Evidence map›Paper›PMID 24358169›Full record

ArticlePloS one2013

Soluble β-amyloid Precursor Protein Alpha binds to p75 neurotrophin receptor to promote neurite outgrowth.

Noriko Hasebe, Yuki Fujita, Masaki Ueno, Kazuhiro Yoshimura, Yuji Fujino, Toshihide Yamashita

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 48 citations in OpenAlex.

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  14. Filling the void: a role for exercise-induced BDNF and brain amyloid precursor protein processing.American journal of physiology. Regulatory, integrative and comparative physiology · 2017
    Review
  15. Amyloid precursor protein in pancreatic islets.The Journal of endocrinology · 2017
    Article
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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

6 authors at 2 institutions in 2 countries.

Noriko HasebeDepartment of Molecular Neuroscience, Graduate School of Medicine, Osaka University, Osaka, Japan ; Department of Anesthesiology and Critical Care Medicine, Graduate School of Medicine, Osaka University, Osaka, Japan ; Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Tokyo, Japan.
Yuki FujitaDepartment of Molecular Neuroscience, Graduate School of Medicine, Osaka University, Osaka, Japan ; Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Tokyo, Japan.
Masaki UenoDepartment of Molecular Neuroscience, Graduate School of Medicine, Osaka University, Osaka, Japan ; Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Tokyo, Japan ; Division of Developmental Biology, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, United States of America.
Kazuhiro YoshimuraDepartment of Molecular Neuroscience, Graduate School of Medicine, Osaka University, Osaka, Japan ; Department of Neurosurgery, Graduate School of Medicine, Osaka University, Osaka, Japan.
Yuji FujinoDepartment of Anesthesiology and Critical Care Medicine, Graduate School of Medicine, Osaka University, Osaka, Japan.
Toshihide YamashitaDepartment of Molecular Neuroscience, Graduate School of Medicine, Osaka University, Osaka, Japan ; Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Tokyo, Japan.
Osaka University · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe cleavage of β-amyloid precursor protein (APP) generates multiple proteins: Soluble β-amyloid Precursor Protein Alpha (sAPPα), sAPPβ, and amyloid β (Aβ). Previous studies have shown that sAPPα and sAPPβ possess neurotrophic properties, whereas Aβ is neurotoxic. However, the underlying mechanism of the opposing effects of APP fragments remains poorly understood. In this study, we have investigated the mechanism of sAPPα-mediated neurotrophic effects. sAPPα and sAPPβ interact with p75 neurotrophin receptor (p75(NTR)), and sAPPα promotes neurite outgrowth. METHODS AND

findingsFirst, we investigated whether APP fragments interact with p75(NTR), because full-length APP and Aβ have been shown to interact with p75(NTR) in vitro. Both sAPPα and sAPPβ were co-immunoprecipitated with p75(NTR) and co-localized with p75(NTR) on COS-7 cells. The binding affinity of sAPPα and sAPPβ for p75(NTR) was confirmed by enzyme-linked immunosorbent assay (ELISA). Next, we investigated the effect of sAPPα on neurite outgrowth in mouse cortical neurons. Neurite outgrowth was promoted by sAPPα, but sAPPα was uneffective in a knockdown of p75(NTR).

conclusionWe conclude that p75(NTR) is the receptor for sAPPα to mediate neurotrophic effects.

Indexed as

Amyloid beta-Protein PrecursorAnimalsCerebral CortexChlorocebus aethiopsCOS CellsMiceNeuritesNeuronsReceptor, Nerve Growth FactorAmyloid beta-Protein PrecursorReceptor, Nerve Growth Factor

Identifiers

PMID24358169
PMCPMC3864954
OpenAlexW2141605428

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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.