Evidence map›Paper›PMID 25689831›Full record

ArticleProteomics. Clinical applications2016

Affinity proteomics discovers decreased levels of AMFR in plasma from Osteoporosis patients.

Ulrika Qundos, Kimi Drobin, Cecilia Mattsson, Mun-Gwan Hong, Ronald Sjöberg, Björn Forsström, David Solomon, Mathias Uhlén, Peter Nilsson, Karl Michaëlsson and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Proteomics. Clinical applications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 2 pooled it
1.2field-weighted citation impact, top 22% 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

11 citing papers in PubMed, 2 syntheses or guidelines pooled it, 17 citations in OpenAlex.

  1. Pooled it
  2. P4 medicine and osteoporosis: a systematic review.Wiener klinische Wochenschrift · 2016
    Pooled it
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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

11 authors at 3 institutions in 1 country.

Ulrika QundosAffinity Proteomics, SciLifeLab, KTH-Royal Institute of Technology, Solna, Sweden.
Kimi DrobinAffinity Proteomics, SciLifeLab, KTH-Royal Institute of Technology, Solna, Sweden.
Cecilia MattssonAffinity Proteomics, SciLifeLab, KTH-Royal Institute of Technology, Solna, Sweden.
Mun-Gwan HongAffinity Proteomics, SciLifeLab, KTH-Royal Institute of Technology, Solna, Sweden.
Ronald SjöbergAffinity Proteomics, SciLifeLab, KTH-Royal Institute of Technology, Solna, Sweden.
Björn ForsströmAffinity Proteomics, SciLifeLab, KTH-Royal Institute of Technology, Solna, Sweden.
David SolomonAffinity Proteomics, SciLifeLab, KTH-Royal Institute of Technology, Solna, Sweden.
Mathias UhlénAffinity Proteomics, SciLifeLab, KTH-Royal Institute of Technology, Solna, Sweden.
Peter NilssonAffinity Proteomics, SciLifeLab, KTH-Royal Institute of Technology, Solna, Sweden.
Karl MichaëlssonDepartment of Surgical Sciences, Section of Orthopedics, Uppsala University, Uppsala, Sweden.
Jochen M SchwenkAffinity Proteomics, SciLifeLab, KTH-Royal Institute of Technology, Solna, Sweden.
KTH Royal Institute of Technology · SEScience for Life Laboratory · SEUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeAffinity proteomic approaches by antibody bead arrays enable multiplexed analysis of proteins in body fluids. In the presented study, we investigated blood plasma within osteoporosis to discovery differential protein profiles and to propose novel biomarkers candidates for subsequent studies. EXPERIMENTAL

designStarting with 4608 antibodies and plasma samples from 22 women for an untargeted screening, a set of 72 proteins were suggested for further analysis. Complementing these with targets from literature and other studies, a targeted bead array of 180 antibodies was built to profile for 92 proteins in plasma samples of 180 women from two independent population-based studies.

resultsDifferential profiles between osteoporosis patients and matched controls were discovered for 12 proteins in at least one of the two study sets. Among these targets, the levels of autocrine motility factor receptor (AMFR) were concordantly lower in plasma of female osteoporosis patients. Subsequently, verification of anti-AMFR antibody selectivity was conducted using high-density peptide and protein arrays, and Western blotting. CONCLUSIONS AND CLINICAL RELEVANCE: Further validation in additional study sets will be needed to determine the clinical value of the observed decrease in AMFR plasma levels in osteoporosis patients, but AMFR may aid our understanding of disease mechanisms and could support existing tools for diagnosis and monitoring of patient mobility within osteoporosis.

Indexed as

AgedAmino Acid SequenceAntibodiesAntibody SpecificityBiomarkersCase-Control StudiesFemaleGene ExpressionHumansMiddle AgedOsteoporosisProtein Array AnalysisProteomicsReceptors, Autocrine Motility FactorAMFR protein, humanAntibodiesBiomarkersReceptors, Autocrine Motility FactorAntibody bead arraysBiomarker discoveryOsteoporosisPlasma

Identifiers

PMID25689831
PMCPMC5029581
OpenAlexW1972760195

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.