Evidence map›Paper›PMID 30718543›Full record

ArticleScientific reports2019

Contribution of syndecans to cellular internalization and fibrillation of amyloid-β(1-42).

Tamás Letoha, Anett Hudák, Erzsébet Kusz, Aladár Pettkó-Szandtner, Ildikó Domonkos, Katalin Jósvay, Martin Hofmann-Apitius, László Szilák

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.9field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Article
  3. Glycocalyx and basal lamina in neurological disorders.Matrix biology : journal of the International Society for Matrix Biology · 2026
    Review
  4. Article
  5. Assessing Aβ-independent effects of Module 42 on immune function in vitro.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Tamás LetohaPharmacoidea Ltd., Szeged, H-6726, Hungary. tamas.letoha@pharmacoidea.eu.ORCID 0000-0002-6035-4009
Anett HudákPharmacoidea Ltd., Szeged, H-6726, Hungary.
Erzsébet KuszPharmacoidea Ltd., Szeged, H-6726, Hungary.
Aladár Pettkó-SzandtnerBiological Research Centre of the Hungarian Academy of Sciences, Szeged, H-6726, Hungary.
Ildikó DomonkosBiological Research Centre of the Hungarian Academy of Sciences, Szeged, H-6726, Hungary.
Katalin JósvayBiological Research Centre of the Hungarian Academy of Sciences, Szeged, H-6726, Hungary.
Martin Hofmann-ApitiusFraunhofer Institute for Algorithms and Scientific Computing (SCAI), Sankt Augustin, 53754, Germany.ORCID 0000-0001-9012-6720
László SzilákSzilak Laboratories, Bioinformatics and Molecule-Design, Szeged, H-6723, Hungary.
HUN-REN Szegedi Biológiai Kutatóközpont · HUFraunhofer Institute for Algorithms and Scientific Computing · DEMTA-SZTE Research Group on Artificial Intelligence · HUUniversity of Szeged · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intraneuronal accumulation of amyloid-β(1-42) (Aβ1-42) 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 Aβ1-42 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 Aβ1-42. Among syndecans, the neuron specific syndecan-3 isoform increased cellular uptake of Aβ1-42 the most. Kinetics of Aβ1-42 uptake also proved to be fairly different among SDC family members: syndecan-3 increased Aβ1-42 uptake from the earliest time points, while other syndecans facilitated Aβ1-42 internalization at a slower pace. Internalized Aβ1-42 colocalized with syndecans and flotillins, highlighting the role of lipid-rafts in syndecan-mediated uptake. Syndecan-3 and 4 also triggered fibrillation of Aβ1-42, 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.

Indexed as

EndocytosisAmyloid beta-PeptidesCell LineHumansK562 CellsKineticsMembrane MicrodomainsMembrane ProteinsNeuronsPeptide FragmentsProtein DomainsSyndecansAmyloid beta-Peptidesamyloid beta-protein (1-42)flotillinsMembrane ProteinsPeptide FragmentsSyndecans

Identifiers

PMID30718543
PMCPMC6362000
OpenAlexW2911426481

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.