• 中国科学论文统计源期刊
  • 中国科技核心期刊
  • 美国化学文摘(CA)来源期刊
  • 日本科学技术振兴机构数据库(JST)

JOURNAL OF CLINICAL TRANSFUSION AND LABORATORY MEDICINE ›› 2026, Vol. 28 ›› Issue (4): 518-524.DOI: 10.3969/j.issn.1671-2587.2026.04.009

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Characterization of High-abundance Intact Glycopeptides in Platelets

ZHI Yuan1,2, ZHANG Chun2, WANG Na1,2, ZHANG Yu1,2, LING Yating1,2, FU Qiang2, HE Chengtao1,2   

  1. 1Research Office, Nanjing Red Cross Blood Center, Nanjing 210003;
    2Key Laboratory of Transfusion Medicine, Nanjing Red Cross Blood Center, Nanjing 210003
  • Received:2026-07-07 Online:2026-08-20 Published:2026-08-26

Abstract: 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.

Key words: Platelets, Glycosylation, C2orf80, Hemostasis and coagulation, Glycopeptide

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