Evidence map›Paper›PMID 30704515›Full record

ArticleActa neuropathologica communications2019

The APMAP interactome reveals new modulators of APP processing and beta-amyloid production that are altered in Alzheimer's disease.

Hermeto Gerber, Sebastien Mosser, Benjamin Boury-Jamot, Michael Stumpe, Alessandra Piersigilli, Christine Goepfert, Joern Dengjel, Urs Albrecht, Fulvio Magara, Patrick C Fraering

Open access · goldAbstract read
In one paragraph

Article in Acta neuropathologica communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  10. Protein Interactome of Amyloid-β as a Therapeutic Target.Pharmaceuticals (Basel, Switzerland) · 2023
    Review
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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

10 authors at 4 institutions in 1 country.

Hermeto GerberFoundation Eclosion, CH-1228, Plan-les-Ouates, Switzerland.
Sebastien MosserFoundation Eclosion, CH-1228, Plan-les-Ouates, Switzerland.
Benjamin Boury-JamotCentre for Psychiatric Neuroscience, Department of Psychiatry, Lausanne University Hospital, CH-1015, Lausanne, Switzerland.
Michael StumpeDepartment of Biology, University of Fribourg, CH-1700, Fribourg, Switzerland.
Alessandra PiersigilliInstitute of Animal Pathology, Vetsuisse Faculty, University of Bern, CH-3012, Bern, Switzerland.
Christine GoepfertInstitute of Animal Pathology, Vetsuisse Faculty, University of Bern, CH-3012, Bern, Switzerland.
Joern DengjelDepartment of Biology, University of Fribourg, CH-1700, Fribourg, Switzerland.
Urs AlbrechtDepartment of Biology, University of Fribourg, CH-1700, Fribourg, Switzerland.
Fulvio MagaraCentre for Psychiatric Neuroscience, Department of Psychiatry, Lausanne University Hospital, CH-1015, Lausanne, Switzerland.
Patrick C FraeringFoundation Eclosion, CH-1228, Plan-les-Ouates, Switzerland. fraeringpatrick@hotmail.com.
University of Fribourg · CHUniversity of Lausanne · CHÉcole Polytechnique Fédérale de Lausanne · CHUniversity of Bern · CH

Funding

THE ROLE OF ADVANCED CAA IN ALZHEIMER'S DEMENTIAP50AG005134 · NIA · MASSACHUSETTS GENERAL HOSPITAL · PI HYMAN, BRADLEY T. · 1985 to 2018
$42.1M
NIA NIH HHS P50 AG005134
6 · The paper itself

Abstract

The adipocyte plasma membrane-associated protein APMAP is expressed in the brain where it associates with γ-secretase, a protease responsible for the generation of the amyloid-β peptides (Aβ) implicated in the pathogenesis of Alzheimer's disease (AD). In this study, behavioral investigations revealed spatial learning and memory deficiencies in our newly generated mouse line lacking the protein APMAP. In a mouse model of AD, the constitutive deletion of APMAP worsened the spatial memory phenotype and led to increased Aβ production and deposition into senile plaques. To investigate at the molecular level the neurobiological functions of APMAP (memory and Aβ formation) and a possible link with the pathological hallmarks of AD (memory impairment and Aβ pathology), we next developed a procedure for the high-grade purification of cellular APMAP protein complexes. The biochemical characterization of these complexes revealed a series of new APMAP interactomers. Among these, the heat shock protein HSPA1A and the cation-dependent mannose-6-phosphate receptor (CD-M6PR) negatively regulated APP processing and Aβ production, while clusterin, calnexin, arginase-1, PTGFRN and the cation-independent mannose-6-phosphate receptor (CI-M6PR/IGF2R) positively regulated APP and Aβ production. Several of the newly identified APMAP interactomers contribute to the autophagy-lysosome system, further supporting an emergent agreement that this pathway can modulate APP metabolism and Aβ generation. Importantly, we have also demonstrated increased alternative splicing of APMAP and lowered levels of the Aβ controllers HSPA1A and CD-M6PR in human brains from neuropathologically verified AD cases.

Indexed as

AgedAged, 80 and overAlzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsBrainCHO CellsCricetulusFemaleFrontal LobeHEK293 CellsHumansMaleMembrane GlycoproteinsMice, Inbred C57BLAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAPMAP protein, mouseMembrane GlycoproteinsProteomeAlternative splicingAlzheimer’s diseaseAPMAP interactomeAPMAP-KOAβ productionLearning and memoryNeurodegeneration

Identifiers

PMID30704515
PMCPMC6354426
OpenAlexW2923683607

What OpenQuestion holds

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LicenceCC BY
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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.