PXD055935-1

PXD055935 is an original dataset announced via ProteomeXchange.

Title	N-Glycoproteomic analysis reveals novel mechanism and clinical relevance in Colorectal Cancer
Description	Glycosylation is largely involved in development and progression of cancer and provides multiple novel targets for diagnostic application and therapeutic strategies. Recent advances in methods for enrichment and mass spectrometric interpreting of intact N-glycoprotein contribute to large-scale clinical glycoproteomics datasets generation, whereas systematic interpretation of these data remains challenging due to the complexity and unstable nature of N-glycosylation modifications. In this study, we mapped the glycoproteome of 45 untreated, resectable colorectal cancer (CRC) tumors, together with their normal adjacent tissues, quantifying over 7,000 N-linked glycoproteins by employing advanced mass spectrometry and high-throughput data analysis. Protein N-sialylation and N-high-mannosylation were revealed to be the most commonly altered modifications in our qualitative and quantitative analysis. Furthermore, we constructed a dynamic N-glycan-site-protein-signaling pathway network based on the N-glycan profiles, highlighting the crucial roles of glycosylated proteins in immune response and various cellular processes. For a comprehensive study on N-glycan functions in CRC, we established a robust scoring system for the combined glycoform profiles, which could potentially be used for biomarker and drug target discovery. In addition, our study revealed FUCA1 and ERO1A as significant dysregulated glycosyltransferases closely related to CRC development and identified APMAP-N196 glycosylation, a potential biomarker for CRC prediction and therapy response monitoring. Overall, the findings underscore the importance of glycosylation dynamics in CRC progression and pave the way for early diagnosis and personalized therapies.
HostingRepository	PRIDE
AnnounceDate	2025-06-16
AnnouncementXML	Submission_2025-06-15_16:20:30.684.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	He Huang
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2024-09-17 06:01:31	ID requested
⏵ 1	2025-06-15 16:20:31	announced

Liu G, Chen L, Zhao J, Jiang Y, Guo Y, Mao X, Ren X, Liu K, Mei Q, Li Q, Huang H, Deciphering the Metabolic Impact and Clinical Relevance of N-Glycosylation in Colorectal Cancer through Comprehensive Glycoproteomic Profiling. Adv Sci (Weinh), 12(21):e2415645(2025) [pubmed]

10.1002/advs.202415645;

submitter keyword: Cancer therapies, Colorectal Cancer,N-Glycoproteomic, Mechanism

He Huang
contact affiliation	Chinese Academy of Sciences Shanghai Institute of Materia Medica
contact email	hhuang@simm.ac.cn
lab head
He Huang
contact affiliation	Shanghai Institute of Materia Medica
contact email	hhuang.nu@gmail.com
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/06/PXD055935

PRIDE project URI

• PRIDE
  1. PXD055935
     1. Label: PRIDE project
     2. Name: N-Glycoproteomic analysis reveals novel mechanism and clinical relevance in Colorectal Cancer