Evidence map›Paper›PMID 30045733›Full record

ArticleJournal of neuroinflammation2018

Levels of ADAM10 are reduced in Alzheimer's disease CSF.

Aitana Sogorb-Esteve, María-Salud García-Ayllón, Johan Gobom, Jordi Alom, Henrik Zetterberg, Kaj Blennow, Javier Sáez-Valero

Open access · goldAbstract read
In one paragraph

Article in Journal of neuroinflammation, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 45 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

7 authors at 2 institutions in 3 countries.

Aitana Sogorb-EsteveInstituto de Neurociencias de Alicante, Universidad Miguel Hernández-CSIC, Av. Ramón y Cajal s/n, Sant Joan d'Alacant, E-03550, Alicante, Spain.
María-Salud García-AyllónInstituto de Neurociencias de Alicante, Universidad Miguel Hernández-CSIC, Av. Ramón y Cajal s/n, Sant Joan d'Alacant, E-03550, Alicante, Spain.
Johan GobomClinical Neurochemistry Laboratory, Sahlgrenska University Hospital, Mölndal, Sweden.
Jordi AlomCentro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED), Sant Joan d'Alacant, Spain.
Henrik ZetterbergClinical Neurochemistry Laboratory, Sahlgrenska University Hospital, Mölndal, Sweden.
Kaj BlennowClinical Neurochemistry Laboratory, Sahlgrenska University Hospital, Mölndal, Sweden.
Javier Sáez-ValeroInstituto de Neurociencias de Alicante, Universidad Miguel Hernández-CSIC, Av. Ramón y Cajal s/n, Sant Joan d'Alacant, E-03550, Alicante, Spain. j.saez@umh.es.ORCID http://orcid.org/0000-0001-7480-320X
Biomedical Research Networking Center on Neurodegenerative Diseases · ESSahlgrenska University Hospital · SE

Funding

Instituto de Salud Carlos III PI11/03026Instituto de Salud Carlos III PI15/00665Ministerio de Economía y Competitividad SEV-2013-0317
6 · The paper itself

Abstract

backgroundThe disintegrin metalloproteinase 10 (ADAM10) is the main α-secretase acting in the non-amyloidogenic processing of the amyloid precursor protein. This study assesses whether ADAM10 is present in cerebrospinal fluid (CSF), and whether it has potential as a biomarker for Alzheimer's disease (AD).

methodsADAM10 was characterized in human CSF samples by immunoprecipitation and western blotting using antibodies specific for different domains of the protein and by ultracentrifugation in sucrose density gradients. Samples from AD patients (n = 20) and age-matched non-AD controls (n = 20) were characterized for classical CSF biomarkers, Aβ42, T-tau, or P-tau by ELISA, and assayed for soluble ADAM10 levels by western blotting.

resultsWe found that ADAM10 is present in human CSF as several distinct species: an immature form retaining the prodomain (proADAM10; ~ 80 kDa), a mature unprocessed full-length form (ADAM10f; ~ 55 kDa), and a truncated large soluble form released from the membrane (sADAM10; ~ 50 kDa). Fractionation by ultracentrifugation on sucrose density gradients showed that the ADAM10f and sADAM10 species form large complexes. Immunoblotting revealed a significant decrease in ADAM10f and sADAM10 in AD CSF compared to control CSF, while proADAM10 levels remained unaltered.

conclusionsSeveral forms of ADAM10 are present in CSF, mainly assembled as high-molecular weight complexes. The determination of the levels of mature forms of CSF-ADAM10 may be useful as a biomarker for AD.

Indexed as

ADAM10 ProteinAgedAged, 80 and overAlzheimer DiseaseAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesAnimalsCell FractionationCHO CellsCricetulusCulture Media, ConditionedFemaleHumansMaleMembrane ProteinsMiddle AgedADAM10 ProteinADAM10 protein, humanAmyloid beta-Peptidesamyloid beta-protein (1-42)Amyloid Precursor Protein SecretasesCulture Media, ConditionedMembrane ProteinsPeptide Fragmentstau Proteins

Identifiers

PMID30045733
PMCPMC6060469
OpenAlexW2883693583

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.