• 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)

临床输血与检验 ›› 2026, Vol. 28 ›› Issue (4): 518-524.DOI: 10.3969/j.issn.1671-2587.2026.04.009

• 基础研究 • 上一篇    下一篇

血小板中高丰度完整糖肽解析*

智渊1,2, 张春2, 王娜1,2, 张钰1,2, 凌亚亭1,2, 傅强2, 何成涛1,2   

  1. 1南京红十字血液中心研究室,江苏南京 210003;
    2南京红十字血液中心输血医学重点实验室,江苏南京 210003
  • 收稿日期:2026-07-07 出版日期:2026-08-20 发布日期:2026-08-26
  • 通讯作者: 何成涛,主要从事输血技术及免疫学方面研究,(E-mail)hechengtao413@126.com。共同通信作者:傅强,主要从事献血服务、管理和血液安全工作,(E-mail)fuqiangnj@hotmail.com。
  • 作者简介:智渊,主要从事输血免疫学研究,(E-mail)biozhiyuan@163.com。并列第一作者:张春,主要从事输血安全管理,(E-mail)18951670998@189.cn。
  • 基金资助:
    *本课题受南京市卫生健康委员会指导性项目(No.ZDXX25187)资助

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

摘要: 目的 对血小板中高丰度的完整糖肽进行解析,并探讨血小板中主要的糖基化修饰所发挥的功能。方法 使用亲水层析色谱法富集血小板中的完整糖肽,并利用液相色谱高分辨质谱检测血小板中高丰度糖肽。结果 本研究共鉴定出76条完整糖肽,归属于28个蛋白中的35个糖基化位点。其中,ITGB3、THBS1等与纤维蛋白粘附功能相关的糖基化修饰被成功鉴定。在这些修饰中,C2orf80蛋白被鉴定出含有平分型糖链修饰。目前,关于C2orf80上特异性糖基化位点尚未见文献报道,现有研究主要集中在该蛋白对应的基因在胶质瘤及精神疾病中的表达变化,其生物学功能仍不明确。结论 本研究揭示了C2orf80蛋白上平分型糖链的糖基化修饰,为后续探索该蛋白的功能提供了重要数据支持。

关键词: 血小板, 糖基化, C2orf80, 凝血止血反应, 糖肽

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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