Evidence map›Paper›PMID 40210651›Full record

ArticleScientific reports2025

Unique N-glycosylation signatures in human iPSC derived microglia activated by Aβ oligomer and lipopolysaccharide.

Xinyu Tang, Ryan Lee Schindler, Jacopo Di Lucente, Armin Oloumi, Jennyfer Tena, Danielle Harvey, Carlito B Lebrilla, Angela M Zivkovic, Lee-Way Jin, Izumi Maezawa

Abstract read
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In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Xinyu Tang *Department of Nutrition, University of California, Davis, CA, 95618, USA.
Ryan Lee Schindler *Department of Chemistry, University of California, Davis, Davis, CA, USA.
Jacopo Di LucenteDepartment of Pathology and Laboratory Medicine and M.I.N.D. Institute, University of California Davis Medical Center, Sacramento, CA, 95817, USA.
Armin OloumiDepartment of Chemistry, University of California, Davis, Davis, CA, USA.
Jennyfer TenaDepartment of Chemistry, University of California, Davis, Davis, CA, USA.
Danielle HarveyDepartment of Public Health Sciences, University of California-Davis, Davis, CA, USA.
Carlito B LebrillaDepartment of Chemistry, University of California, Davis, Davis, CA, USA.
Angela M ZivkovicDepartment of Nutrition, University of California, Davis, CA, 95618, USA. amzivkovic@ucdavis.edu.
Lee-Way JinDepartment of Pathology and Laboratory Medicine and M.I.N.D. Institute, University of California Davis Medical Center, Sacramento, CA, 95817, USA. lwjin@ucdavis.edu.
Izumi MaezawaDepartment of Pathology and Laboratory Medicine and M.I.N.D. Institute, University of California Davis Medical Center, Sacramento, CA, 95817, USA. imaezawa@ucdavis.edu.

Funding

Comprehensive Characterization of Glycosylation Alterations in Alzheimer’s DiseaseR01AG062240 · NIA · UNIVERSITY OF CALIFORNIA AT DAVIS · PI JIN, LEE-WAY, LEBRILLA, CARLITO B · 2018 to 2022
$3.3M
Development of a Novel Technology for Preparative Fractionation and Characterization of Lipoprotein ParticlesR01GM147545 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI ZIVKOVIC, ANGELA M · 2022 to 2025
$1.2M
NIA NIH HHS R01 AG062240NIGMS NIH HHS R01 GM147545
6 · The paper itself

Abstract

Microglia are the immune cells in the central nervous system (CNS) and become pro-inflammatory/activated in Alzheimer's disease (AD). Cell surface glycosylation plays an important role in immune cells; however, the N-glycosylation and glycosphingolipid (GSL) signatures of activated microglia are poorly understood. Here, we study comprehensively combined transcriptomic and glycomic profiles using human induced pluripotent stem cells-derived microglia (hiMG). Distinct changes in N-glycosylation patterns in amyloid-β oligomer (AβO) and LPS-treated hiMG were observed. In AβO-treated cells, the relative abundance of bisecting N-acetylglucosamine (GlcNAc) N-glycans decreased, corresponding with a downregulation of MGAT3. The sialylation of N-glycans increased in response to AβO, accompanied by an upregulation of genes involved in N-glycan sialylation (ST3GAL4 and 6). Unlike AβO-induced hiMG, LPS-induced hiMG exhibited a decreased abundance of complex-type N-glycans, aligned with downregulation of mannosidase genes (MAN1A1, MAN2A2, and MAN1C1) and upregulation of ER degradation related-mannosidases (EDEM1-3). Fucosylation increased in LPS-induced hiMG, aligned with upregulated fucosyltransferase 4 (FUT4) and downregulated alpha-L-fucosidase 1 (FUCA1) gene expression, while sialofucosylation decreased, aligned with upregulated neuraminidase 4 (NEU4). Inhibition of sialylation and fucosylation in AβO- and LPS-induced hiMG alleviated pro-inflammatory responses. However, the GSL profile did not exhibit significant changes in response to AβO or LPS activation, at least in the 24-hour stimulation timeframe. AβO- and LPS- specific glycosylation changes could contribute to impaired microglia function, highlighting glycosylation pathways as potential therapeutic targets for AD.

Indexed as

Amyloid beta-PeptidesInduced Pluripotent Stem CellsLipopolysaccharidesMicrogliaAlzheimer DiseaseGlycosphingolipidsGlycosylationHumansPolysaccharidesAmyloid beta-PeptidesGlycosphingolipidsLipopolysaccharidesPolysaccharidesAmyloidFucosylationGlycosylationLipopolysaccharideMicrogliaSialylation

Identifiers

PMID40210651
PMCPMC11985925

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Registered trials

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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.