Evidence map›Paper›PMID 30817799›Full record

ArticlePloS one2019

Human cerebrospinal fluid 6E10-immunoreactive protein species contain amyloid precursor protein fragments.

Marianne K O Grant, Maureen Handoko, Malgorzata Rozga, Gunnar Brinkmalm, Erik Portelius, Kaj Blennow, Karen H Ashe, Kathleen R Zahs, Peng Liu

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

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  5. Towards a Unitary Hypothesis of Alzheimer's Disease Pathogenesis.Journal of Alzheimer's disease : JAD · 2024
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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

9 authors at 4 institutions in 2 countries.

Marianne K O GrantDepartment of Neurology, University of Minnesota, Minneapolis, Minnesota, United States of America.
Maureen HandokoDepartment of Neurology, University of Minnesota, Minneapolis, Minnesota, United States of America.
Malgorzata RozgaInstitute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at University of Gothenburg, Mölndal, Sweden.
Gunnar BrinkmalmInstitute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at University of Gothenburg, Mölndal, Sweden.
Erik PorteliusInstitute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at University of Gothenburg, Mölndal, Sweden.
Kaj BlennowInstitute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at University of Gothenburg, Mölndal, Sweden.
Karen H AsheDepartment of Neurology, University of Minnesota, Minneapolis, Minnesota, United States of America.
Kathleen R ZahsDepartment of Neurology, University of Minnesota, Minneapolis, Minnesota, United States of America.
Peng LiuDepartment of Neurology, University of Minnesota, Minneapolis, Minnesota, United States of America.
Berman Center for Outcomes and Clinical Research · USUniversity of Gothenburg · SEUniversity of Minnesota · USSahlgrenska University Hospital · SE

Funding

TOWARD A MODEL OF ALZHEIMERS DISEASER01NS033249 · NINDS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI ASHE, KAREN H · 1994 to 2013
$6.5M
Specific amyloid-beta oligomer aptamersRC1AG035870 · NIA · UNIVERSITY OF MINNESOTA · PI ASHE, KAREN H · 2009 to 2010
$739k
NIA NIH HHS RC1 AG035870NINDS NIH HHS R01 NS033249
6 · The paper itself

Abstract

In a previous study, we reported that levels of two types of protein species-a type of ~55-kDa species and a type of ~15-kDa species-are elevated in the lumbar cerebrospinal fluid (CSF) of cognitively intact elderly individuals who are at risk for Alzheimer's disease (AD). These species are immunoreactive to the monoclonal antibody 6E10, which is directed against amino acids 6-10 of amyloid-β (Aβ), and their levels correlate with levels of total tau and tau phosphorylated at Thr181. In this study, we investigated the molecular composition of these AD-related proteins using immunoprecipitation (IP)/Western blotting coupled with IP/mass spectrometry. We show that canonical Aβ1-40/42 peptides, together with amyloid-β precursor protein (APP) fragments located N-terminally of Aβ, are present in the ~55-kDa, 6E10-immunoreactive species. We demonstrate that APP fragments located N-terminally of Aβ, plus the N-terminal region of Aβ, are present in the ~15-kDa, 6E10-immunoreactive species. These findings add to the catalog of AD-related Aβ/APP species found in CSF and should motivate further study to determine whether these species may serve as biomarkers of disease progression.

Indexed as

AgedAged, 80 and overAlzheimer DiseaseAmino Acid SequenceAmyloid beta-PeptidesBiomarkersBlotting, WesternDisease ProgressionFemaleHumansImmunoprecipitationMaleMass SpectrometryMiddle AgedMolecular WeightPeptide FragmentsAmyloid beta-PeptidesBiomarkersPeptide Fragments

Identifiers

PMID30817799
PMCPMC6394962
OpenAlexW2918191744

What OpenQuestion holds

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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 OpenQuestion graph.