Evidence map›Paper›PMID 31083443›Full record

ArticleInternational journal of molecular sciences2019

Multiple Glycation Sites in Blood Plasma Proteins as an Integrated Biomarker of Type 2 Diabetes Mellitus.

Alena Soboleva, Gregory Mavropulo-Stolyarenko, Tatiana Karonova, Domenika Thieme, Wolfgang Hoehenwarter, Christian Ihling, Vasily Stefanov, Tatiana Grishina, Andrej Frolov

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.3field-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

24 citing papers in PubMed, 45 citations in OpenAlex.

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  19. Integrative Role of Albumin: Evolutionary, Biochemical and Pathophysiological Aspects.Journal of evolutionary biochemistry and physiology · 2021
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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 4 institutions in 2 countries.

Alena SobolevaDepartment of Biochemistry, St. Petersburg State University, 199034 Saint Petersburg, Russia. st021585@student.spbu.ru.ORCID 0000-0002-7318-8628
Gregory Mavropulo-StolyarenkoDepartment of Biochemistry, St. Petersburg State University, 199034 Saint Petersburg, Russia. gm2124@mail.ru.
Tatiana KaronovaAlmazov National Medical Research Centre, 197341 Saint Petersburg, Russia. karonova@mail.ru.
Domenika ThiemeProteome Analytics Research Group, Leibniz Institute of Plant Biochemistry, D-06120 Halle (Saale), Germany. Domenika.Thieme@ipb-halle.de.
Wolfgang HoehenwarterProteome Analytics Research Group, Leibniz Institute of Plant Biochemistry, D-06120 Halle (Saale), Germany. Wolfgang.Hoehenwarter@ipb-halle.de.ORCID 0000-0002-7669-7524
Christian IhlingInstitute of Pharmacy, Martin Luther University of Halle-Wittenberg, D-06120 Halle (Saale), Germany. christian.ihling@pharmazie.uni-halle.de.
Vasily StefanovDepartment of Biochemistry, St. Petersburg State University, 199034 Saint Petersburg, Russia. vastef@mail.ru.
Tatiana GrishinaDepartment of Biochemistry, St. Petersburg State University, 199034 Saint Petersburg, Russia. tgrishina@mail.ru.ORCID 0000-0002-5306-2980
Andrej FrolovDepartment of Biochemistry, St. Petersburg State University, 199034 Saint Petersburg, Russia. afrolov@ipb-halle.de.
St Petersburg University · RULeibniz Institute of Plant Biochemistry · DEFirst Pavlov State Medical University of St. Petersburg · RUMartin Luther University Halle-Wittenberg · DE

Funding

Russian Foundation for Basic Research 18-34-00927Saint Petersburg State University 28223644
6 · The paper itself

Abstract

Type 2 diabetes mellitus (T2DM) is one of the most widely spread metabolic diseases. Because of its asymptomatic onset and slow development, early diagnosis and adequate glycaemic control are the prerequisites for successful T2DM therapy. In this context, individual amino acid residues might be sensitive indicators of alterations in blood glycation levels. Moreover, due to a large variation in the half-life times of plasma proteins, a generalized biomarker, based on multiple glycation sites, might provide comprehensive control of the glycemic status across any desired time span. Therefore, here, we address the patterns of glycation sites in highly-abundant blood plasma proteins of T2DM patients and corresponding age- and gender-matched controls by comprehensive liquid chromatography-mass spectrometry (LC-MS). The analysis revealed 42 lysyl residues, significantly upregulated under hyperglycemic conditions. Thereby, for 32 glycation sites, biomarker behavior was demonstrated here for the first time. The differentially glycated lysines represented nine plasma proteins with half-lives from 2 to 21 days, giving access to an integrated biomarker based on multiple protein-specific Amadori peptides. The validation of this biomarker relied on linear discriminant analysis (LDA) with random sub-sampling of the training set and leave-one-out cross-validation (LOOCV), which resulted in an accuracy, specificity, and sensitivity of 92%, 100%, and 85%, respectively.

Indexed as

Amino Acid SequenceBiomarkersBlood ProteinsDiabetes Mellitus, Type 2Discriminant AnalysisGlycosylationHalf-LifeHumansPeptidesPrincipal Component AnalysisTrypsinBiomarkersBlood ProteinsPeptidesTrypsinAmadori compoundsbiomarkersglycationglycation siteslabel-free quantificationlinear discriminant analysismass spectrometryplasma proteinstype 2 diabetes mellitus

Identifiers

PMID31083443
PMCPMC6539793
OpenAlexW2944374577

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.