyword MajorTopicYN="N">α-synuclein</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>04</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2017</Year><Month>01</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>01</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>1</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>1</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>1</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28132929</ArticleId><ArticleId IdType="pii">S0969-9961(17)30018-9</ArticleId><ArticleId IdType="doi">10.1016/j.nbd.2017.01.007</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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