Exploring serum N-glycome patterns as candidate non-invasive biomarkers in inguinal hernia

Although inguinal hernia (IH) is prevalent in elderly males, research on its specific diagnostic biomarkers is limited. Protein N-glycosylation is one of the most important and ubiquitous post-translational modifications and often results in a remarkable heterogeneity of protein glycoforms. Protein N-glycosylation often changes in a disease and holds great potential for discovering non-invasive biomarkers. This study aimed to gain insights into total serum protein N-glycosylation of IH to identify candidate non-invasive biomarkers for diagnosis and subtype classification of IH.

Linkage-specific sialylation derivatization combined with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry detection was used to analyze serum protein N-glycosylation patterns in IH patients and healthy controls.

IH patients had abnormal glycan fucosylation and sialylation compared to healthy controls (HC), of which two glycan traits representing linkage-specific sialylation within monoantennary glycans showed high potential as diagnostic biomarkers for IH with an area under the curve (AUC) of 0.75. Additionally, serum N-glycans were different between indirect IH and direct IH in glycosylation features, namely complexity, fucosylation, galactosylation, sialylation, and α2,6-linked sialylation. Four distinctive glycans between the two subtypes showed good performance with AUC >0.8, suggesting that these glycan traits have potential as biomarkers for subtype classification.

We first reported the serum N-glycomic features of IH patients. Furthermore, we identified several potential biomarkers for the diagnosis and subtype classification of IH. These findings can deepen the understanding of IH.