Evidence map›Paper›PMID 42237277›Full record

ArticleBMC psychiatry2026

Site-specific N-glycosylation alterations in serum proteins across subtypes of adolescent depressive disorder.

Xinyuan Hu, Xinhao Liang, Yumei Wan, Kaihong Zhang, Fengjuan Zou, Jueqi Du, Cheng Li, Yunshao Zheng

Abstract read
In one paragraph

Article in BMC psychiatry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
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0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Xinyuan HuShandong Provincial Key Medical and Health Laboratory of Shandong Mental Health Center, Shandong University, Jinan, 250014, China. moonriveryue@163.com.
Xinhao LiangDepartment of Child and Adolescent Mental Behavior, Shandong Mental Health Center, Shandong University, Jinan, 250014, China.
Yumei WanDepartment of Psychiatry, Shandong Mental Health Center, Shandong University, Jinan, 250014, China.
Kaihong ZhangDepartment of Psychiatry, Shandong Mental Health Center, Shandong University, Jinan, 250014, China.
Fengjuan ZouNational Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, Qingdao, 266237, China.
Jueqi DuNational Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, Qingdao, 266237, China.
Cheng LiCollege of Life Sciences, Northwest University, Xi'an, 710069, China. chengli_glyco@163.com.
Yunshao ZhengDepartment of Psychiatry, Shandong Mental Health Center, Shandong University, Jinan, 250014, China. zys19810810@163.com.

Funding

Shandong Provincial Medical and Health Technology Development Plan No.202201060948Shandong Provincial Natural Science Foundation Youth Program ZR2021QH283Shandong Provincial Traditional Chinese Medicine Science and Technology Project Z-2023061
6 · The paper itself

Abstract

backgroundAdolescent depressive disorder is a clinically heterogeneous condition with poorly understood molecular mechanisms. Protein N-glycosylation, a key post-translational modification involved in immune regulation and neuronal communication, has not been systematically investigated across depressive subtypes in youth. Understanding glycosylation alterations may reveal novel biochemical pathways underlying disease heterogeneity and pathophysiology.

methodsWe applied a site-specific glycoproteomic approach integrating liquid chromatography-tandem mass spectrometry (LC-MS/MS) and StrucGP to profile serum N-glycosylation in adolescents with major depressive disorder (MDD), MDD with non-suicidal self-injury (NSSI), and MDD with suicide attempts (SA), compared with healthy controls. Serum samples were pooled by group (10 individuals per pool), and glycan alterations were identified using predefined fold-change thresholds. This approach is classified as an exploratory research strategy, which does not support statistical inference.

resultsAll depressive subtypes displayed shared alterations, characterized by reduced bi-antennary glycans and LacNAc/Lewis structures, alongside elevated tetra-antennary sialylation, particularly N6H7S4. Candidate subtype-associated patterns were also observed: increased tri-antennary sialylation in NSSI, and selective upregulation of N6H7S4 on ORM2 in SA. Differentially glycosylated proteins, including SERPING1 and A2M, were enriched in immune, complement, and coagulation pathways. Notably, protein-level changes were minimal in label-free quantification, suggesting glycan-specific dysregulation.

conclusionsThis exploratory study identifies candidate subtype-dependent alterations in N-glycosylation in adolescent depression, which may implicate glycan-mediated immune and neuroinflammatory mechanisms in its molecular heterogeneity. This study provides a preliminary, pooled-sample based catalog of candidate site-specific N-glycosylation alterations for adolescent depression, warranting validation in larger, individual-level cohorts.

Indexed as

Blood ProteinsMajor Depressive DisorderAdolescentChromatography, LiquidFemaleGlycosylationHumansLiquid Chromatography-Mass SpectrometryMalePolysaccharidesSelf-Injurious BehaviorSuicide, AttemptedTandem Mass SpectrometryBlood ProteinsPolysaccharidesAdolescent depressive disorderBiomarkersDepression subtypesGlycoproteomicMass spectrometryN-glycosylation

Identifiers

PMID42237277
PMCPMC13449685

What Socratic holds

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LicenceCC BY-NC-ND
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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 Socratic graph.