Evidence map›Paper›PMID 19366591›Full record

ArticleBiochimica et biophysica acta2009

The interaction of beta-amyloid protein with cellular membranes stimulates its own production.

Imke Peters, Urule Igbavboa, Tanja Schütt, Schamim Haidari, Ulrike Hartig, Ximena Rosello, Steffi Böttner, Ekaterini Copanaki, Thomas Deller, Donat Kögel and 3 more

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 90 citations in OpenAlex.

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  11. Hexahydropyrrolo[2,3-ACS chemical neuroscience · 2019
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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

13 authors at 2 institutions in 2 countries.

Imke PetersDepartment of Pharmacology, Goethe-University of Frankfurt am Main, Campus Riedberg, Biocenter Geb. N260, R.1.09, Max-von-Laue Str. 9, D-60438 Frankfurt, Germany.
Urule Igbavboa
Tanja Schütt
Schamim Haidari
Ulrike Hartig
Ximena Rosello
Steffi Böttner
Ekaterini Copanaki
Thomas Deller
Donat Kögel
W Gibson Wood
Walter E Müller
Gunter P Eckert
Goethe University Frankfurt · DEUniversity of Minnesota · US

Funding

PATHOGENESIS OF PHOSPHOLIPASES A2 IN ADP01AG018357 · NIA · UNIVERSITY OF MISSOURI-COLUMBIA · PI SUN, GRACE Y · 2001 to 2012
$10.4M
Amyloid Beta-Protein: ApoE and Cholesterol HomeostasisR01AG023524 · NIA · UNIVERSITY OF MINNESOTA TWIN CITIES · PI WOOD, WELLINGTON GIBSON · 2005 to 2009
$1.2M
NIA NIH HHS AG-18357NIA NIH HHS AG-23524NIA NIH HHS P01 AG018357NIA NIH HHS R01 AG023524
6 · The paper itself

Abstract

Gradual changes in steady-state levels of beta amyloid peptides (Abeta) in brain are considered an initial step in the amyloid cascade hypothesis of Alzheimer's disease. Abeta is a product of the secretase cleavage of amyloid precursor protein (APP). There is evidence that the membrane lipid environment may modulate secretase activity and alters its function. Cleavage of APP strongly depends on membrane properties. Since Abeta perturbs cell membrane fluidity, the cell membrane may be the location where the neurotoxic cascade of Abeta is initiated. Therefore, we tested effects of oligomeric Abeta on membrane fluidity of whole living cells, the impact of exogenous and cellular Abeta on the processing of APP and the role of GM-1 ganglioside. We present evidence that oligoAbeta((1-40)) stimulates the amyloidogenic processing of APP by reducing membrane fluidity and complexing with GM-1 ganglioside. This dynamic action of Abeta may start a vicious circle, where endogenous Abeta stimulates its own production. Based on our novel findings, we propose that oligoAbeta((1-40)) accelerates the proteolytic cleavage of APP by decreasing membrane fluidity.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAnimalsBiophysical PhenomenaCell LineCell MembraneCholesterolG(M1) GangliosideHumansMembrane FluidityMembrane LipidsMiceMicroscopy, ConfocalPeptide FragmentsAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)Amyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesCholesterolG(M1) GangliosideMembrane LipidsPeptide Fragments

Identifiers

PMID19366591
PMCPMC2674130
OpenAlexW2027846974

What OpenQuestion holds

Textmetadata
LicenceTDM
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.