Evidence map›Paper›PMID 26023067›Full record

ArticleMolecular & cellular proteomics : MCP2015

Development of Diagnostic Fragment Ion Library for Glycated Peptides of Human Serum Albumin: Targeted Quantification in Prediabetic, Diabetic, and Microalbuminuria Plasma by Parallel Reaction Monitoring, SWATH, and MSE.

Arvind M Korwar, Garikapati Vannuruswamy, Mashanipalya G Jagadeeshaprasad, Ramesha H Jayaramaiah, Shweta Bhat, Bhaskaran S Regin, Sureshkumar Ramaswamy, Ashok P Giri, Viswanathan Mohan, Muthuswamy Balasubramanyam and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

19 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Comprehensive Quantification of Carboxymethyllysine-Modified Peptides in Human Plasma.Journal of the American Society for Mass Spectrometry · 2021
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Notch2 and Proteomic Signatures in Mouse Neointimal Lesion Formation.Arteriosclerosis, thrombosis, and vascular biology · 2018
    Article
  12. Article
  13. Article
  14. Maillard Proteomics: Opening New Pages.International journal of molecular sciences · 2017
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
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 2 institutions in 1 country.

Arvind M KorwarFrom the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;
Garikapati VannuruswamyFrom the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;
Mashanipalya G JagadeeshaprasadFrom the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;
Ramesha H JayaramaiahFrom the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;
Shweta BhatFrom the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;
Bhaskaran S Regin‡Madras Diabetes Research Foundation, Chennai- 600 086, India.
Sureshkumar RamaswamyFrom the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;
Ashok P GiriFrom the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.;
Viswanathan Mohan‡Madras Diabetes Research Foundation, Chennai- 600 086, India.
Muthuswamy Balasubramanyam‡Madras Diabetes Research Foundation, Chennai- 600 086, India.
Mahesh J KulkarniFrom the §Mass-Spectrometry and Proteomics Facility, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune-411008, India.; mj.kulkarni@ncl.res.in.
National Chemical Laboratory · INMadras Diabetes Research Foundation · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human serum albumin is one of the most abundant plasma proteins that readily undergoes glycation, thus glycated albumin has been suggested as an additional marker for monitoring glycemic status. Hitherto, only Amadori-modified peptides of albumin were quantified. In this study, we report the construction of fragment ion library for Amadori-modified lysine (AML), N(ε)-(carboxymethyl)lysine (CML)-, and N(ε)-(carboxyethyl)lysine (CEL)-modified peptides of the corresponding synthetically modified albumin using high resolution accurate mass spectrometry (HR/AM). The glycated peptides were manually inspected and validated for their modification. Further, the fragment ion library was used for quantification of glycated peptides of albumin in the context of diabetes. Targeted Sequential Window Acquisition of all THeoretical Mass Spectra (SWATH) analysis in pooled plasma samples of control, prediabetes, diabetes, and microalbuminuria, has led to identification and quantification of 13 glycated peptides comprised of four AML, seven CML, and two CEL modifications, representing nine lysine sites of albumin. Five lysine sites namely K549, K438, K490, K88, and K375, were observed to be highly sensitive for glycation modification as their respective m/z showed maximum fold change and had both AML and CML modifications. Thus, peptides involving these lysine sites could be potential novel markers to assess the degree of glycation in diabetes.

Indexed as

Peptide LibraryAlbuminuriaAmino Acid SequenceAnalysis of VarianceDiabetes MellitusGlycated Serum AlbuminGlycation End Products, AdvancedHumansLysineMolecular Sequence DataPeptidesPrediabetic StateSerum AlbuminTandem Mass SpectrometryGlycated Serum AlbuminGlycation End Products, AdvancedLysineN(6)-carboxymethyllysinePeptide LibraryPeptidesSerum Albumin

Identifiers

PMID26023067
PMCPMC4528244
OpenAlexW2200136585

What OpenQuestion holds

Textmetadata
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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.