Evidence map›Paper›PMID 27667389›Full record

ArticleJournal of proteomics2017

On-column trypsin digestion coupled with LC-MS/MS for quantification of apolipoproteins.

Christopher A Toth, Zsuzsanna Kuklenyik, Jeffrey I Jones, Bryan A Parks, Michael S Gardner, David M Schieltz, Jon C Rees, Michael L Andrews, Lisa G McWilliams, James L Pirkle and 1 more

Open access · greenAbstract readEvaluation Study
In one paragraph

Article in Journal of proteomics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 53 citations in OpenAlex.

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  7. The small HDL particle hypothesis of Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2023
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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 1 institution in 1 country.

Christopher A TothCenters for Disease Control and Prevention, Division of Laboratory Sciences, Atlanta, GA, United States.
Zsuzsanna KuklenyikCenters for Disease Control and Prevention, Division of Laboratory Sciences, Atlanta, GA, United States. Electronic address: ZKuklenyik@cdc.gov.
Jeffrey I JonesCenters for Disease Control and Prevention, Division of Laboratory Sciences, Atlanta, GA, United States.
Bryan A ParksCenters for Disease Control and Prevention, Division of Laboratory Sciences, Atlanta, GA, United States.
Michael S GardnerCenters for Disease Control and Prevention, Division of Laboratory Sciences, Atlanta, GA, United States.
David M SchieltzCenters for Disease Control and Prevention, Division of Laboratory Sciences, Atlanta, GA, United States.
Jon C ReesCenters for Disease Control and Prevention, Division of Laboratory Sciences, Atlanta, GA, United States.
Michael L AndrewsCenters for Disease Control and Prevention, Division of Laboratory Sciences, Atlanta, GA, United States.
Lisa G McWilliamsCenters for Disease Control and Prevention, Division of Laboratory Sciences, Atlanta, GA, United States.
James L PirkleCenters for Disease Control and Prevention, Division of Laboratory Sciences, Atlanta, GA, United States.
John R BarrCenters for Disease Control and Prevention, Division of Laboratory Sciences, Atlanta, GA, United States.
Centers for Disease Control and Prevention · US

Funding

Intramural CDC HHS CC999999
6 · The paper itself

Abstract

Apolipoproteins measured in plasma or serum are potential biomarkers for assessing metabolic irregularities that are associated with the development of cardiovascular disease (CVD). LC-MS/MS allows quantitative measurement of multiple apolipoproteins in the same sample run. However, the accuracy and precision of the LC-MS/MS measurement depends on the reproducibility of the enzymatic protein digestion step. With the application of an immobilized enzyme reactor (IMER), the reproducibility of the trypsin digestion can be controlled with high precision via flow rate, column volume and temperature. In this report, we demonstrate the application of an integrated IMER-LC-MS/MS platform for the simultaneous quantitative analysis of eight apolipoproteins. Using a dilution series of a characterized serum pool as calibrator, the method was validated by repeated analysis of pooled sera and individual serum samples with a wide range of lipid profiles, all showing intra-assay CV<4.4% and inter-assay CV<8%. In addition, the method was compared with traditional homogeneous digestion coupled LC-MS/MS for the quantification of apoA-I and apoB-100. Applied in large scale human population studies, this method can serve the translation of a wider panel of apolipoprotein biomarkers from research to clinical application. SIGNIFICANCE: Currently, the translation of apolipoprotein biomarkers to clinical application is impaired because of the high cost of large cohort studies using traditional single-analyte immunoassays. The application of on-line tryptic digestion coupled with LC-MS/MS analysis is an effective way to address this problem. In this work we demonstrate a high throughput, multiplexed, automated proteomics workflow for the simultaneous analysis of multiple proteins.

Indexed as

ProteolysisApolipoproteinsBiomarkersBlood Chemical AnalysisBlood ProteinsChromatography, LiquidFeasibility StudiesHumansProteomicsReproducibility of ResultsTandem Mass SpectrometryTrypsinApolipoproteinsBiomarkersBlood ProteinsTrypsin

Identifiers

PMID27667389
PMCPMC10071838
OpenAlexW2523568958

What OpenQuestion holds

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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.