血小板中高丰度完整糖肽解析OA

Objective This study aims to characterize high-abundance intact glycopeptides in platelets and explore the functions of major glycosylation modifications.Methods Intact glycopeptides from platelets were enriched using hydrophilic interaction liquid chromatography(HILIC)and analyzed by liquid chromatography coupled with high-resolution mass spectrometry(LC-HRMS).Results A total of 76 intact glycopeptides were identified,mapping to 35 glycosylation sites derived from 28 platelet proteins.Among these,glycosylation modifications associated with fibrin adhesion,including those on ITGB3 and THBS1,were successfully identified.Notably,the C2orf80 protein was found to carry a bisecting N-glycan modification.To date,no site-specific glycosylation on C2orf80 has been reported in the literature;existing studies have primarily focused on the expression changes of the gene encoding this protein in gliomas and psychiatric disorders,while its biological function remains poorly characterized.Conclusion This study first identified the bisecting N-glycan modification of C2orf80 in platelets,which provides a crucial theoretical and data basis for further exploration of the biological function of C2orf80.