Evidence map›Paper›PMID 22138302›Full record

ArticleBiochimica et biophysica acta2012

Preferential interactions between ApoE-containing lipoproteins and Aβ revealed by a detection method that combines size exclusion chromatography with non-reducing gel-shift.

Mary Jo LaDu, Gregory W Munson, Lisa Jungbauer, Godfrey S Getz, Catherine A Reardon, Leon M Tai, Chunjiang Yu

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Toward refining Alzheimer's disease into overlapping subgroups.Alzheimer's & dementia (New York, N. Y.) · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Age, APOE and sex: Triad of risk of Alzheimer's disease.The Journal of steroid biochemistry and molecular biology · 2016
    Review
  12. Article
  13. Cerebrospinal Fluid Particles in Alzheimer Disease and Parkinson Disease.Journal of neuropathology and experimental neurology · 2015
    Article
  14. Role of apolipoprotein E in neurodegenerative diseases.Neuropsychiatric disease and treatment · 2015
    Review
  15. Review
  16. Review
  17. What are lipoproteins doing in the brain?Trends in endocrinology and metabolism: TEM · 2014
    Article
  18. ApoE influences amyloid-β (Aβ) clearance despite minimal apoE/Aβ association in physiological conditions.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Mary Jo LaDuDepartment of Anatomy and Cell Biology, University of Illinois, Chicago, IL 60612, USA. mladu@uic.edu
Gregory W Munson
Lisa Jungbauer
Godfrey S Getz
Catherine A Reardon
Leon M Tai
Chunjiang Yu
University of Illinois Chicago · USUniversity of Chicago · US

Funding

TRANSGENIC MOUSE COREP01AG030128 · NIA · UNIVERSITY OF ILLINOIS AT CHICAGO · PI ESTUS, STEVEN · 2009 to 2013
$9.4M
Role of Glia in Neuronal Degeneration (Supplemental Application Binder Proj 2)P01AG021184 · NIA · NORTHWESTERN UNIVERSITY AT CHICAGO · PI VAN ELDIK, LINDA J · 2003 to 2007
$7.2M
NIA NIH HHS P01 AG021184NIA NIH HHS P01AG021184NIA NIH HHS P01 AG030128NINDS NIH HHS NS520138
6 · The paper itself

Abstract

The association between apolipoprotein E (apoE) and amyloid-β peptide (Aβ) may significantly impact the function of both proteins, thus affecting the etiology of Alzheimer's disease (AD). However, apoE/Aβ interactions remain fundamentally defined by the stringency of the detection method. Here we use size exclusion chromatography (SEC) as a non-stringent approach to the detection of apoE/Aβ interactions in solution, specifically apoE and both endogenous and exogenous Aβ from plasma, CSF and astrocyte conditioned media. By SEC analysis, Aβ association with plasma and CNS lipoproteins is apoE-dependent. While endogenous Aβ elutes to specific human plasma lipoproteins distinct from those containing apoE, it is the apoE-containing lipoproteins that absorb excess amounts of exogenous Aβ40. In human CSF, apoE, endogenous Aβ and phospholipid elute in an almost identical profile, as do apoE, exogenous Aβ and phospholipid from astrocyte conditioned media. Combining SEC fractionation with subsequent analysis for SDS-stable apoE/Aβ complex reveals that apoE-containing astrocyte lipoproteins exhibit the most robust interactions with Aβ. Thus, standardization of the methods for detecting apoE/Aβ complex is necessary to determine its functional significance in the neuropathology characteristic of AD. Importantly, a systematic understanding of the role of apoE-containing plasma and CNS lipoproteins in Aβ homeostasis could potentially contribute to identifying a plasma biomarker currently over-looked because it has multiple components.

Indexed as

Amyloid beta-PeptidesAnimalsApolipoproteins EAstrocytesChromatography, GelElectrophoresis, Polyacrylamide GelHumansLipoproteinsLipoproteins, HDLProtein BindingRatsRats, Sprague-DawleyAmyloid beta-PeptidesApolipoproteins ELipoproteinsLipoproteins, HDL

Identifiers

PMID22138302
PMCPMC3273043
OpenAlexW2128774494

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.