Evidence map›Paper›PMID 29530923›Full record

ArticleMolecular and cellular biology2018

Endosomal-Lysosomal Cholesterol Sequestration by U18666A Differentially Regulates Amyloid Precursor Protein (APP) Metabolism in Normal and APP-Overexpressing Cells.

J Chung, G Phukan, D Vergote, A Mohamed, M Maulik, M Stahn, R J Andrew, G Thinakaran, E Posse de Chaves, S Kar

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 16 citations in OpenAlex.

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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 2 institutions in 2 countries.

J ChungCentre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta, Canada.
G PhukanCentre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta, Canada.
D VergoteFaculté Saint-Jean, University of Alberta, Edmonton, Alberta, Canada.
A MohamedDepartment of Pharmacology, University of Alberta, Edmonton, Alberta, Canada.
M MaulikCentre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta, Canada.
M StahnCentre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta, Canada.
R J AndrewDepartments of Neurobiology, Neurology, and Pathology, The University of Chicago, Chicago, Illinois, USA.
G ThinakaranDepartments of Neurobiology, Neurology, and Pathology, The University of Chicago, Chicago, Illinois, USA.
E Posse de ChavesDepartment of Pharmacology, University of Alberta, Edmonton, Alberta, Canada.
S KarCentre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta, Canada skar@ualberta.ca.
University of Alberta · CAUniversity of Chicago · US

Funding

STRUCTURAL AND FUNCTIONAL ANALYSIS OF PRESENILINSR01AG019070 · NIA · UNIVERSITY OF CHICAGO · PI THINAKARAN, GOPAL · 2001 to 2015
$4.9M
CIHR MOP-123258CIHR MOP-93738NIA NIH HHS R01 AG019070
6 · The paper itself

Abstract

Amyloid β (Aβ) peptide, derived from amyloid precursor protein (APP), plays a critical role in the development of Alzheimer's disease. Current evidence indicates that altered levels or subcellular distribution of cholesterol can regulate Aβ production and clearance, but it remains unclear how cholesterol sequestration within the endosomal-lysosomal (EL) system can influence APP metabolism. Thus, we evaluated the effects of U18666A, which triggers cholesterol redistribution within the EL system, on mouse N2a cells expressing different levels of APP in the presence or absence of extracellular cholesterol and lipids provided by fetal bovine serum (FBS). Our results reveal that U18666A and FBS differentially increase the levels of APP and its cleaved products, the α-, β-, and η-C-terminal fragments, in N2a cells expressing normal levels of mouse APP (N2awt), higher levels of human wild-type APP (APPwt), or "Swedish" mutant APP (APPsw). The cellular levels of Aβ

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesAndrostenesAspartic Acid EndopeptidasesCells, CulturedCholesterolEndosomesHumansLysosomes3-beta-(2-(diethylamino)ethoxy)androst-5-en-17-oneAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesAndrostenesAspartic Acid EndopeptidasesCholesterolAlzheimer's diseaseamyloid precursor proteindelipidationendosomal-lysosomal systemlipid raftβ-amyloidβ-secretaseγ-secretase

Identifiers

PMID29530923
PMCPMC5954187
OpenAlexW2792248701

What OpenQuestion holds

Textmetadata
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.