Evidence map›Paper›PMID 37533067›Full record

ArticleCell & bioscience2023

APP family member dimeric complexes are formed predominantly in synaptic compartments.

Sandra Schilling, Alexander August, Mathieu Meleux, Carolin Conradt, Luisa M Tremmel, Sandra Teigler, Virginie Adam, Ulrike C Müller, Edward H Koo, Stefan Kins and 1 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell & bioscience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

11 authors at 3 institutions in 2 countries.

Sandra SchillingDepartment of Human Biology and Human Genetics, University of Kaiserslautern, 67663, Kaiserslautern, Germany.
Alexander AugustDepartment of Human Biology and Human Genetics, University of Kaiserslautern, 67663, Kaiserslautern, Germany.
Mathieu MeleuxDepartment of Human Biology and Human Genetics, University of Kaiserslautern, 67663, Kaiserslautern, Germany.
Carolin ConradtDepartment of Human Biology and Human Genetics, University of Kaiserslautern, 67663, Kaiserslautern, Germany.
Luisa M TremmelDepartment of Human Biology and Human Genetics, University of Kaiserslautern, 67663, Kaiserslautern, Germany.
Sandra TeiglerDepartment of Human Biology and Human Genetics, University of Kaiserslautern, 67663, Kaiserslautern, Germany.
Virginie AdamDepartment of Human Biology and Human Genetics, University of Kaiserslautern, 67663, Kaiserslautern, Germany.
Ulrike C MüllerInstitute for Pharmacy and Molecular Biotechnology, University of Heidelberg, 69120, Heidelberg, Germany.
Edward H KooDepartment of Neuroscience, University of California, San Diego (UCSD), La Jolla, CA, 92093-0662, USA.
Stefan Kins *Department of Human Biology and Human Genetics, University of Kaiserslautern, 67663, Kaiserslautern, Germany.
Simone Eggert *Department of Human Biology and Human Genetics, University of Kaiserslautern, 67663, Kaiserslautern, Germany. simone.eggert@mpinat.mpg.de.ORCID http://orcid.org/0000-0002-6792-5556
University of Kaiserslautern · DEHeidelberg University · DEUniversity of California San Diego · US

Funding

Alzheimer Forschung Initiative 19084Deutsche Forschungsgemeinschaft Kl 819/9-1
6 · The paper itself

Abstract

backgroundThe amyloid precursor protein (APP), a key player in Alzheimer's disease (AD), is part of a larger gene family, including the APP like proteins APLP1 and APLP2. They share similar structures, form homo- and heterotypic dimers and exhibit overlapping functions.

resultsWe investigated complex formation of the APP family members via two inducible dimerization systems, the FKBP-rapamycin based dimerization as well as cysteine induced dimerization, combined with co-immunoprecipitations and Blue Native (BN) gel analyses. Within the APP family, APLP1 shows the highest degree of dimerization and high molecular weight (HMW) complex formation. Interestingly, only about 20% of APP is dimerized in cultured cells whereas up to 50% of APP is dimerized in mouse brains, independent of age and splice forms. Furthermore, we could show that dimerized APP originates mostly from neurons and is enriched in synaptosomes. Finally, BN gel analysis of human cortex samples shows a significant decrease of APP dimers in AD patients compared to controls.

conclusionsTogether, we suggest that loss of full-length APP dimers might correlate with loss of synapses in the process of AD.

Indexed as

Alzheimer’s diseaseAmyloid precursor proteinAPLP1APLP2Blue Native gelsDimerizationSynaptosomes

Identifiers

PMID37533067
PMCPMC10398996
OpenAlexW4385491453

What Socratic holds

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LicenceCC BY
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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 Socratic graph.