Evidence map›Paper›PMID 39676134›Full record

ArticleAnalytical and bioanalytical chemistry2025

Inter-tissue glycan heterogeneity: site-specific glycoform analysis of mouse tissue N-glycoproteomes using MS1-based glycopeptide detection method assisted by lectin microarray.

Chiaki Nagai-Okatani, Azusa Tomioka, Daisuke Tominaga, Hiroaki Sakaue, Atsushi Kuno, Hiroyuki Kaji

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Article in Analytical and bioanalytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

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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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Temporal and Sex-DependentInternational journal of molecular sciences · 2025
    Article
4 · The record

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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

6 authors.

Chiaki Nagai-OkataniMolecular and Cellular Glycoproteomics Research Group, Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, 305-8565, Japan. chiaki-okatani@aist.go.jp.ORCID http://orcid.org/0000-0003-4084-3128
Azusa TomiokaMolecular and Cellular Glycoproteomics Research Group, Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, 305-8565, Japan.
Daisuke TominagaMolecular and Cellular Glycoproteomics Research Group, Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, 305-8565, Japan.ORCID http://orcid.org/0000-0003-4390-423X
Hiroaki SakaueMolecular and Cellular Glycoproteomics Research Group, Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, 305-8565, Japan.ORCID http://orcid.org/0000-0002-1977-0318
Atsushi KunoMolecular and Cellular Glycoproteomics Research Group, Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, 305-8565, Japan.ORCID http://orcid.org/0000-0002-6147-6171
Hiroyuki KajiMolecular and Cellular Glycoproteomics Research Group, Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, 305-8565, Japan. kaji.hiroyuki.j8@f.mail.nagoya-u.ac.jp.ORCID http://orcid.org/0000-0002-0910-9999

Funding

Japan Agency for Medical Research and Development JP20ae0101021h0005Japan Society for the Promotion of Science JP15K14426
6 · The paper itself

Abstract

To understand the biological and pathological functions of protein glycosylation, the glycan heterogeneities for each glycosite in a single glycoprotein need to be elucidated depending on the type and status of cells. For this aim, a reliable strategy is needed to compare site-specific glycoforms of multiple glycoprotein samples in a comprehensive manner. To analyze this "inter-heterogeneity" of samples, we previously introduced an MS1-based glycopeptide detection method, "Glyco-RIDGE." Here, to elucidate inter-tissue glycan heterogeneities, this estimation method was applied to site-specific N-glycoforms of glycoproteins from six normal mouse tissues (liver, kidney, spleen, pancreas, stomach, and testis). The analyses of desialylated glycopeptides estimated 11,325 site-specific N-glycoforms with 239 glycan compositions at 1260 sites (1122 non-redundant core peptides) in 800 glycoproteins, revealing inter-tissue differences in macro-, micro-, and meta-glycan heterogeneities. To obtain detailed information on their glycan features and tissue distribution, the Glyco-RIDGE results were compared with laser microdissection-assisted lectin microarray (LMD-LMA)-based mouse tissue glycome mapping data deposited on LM-GlycomeAtlas, as well as MS-based mouse tissue glycome data deposited on GlycomeAtlas. This integrated approach supported the certainty of Glyco-RIDGE results and suggested that inter-tissue differences exist in glycan motifs, such as alpha-galactose and bisecting N-acetylglucosamine, in both whole tissue glycomes and specific glycoproteins, Anpep and Lamc1. In addition, the comparison with LMD-LMA-based tissue glycome mapping data suggested the possibility of estimating the tissue distribution of the assigned glycans and glycopeptides. Taken together, these findings demonstrate the utility of an integrated approach using MS assisted by LMA for large-scale analyses.

Indexed as

GlycopeptidesGlycoproteinsLectinsPolysaccharidesProtein Array AnalysisProteomeAnimalsGlycosylationMaleMiceProteomicsTandem Mass SpectrometryGlycopeptidesGlycoproteinsLectinsPolysaccharidesProteomeGlycan heterogeneityGlycoproteomicsLectin microarrayMass spectrometrySite-specific glycoformTissue glycome mapping

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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.