Site-specific N-glycan changes during semen liquefaction

被引:2
作者
Li, Cheng [1 ]
Dan, Wei [1 ]
Li, Pengfei [1 ]
Xin, Miaomiao [1 ]
Lan, Rongxia [1 ]
Zhu, Bojing [1 ]
Chen, Zexuan [1 ]
Dong, Wenbo [1 ]
Dang, Liuyi [1 ]
Zhang, Xinwen [2 ]
Sun, Shisheng [1 ]
机构
[1] Northwest Univ, Coll Life Sci, Xian 710069, Shaanxi Provinc, Peoples R China
[2] Xian Peoples Hosp, Xian Hosp 4, Ctr Med Genet, Xian 710004, Shaanxi, Peoples R China
基金
中国国家自然科学基金;
关键词
Semen; Liquefaction; Glycoproteome; N -Glycan structures; Mass spectrometry; PROSTATIC-ACID-PHOSPHATASE; HUMAN SEMINAL PLASMA; PROTEIN GLYCOSYLATION; CARBOXYPEPTIDASE; IDENTIFICATION; FERTILITY; SPERM;
D O I
10.1016/j.ab.2023.115318
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Normal liquefaction of semen is one of the key steps to ensure the smooth progress of fertilization, and glycosylation has been reported to be involved in the whole process of fertilization. Till now, it is still unclear whether and how glycosylation changes during the liquefaction process of semen. In this study, by performing a glycoproteomic analysis of human semen with the liquefaction process (liquefaction time of semen: 0 min vs 30 min) using our recently developed StrucGP software combined with the Tandem Mass Tags (TMT) based quantification, we identified 25 intact glycopeptides (IGPs) from 10 glycoproteins in semen that were significantly changed during liquefaction, including 23 up-regulated and two down-regulated. Among the 23 up-regulated glycopeptides, half were modified with sialylated glycans, suggesting that sialylated glycans may play a key role in the semen liquefaction process. The data provide an invaluable resource for further studies on the role of glycosylation during semen liquefaction.
引用
收藏
页数:8
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