Evidence map›Paper›PMID 29588628›Full record

ArticleClinical proteomics2018

A robust mass spectrometry method for rapid profiling of erythrocyte ghost membrane proteomes.

Haddy K S Fye, Paul Mrosso, Lesley Bruce, Marie-Laëtitia Thézénas, Simon Davis, Roman Fischer, Gration L Rwegasira, Julie Makani, Benedikt M Kessler

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Clinical proteomics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

10 citing papers in PubMed, 26 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

9 authors at 3 institutions in 2 countries.

Haddy K S Fye1Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ UK.ORCID 0000-0001-5597-3975
Paul Mrosso2Muhimbili Wellcome Programme, Muhimbili University of Health and Allied Sciences, PO Box 65001, Dar es Salaam, Tanzania.
Lesley Bruce3Bristol Institute for Transfusion Sciences, NHS Blood and Transplant, 500 North Bristol Park, Filton, Bristol, BS34 7QH UK.
Marie-Laëtitia Thézénas1Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ UK.
Simon Davis1Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ UK.
Roman Fischer1Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ UK.
Gration L Rwegasira2Muhimbili Wellcome Programme, Muhimbili University of Health and Allied Sciences, PO Box 65001, Dar es Salaam, Tanzania.
Julie Makani2Muhimbili Wellcome Programme, Muhimbili University of Health and Allied Sciences, PO Box 65001, Dar es Salaam, Tanzania.
Benedikt M Kessler1Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ UK.
University of Oxford · GBMuhimbili University of Health and Allied Sciences · TZNHS Blood and Transplant · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundRed blood cell (RBC) physiology is directly linked to many human disorders associated with low tissue oxygen levels or anemia including chronic obstructive pulmonary disease, congenital heart disease, sleep apnea and sickle cell anemia. Parasites such as

methodsHere, we describe an optimised erythrocyte isolation protocol from blood, tested for various storage conditions and explored using different fractionation conditions for isolating ghost RBC membranes. Liquid chromatography mass spectrometry (LC-MS) analysis on a Q-Exactive Orbitrap instrument was used to profile proteins isolated from the comparative conditions. Data analysis was run on the MASCOT and MaxQuant platforms to assess their scope and diversity.

resultsThe results obtained demonstrate a robust method for membrane enrichment enabling consistent MS based characterisation of > 900 RBC membrane proteins in single LC-MS/MS analyses. Non-detergent based membrane solubilisation methods using the tissue and supernatant fractions of isolated ghost membranes are shown to offer effective haemoglobin removal as well as diverse recovery including erythrocyte membrane proteins of high and low abundance.

conclusionsThe methods described in this manuscript propose a medium to high throughput framework for membrane proteome profiling by LC-MS of potential applicability to larger clinical cohorts in a variety of disease contexts.

Indexed as

Erythrocyte ghostsHaemoglobinopathiesMembrane proteomeShotgun proteomicsTandem mass spectrometry

Identifiers

PMID29588628
PMCPMC5863380
OpenAlexW2789567874

What OpenQuestion holds

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Registered trials

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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.