Evidence map›Paper›PMID 26637294›Full record

ArticleMolecular brain2015

Metallothionein-3 modulates the amyloid β endocytosis of astrocytes through its effects on actin polymerization.

Sook-Jeong Lee, Bo-Ra Seo, Jae-Young Koh

Open access · goldAbstract read
In one paragraph

Article in Molecular brain, 2015. 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
2.7field-weighted citation impact, top 11% 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, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Amyloid-Frontiers in neuroscience · 2026
    Review
  4. Article
  5. Article
  6. Kisspeptin signaling in astrocytes modulates the reproductive axis.The Journal of clinical investigation · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Complement System in Alzheimer's Disease.International journal of molecular sciences · 2021
    Review
  16. Article
  17. Review
  18. Review
  19. Review
  20. Article
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

3 authors at 1 institution in 1 country.

Sook-Jeong LeeNeural Injury Research Center, Asan Institute for Life Sciences, University of Ulsan College of Medicine, Seoul, South Korea. sjlee0102@nate.com.
Bo-Ra SeoNeural Injury Research Center, Asan Institute for Life Sciences, University of Ulsan College of Medicine, Seoul, South Korea. addibora@nate.com.
Jae-Young KohNeural Injury Research Center, Asan Institute for Life Sciences, University of Ulsan College of Medicine, Seoul, South Korea. jkko@amc.seoul.kr.
Ulsan College · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAstrocytes may play important roles in the pathogenesis of Alzheimer's disease (AD) by clearing extracellular amyloid beta (Aβ) through endocytosis and degradation. We recently showed that metallothionein 3 (Mt3), a zinc-binding metallothionein that is enriched in the central nervous system, contributes to actin polymerization in astrocytes. Because actin is likely involved in the endocytosis of Aβ, we investigated the possible role of Mt3 in Aβ endocytosis by cortical astrocytes in this study.

resultsTo assess the route of Aβ uptake, we exposed cultured astrocytes to fluorescently labeled Aβ1-40 or Aβ1-42 together with chloropromazine (CP) or methyl-beta-cyclodextrin (MβCD), inhibitors of clathrin- and caveolin-dependent endocytosis, respectively. CP treatment almost completely blocked Aβ1-40 and Aβ1-42 endocytosis, whereas exposure to MβCD had no significant effect. Actin disruption with cytochalasin D (CytD) or latrunculin B also completely blocked Aβ1-40 and Aβ1-42 endocytosis. Because the absence of Mt3 also results in actin disruption, we examined Aβ1-40 and Aβ1-42 uptake and expression in Mt3 (-/-) astrocytes. Compared with wild-type (WT) cells, Mt3 (-/-) cells exhibited markedly reduced Aβ1-40 and Aβ1-42 endocytosis and expression of Aβ1-42 monomers and oligomers. A similar reduction was observed in CytD-treated WT cells. Finally, actin disruption and Mt3 knockout each increased the overall levels of clathrin and the associated protein phosphatidylinositol-binding clathrin assembly protein (PICALM) in astrocytes.

conclusionsOur results suggest that the absence of Mt3 reduces Aβ uptake in astrocytes through an abnormality in actin polymerization. In light of evidence that Mt3 is downregulated in AD, our findings indicate that this mechanism may contribute to the extracellular accumulation of Aβ in this disease.

Indexed as

EndocytosisPolymerizationActinsAmyloid beta-PeptidesAnimalsAstrocytesBridged Bicyclo Compounds, HeterocyclicCells, CulturedCholera ToxinClathrinCytochalasin DGene DeletionMaleMetallothionein 3MiceMonomeric Clathrin Assembly ProteinsActinsAmyloid beta-PeptidesBridged Bicyclo Compounds, HeterocyclicCholera ToxinClathrinCytochalasin Dlatrunculin BMetallothionein 3Monomeric Clathrin Assembly ProteinsMt3 protein, mouseNerve Tissue ProteinsPICALM protein, mouseThiazolidines

Identifiers

PMID26637294
PMCPMC4670512
OpenAlexW2187526329

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.