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Data Independent Acquisition Mass Spectrometry Enhanced Personalized Glycosylation Profiling of Haptoglobin in Hepatocellular Carcinoma

ABSTRACT: This study developed an integrated workflow to demonstrate unbiased and enhanced glycosylation profiling of haptoglobin as a model protein in hepatocellular carcinoma (HCC)

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Yu-Ju, Chen

PROVIDER: PXD050708 | JPOST Repository | Tue Mar 18 00:00:00 GMT 2025

REPOSITORIES: jPOST

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			Action	DRS
	20230221_Tiara_B001_16Da_HCD31_90min_DIA_1.raw	Raw
	20230221_Tiara_B002_16Da_HCD31_90min_DIA_1.raw	Raw
	20230221_Tiara_B003_16Da_HCD31_90min_DIA_1.raw	Raw
	20230221_Tiara_B004_16Da_HCD31_90min_DIA_1.raw	Raw
	20230221_Tiara_B005_16Da_HCD31_90min_DIA_1.raw	Raw

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Data Independent Acquisition Mass Spectrometry Enhanced Personalized Glycosylation Profiling of Haptoglobin in Hepatocellular Carcinoma.

Project description:Aberrant glycosylation has gained significant interest for biomarker discovery. However, low detectability, complex glycan structures, and heterogeneity present challenges in glycoprotein assay development. Using haptoglobin (Hp) as a model, we developed an integrated platform combining functionalized magnetic nanoparticles and zwitterionic hydrophilic interaction liquid chromatography (ZIC-HILIC) for highly specific glycopeptide enrichment, followed by a data-independent acquisition (DIA) strategy to establish a deep cancer-specific Hp-glycosylation profile in hepatitis B virus (HBV, n = 5) and hepatocellular carcinoma (HCC, n = 5) patients. The DIA strategy established one of the deepest Hp-glycosylation landscapes (1029 glycopeptides, 130 glycans) across serum samples, including 54 glycopeptides exclusively detected in HCC patients. Additionally, single-shot DIA searches against a DIA-based spectral library outperformed the DDA approach by 2-3-fold glycopeptide coverage across patients. Among the four N-glycan sites on Hp (N-184, N-207, N-211, N-241), the total glycan type distribution revealed significantly enhanced detection of combined fucosylated-sialylated glycans, which were the most dominant glycoforms identified in HCC patients. Quantitation analysis revealed 48 glycopeptides significantly enriched in HCC (p < 0.05), including a hybrid monosialylated triantennary glycopeptide on the N-184 site with nearly none-to-all elevation to differentiate HCC from the HBV group (HCC/HBV ratio: 2462 ± 766, p < 0.05). In summary, DIA-MS presents an unbiased and comprehensive alternative for targeted glycoproteomics to guide discovery and validation of glyco-biomarkers.

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