Evidence map›Paper›PMID 28112871›Full record

ArticleProteomics. Clinical applications2017

Quantification by nano liquid chromatography parallel reaction monitoring mass spectrometry of human apolipoprotein A-I, apolipoprotein B, and hemoglobin A1c in dried blood spots.

Clark M Henderson, James G Bollinger, Jessica O Becker, Jennifer M Wallace, Thomas J Laha, Michael J MacCoss, Andrew N Hoofnagle

Abstract read
In one paragraph

Article in Proteomics. Clinical applications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.

  1. Dried Blood Spots to Assess Cardiovascular-Kidney-Metabolic Health.Journal of the American Heart Association · 2025
    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

7 authors at 2 institutions in 1 country.

Clark M HendersonDepartment of Laboratory Medicine, University of Washington, Seattle, WA, USA.
James G BollingerDepartments of Genome Sciences, University of Washington, Seattle, WA, USA.
Jessica O BeckerDepartment of Laboratory Medicine, University of Washington, Seattle, WA, USA.
Jennifer M WallaceDepartment of Laboratory Medicine, University of Washington, Seattle, WA, USA.
Thomas J LahaDepartment of Laboratory Medicine, University of Washington, Seattle, WA, USA.
Michael J MacCossDepartments of Genome Sciences, University of Washington, Seattle, WA, USA.
Andrew N HoofnagleDepartment of Laboratory Medicine, University of Washington, Seattle, WA, USA.
University of Washington · USUniversity of Washington Applied Physics Laboratory · US

Funding

PILOT STUDY--CLINICAL NUTRITION RESEARCHP30DK035816 · NIDDK · UNIVERSITY OF WASHINGTON · PI Ellen A Schur · 1986 to 2026
$30.4M
Nutrition, Obesity and Atherosclerosis Training ProgramT32HL007028 · NHLBI · UNIVERSITY OF WASHINGTON · PI Karin E Bornfeldt · 1985 to 2026
$6.4M
HDL and cardiovascular risk in chronic kidney diseaseR01HL111375 · NHLBI · UNIVERSITY OF WASHINGTON · PI HOOFNAGLE, ANDREW N · 2012 to 2015
$1.5M
NHLBI NIH HHS R01 HL111375NHLBI NIH HHS T32 HL007028NIDDK NIH HHS P30 DK035816
6 · The paper itself

Abstract

purposeProteomic analysis of blood proteins in dried blood spots (DBS) is gaining attention as a possible replacement for measurements in plasma/serum collected by venipuncture. We aimed to develop and provisionally validate a nanoflow LC-PRM-MS method for clinical use. EXPERIMENTAL

designWe used Skyline to develop a nanoflow LC-PRM-MS method to quantify glycated hemoglobin-β, apolipoprotein A-I, and apolipoprotein B in DBS. Precision, linearity, interferences, and stability were determined and the method was used to analyze samples from 36 human volunteers. The method was compared with clinically validated measurements in paired blood collected via venipuncture.

resultsThe method was relatively precise for these proteins (10-11% CV) and linear across the normal concentration ranges of these proteins. Interference from high total serum protein concentration (>8 g/dL) was noted for apolipoprotein A-I and apolipoprotein B. Proteins in DBS were stable for 14 days at temperatures below 25°C and trypsinized samples were stable for 48 h at 7°C. There was moderate correlation with clinical methods (r = 0.783-0.858) and significant bias in individual samples. CONCLUSIONS AND CLINICAL RELEVANCE: Although the method had adequate precision and linearity for a biomarker, the accuracy compared with clinically validated assays raises concerns regarding the use of DBS compared with venipuncture for clinical use.

Indexed as

Apolipoprotein A-IApolipoproteins BCalibrationChromatography, LiquidDried Blood Spot TestingGlycated HemoglobinHumansMass SpectrometryNanotechnologyProteomicsApolipoprotein A-IApolipoproteins BGlycated HemoglobinApolipoproteinsBiomarkersDiabetesDried blood spotsLC-MS/MSMethod evaluationMultiplexingProvisional validationQuantification

Identifiers

PMID28112871
PMCPMC5501987
OpenAlexW2581357643

What OpenQuestion holds

Textmetadata
LicenceTDM
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.