Intact N-glycopeptide analysis of human platelets reveals a Glycostructure important for platelet function.

This article focuses on the global analysis of intact N-glycopeptides in human platelets to characterize glycosylation patterns and their functional roles, particularly the involvement of the Lewis y antigen in platelet adhesion. Using ZIC-hydrophilic interaction chromatography and Liquid Chromatography–Tandem Mass Spectrometry, the study identified 1,425 intact glycopeptides from 190 N-glycoproteins, revealing 358 glycans modifying 328 glycosites. Functional analyses highlighted glycoproteins involved in platelet adhesion, notably von Willebrand factor (VWF), thrombospondin 1 (THBS1), and glycoprotein V (GPV), all carrying the Lewis y antigen, a blood group-related carbohydrate structure. Immunoprecipitation confirmed Lewis y modification on these proteins, and adhesion assays demonstrated that blocking Lewis y significantly reduced platelet adhesion to collagen I under static and flow conditions, indicating its role in mediating platelet–collagen interactions.