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Pharmacoidea Ltd., Szeged, H-6726, Hungary
Biological Research Centre of the Hungarian Academy of Sciences, Szeged, H-6726, Hungary
Fraunhofer Institute for Algorithms and Scientific Computing (SCAI), Sankt Augustin, 53754, Germany
Szilak Laboratories, Bioinformatics and Molecule-Design, Szeged, H-6723, Hungary
Cited By :3
Export Date: 18 February 2020
Correspondence Address: Letoha, T.; Pharmacoidea Ltd.Hungary; email: tamas.letoha@pharmacoidea.eu
Pharmacoidea Ltd., Szeged, H-6726, Hungary
Biological Research Centre of the Hungarian Academy of Sciences, Szeged, H-6726, Hungary
Fraunhofer Institute for Algorithms and Scientific Computing (SCAI), Sankt Augustin, 53754, Germany
Szilak Laboratories, Bioinformatics and Molecule-Design, Szeged, H-6723, Hungary
Cited By :3
Export Date: 20 February 2020
Correspondence Address: Letoha, T.; Pharmacoidea Ltd.Hungary; email: tamas.letoha@pharmacoidea.eu
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Contribution of syndecans to cellular internalization and fibrillation of amyloid-β (1–42)
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Intraneuronal accumulation of amyloid-beta(1-42) (A beta 1-42) is one of the earliest signs of Alzheimer's disease (AD). Cell surface heparan sulfate proteoglycans (HSPGs) have profound influence on the cellular uptake of A beta 1-42 by mediating its attachment and subsequent internalization into the cells. Colocalization of amyloid plaques with members of the syndecan family of HSPGs, along with the increased expression of syndecan-3 and -4 have already been reported in postmortem AD brains. Considering the growing evidence on the involvement of syndecans in the pathogenesis of AD, we analyzed the contribution of syndecans to cellular uptake and fibrillation of A beta 1-42. Among syndecans, the neuron specific syndecan-3 isoform increased cellular uptake of A beta 1-42 the most. Kinetics of A beta 1-42 uptake also proved to be fairly different among SDC family members: syndecan-3 increased A beta 1-42 uptake from the earliest time points, while other syndecans facilitated A beta 1-42 internalization at a slower pace. Internalized A beta 1-42 colocalized with syndecans and flotillins, highlighting the role of lipid-rafts in syndecan-mediated uptake. Syndecan-3 and 4 also triggered fibrillation of A beta 1-42, further emphasizing the pathophysiological relevance of syndecans in plaque formation. Overall our data highlight syndecans, especially the neuron-specific syndecan-3 isoform, as important players in amyloid pathology and show that syndecans, regardless of cell type, facilitate key molecular events in neurodegeneration.
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<div class="JournalArticle Publication short-list"> <div class="authors"> <span class="author-name" mtid="10025128"> <a href="/gui2/?type=authors&mode=browse&sel=10025128" target="_blank">Letoha, Tamás ✉</a> </span> <span class="author-type"> </span> ; <span class="author-name" > Hudák, Anett </span> <span class="author-type"> </span> ; <span class="author-name" > Kusz, Erzsébet </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10025208"> <a href="/gui2/?type=authors&mode=browse&sel=10025208" target="_blank">Pettkó-Szandtner, Aladár</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10012903"> <a href="/gui2/?type=authors&mode=browse&sel=10012903" target="_blank">Domonkos, Ildikó</a> </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10029111"> <a href="/gui2/?type=authors&mode=browse&sel=10029111" target="_blank">Jósvay, Katalin</a> </span> <span class="author-type"> </span> ; <span class="author-name" > Hofmann-Apitius, Martin </span> <span class="author-type"> </span> ; <span class="author-name" mtid="10026611"> <a href="/gui2/?type=authors&mode=browse&sel=10026611" target="_blank">Szilák, László</a> </span> <span class="author-type"> </span> </div ><div class="title"><a href="/gui2/?mode=browse¶ms=publication;30462206" mtid="30462206" target="_blank">Contribution of syndecans to cellular internalization and fibrillation of amyloid-β (1–42)</a></div> <div class="pub-info"> <span class="journal-title">SCIENTIFIC REPORTS</span> <span class="journal-volume">9</span> : <span class="journal-issue">1</span> <span class="page"> Paper: 1393 , 17 p. </span> <span class="year">(2019)</span> </div> <div class="pub-end"><div class="identifier-list"> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1038/s41598-018-37476-9" target="_blank" href="https://doi.org/10.1038/s41598-018-37476-9"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="000457616300281" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/000457616300281"> WoS </a> </span> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:black" title="103631" target="_blank" href="http://real.mtak.hu/103631"> REAL </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85061065238" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85061065238"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="30718543" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=30718543&dopt=Abstract"> PubMed </a> </span> </span> </div> <div class="short-pub-prop-list"> <span class="short-pub-mtid"> Közlemény:30462206 </span> <span class="status-holder"><span class="status-data status-APPROVED"> Nyilvános </span></span> <span class="pub-core">Forrás Idéző </span> <span class="pub-type">Folyóiratcikk (Szakcikk ) </span> <!-- && !record.category.scientific --> <span class="pub-category">Tudományos</span> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 25</span> | Független: 16 | Függő: 9 | Nem jelölt: 0 | WoS jelölt: 24 | Scopus jelölt: 20 | WoS/Scopus jelölt: 25 | DOI jelölt: 25 </div> </div> </div> </div><div class="JournalArticle Publication long-list">
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<span class="author-affil"><span title="Szegedi Biológiai Kutatóközpont">SZBK</span>/Növénybiológiai Intézet</span>
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<span class="authorAux-mtmt"> molekuláris biológia</span>)
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<span class="author-affil"><span title="Szegedi Biológiai Kutatóközpont">SZBK</span>/Biokémiai Intézet</span>
;
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<span class="author-name" mtid="10026611"><a
href="/gui2/?type=authors&mode=browse&sel=10026611" target="_blank">Szilák László
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<div class="title"><a href="/gui2/?mode=browse¶ms=publication;30462206" target="_blank">Contribution of syndecans to cellular internalization and fibrillation of amyloid-β (1–42)</a></div> <div> <span class="journal-title">SCIENTIFIC REPORTS</span>
<span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/2045-2322">2045-2322</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/2045-2322">2045-2322</a>)</span>:
<span class="journal-volume">9</span> <span class="journal-issue">1</span>
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Paper 1393.
17 p.
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<span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 25</span>
| Független: 16
| Függő: 9
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<div class="mtid"><span class="long-pub-mtid">Közlemény: 30462206</span>
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Forrás Idéző
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<div class="lastModified">Utolsó módosítás: 2023.08.03. 14:37 Pécsi Éva (MTMT Közp 3, admin)
</div>
<pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Pharmacoidea Ltd., Szeged, H-6726, Hungary
Biological Research Centre of the Hungarian Academy of Sciences, Szeged, H-6726, Hungary
Fraunhofer Institute for Algorithms and Scientific Computing (SCAI), Sankt Augustin, 53754, Germany
Szilak Laboratories, Bioinformatics and Molecule-Design, Szeged, H-6723, Hungary
...</pre>
</div></div>