Evidence map›Paper›PMID 41032136›Full record

ArticleAnalytical and bioanalytical chemistry2025

Glycoproteomics analysis of colorectal cancer reveals differential alterations of glycoproteins and glycans.

Wenqi Zhang, Xiaotong Wang, Shengye Wen, Wei Ge, Jianbo Deng, Zeyang Zhou, Junhong Jiang, Xiaodong Yang, Yan Wang, Shuang Yang

Abstract read
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In one paragraph

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

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

10 authors.

Wenqi Zhang *Laboratory of Clinical and Molecular Glycobiology, Institute of Glycomics, Shantou University Medical College, Shantou, 515041, Guangdong, China.
Xiaotong Wang *Center for Clinical Mass Spectrometry, College of Pharmaceutical Sciences, Soochow University, Jiangsu, 215123, China.
Shengye WenCenter for Clinical Mass Spectrometry, College of Pharmaceutical Sciences, Soochow University, Jiangsu, 215123, China.
Wei GeCenter for Clinical Mass Spectrometry, College of Pharmaceutical Sciences, Soochow University, Jiangsu, 215123, China.
Jianbo DengCenter for Clinical Mass Spectrometry, College of Pharmaceutical Sciences, Soochow University, Jiangsu, 215123, China.
Zeyang ZhouCenter for Clinical Mass Spectrometry, College of Pharmaceutical Sciences, Soochow University, Jiangsu, 215123, China.
Junhong JiangDepartment of Respiratory Medicine, The Fourth Affiliated Hospital of Soochow University, Suzhou, 215123, Jiangsu, China.
Xiaodong YangDepartment of General Surgery, The Second Affiliated Hospital of Soochow University, Suzhou, 215004, China.
Yan WangMass Spectrometry Facility, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD, 20892, USA. yan.wang2@nih.gov.
Shuang YangLaboratory of Clinical and Molecular Glycobiology, Institute of Glycomics, Shantou University Medical College, Shantou, 515041, Guangdong, China. shuangyang@stu.edu.cn.ORCID http://orcid.org/0000-0001-7958-0594

Funding

Mass Spectrometry FacilityZIADE000751 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI WANG, YAN · 2019 to 2019
$193k
Intramural NIH HHS ZIA DE000751the Jiangsu Science and Technology Plan Funding BX2022023the Jiangsu Shuangchuang Boshi Funding JSSCBS20210697the Suzhou Health Talents Program GSWS2022087the Suzhou Medical Innovation Funding SKJY2021141
6 · The paper itself

Abstract

Colorectal cancer (CRC) remains a global health concern, with an urgent need for better early detection and targeted therapies. Our glycoproteomics analysis comparing CRC to paracancerous (PCA) tissue revealed significant alterations. Global proteomic analysis showed more unique proteins in CRC, with differential expression across CRC stages, especially in protein synthesis, translation, and degradation pathways. Despite overall proteomic differences, intact glycopeptide analysis showed high glycosylation similarity between CRC and PCA, with 722 shared glycosites, 2102 shared glycopeptides, and 435 shared glycoproteins. However, a significant shift in CRC's N-glycan composition was observed: an upregulation of high-mannose N-glycans and a decrease in complex N-glycans, including sialoglycans and fucosylated sialoglycans. While glycosylation motif analysis showed conserved peptide sequences, the attached N-glycan types differed remarkably. KEGG pathway analysis suggested that extracellular matrix and lysosomal glycoproteins like COL1A1 and LAMP1 might modulate the PI3K/Akt signaling pathway via TGFβ1-mediated mechanisms, potentially contributing to tumor progression. These findings suggest that while global protein expression changes significantly in CRC, subtle but crucial changes in N-glycan composition, specifically the increase of high-mannose N-glycans and the decrease of complex N-glycans, may play a significant role in tumor progression and metastasis, potentially through modulation of key signaling pathways.

Indexed as

Colorectal NeoplasmsGlycoproteinsPolysaccharidesProteomicsGlycosylationHumansGlycoproteinsPolysaccharidesColorectal cancerGlycanGlycoformMass spectrometrySite-specific glycosylation

Identifiers

PMID41032136

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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.