Tharmalingam-Jaikaran T, Walsh S W, McGettigan P A, Potter O, Struwe W B, Evans A C O, Rudd P M, Carrington S D
Dublin-Oxford Glycobiology LaboratoryNIBRT - The National Institute for Bioprocessing Research and Training, Fosters Avenue, Mount Merrion, Blackrock, Co. Dublin, IrelandSchool of Agriculture and Food ScienceUniversity College Dublin, Belfield, Dublin 4, IrelandSchool of Veterinary MedicineUniversity College Dublin, Belfield, Dublin 4, Ireland Dublin-Oxford Glycobiology LaboratoryNIBRT - The National Institute for Bioprocessing Research and Training, Fosters Avenue, Mount Merrion, Blackrock, Co. Dublin, IrelandSchool of Agriculture and Food ScienceUniversity College Dublin, Belfield, Dublin 4, IrelandSchool of Veterinary MedicineUniversity College Dublin, Belfield, Dublin 4, Ireland.
Dublin-Oxford Glycobiology LaboratoryNIBRT - The National Institute for Bioprocessing Research and Training, Fosters Avenue, Mount Merrion, Blackrock, Co. Dublin, IrelandSchool of Agriculture and Food ScienceUniversity College Dublin, Belfield, Dublin 4, IrelandSchool of Veterinary MedicineUniversity College Dublin, Belfield, Dublin 4, Ireland.
Reproduction. 2014 Dec;148(6):569-80. doi: 10.1530/REP-14-0035. Epub 2014 Sep 11.
Follicular fluid (FF), an important microenvironment for the development of oocytes, contains many proteins that are glycosylated with N-linked glycans. This study aimed i) to present an initial analysis of the N-linked glycan profile of bovine FF using hydrophilic interaction liquid chromatography, anion exchange chromatography, high performance liquid chromatography (HPLC)-based separations and subsequent liquid chromatography-mass spectrometry/mass spectrometry analysis; ii) to determine differences in the N-glycan profile between FF from dominant and subordinate follicles from dairy heifers and lactating dairy cows and iii) to identify alterations in the N-glycan profile of FF during preovulatory follicle development using newly selected, differentiated (preovulatory) and luteinised dominant follicles from dairy heifers and lactating cows. We found that the majority of glycans on bovine FF are based on biantennary hypersialylated structures, where the glycans are sialylated on both the galactose and N-acetylglucosamine terminal sugars. A comparison of FF N-glycans from cows and heifers indicated higher levels of nonsialylated glycans with a lower proportion of sialylated glycans in cows than in heifers. Overall, as the follicle develops from Selection, Differentiation and Luteinisation in both cows and heifers, there is an overall decrease in sialylated structures on FF N-glycans.
卵泡液（FF）是卵母细胞发育的重要微环境，含有许多被N-连接聚糖糖基化的蛋白质。本研究旨在：i）使用亲水相互作用液相色谱、阴离子交换色谱、基于高效液相色谱（HPLC）的分离方法及随后的液相色谱-质谱/质谱分析，对牛卵泡液的N-连接聚糖谱进行初步分析；ii）确定来自奶牛和泌乳奶牛的优势卵泡和从属卵泡的卵泡液中N-聚糖谱的差异；iii）使用从奶牛和泌乳奶牛新选择的、分化的（排卵前）和黄体化的优势卵泡，确定排卵前卵泡发育过程中卵泡液N-聚糖谱的变化。我们发现，牛卵泡液上的大多数聚糖基于双天线高度唾液酸化结构，其中聚糖在半乳糖和N-乙酰葡糖胺末端糖上均被唾液酸化。对奶牛和小母牛卵泡液N-聚糖的比较表明，奶牛中非唾液酸化聚糖的水平较高，唾液酸化聚糖的比例低于小母牛。总体而言，随着卵泡在奶牛和小母牛中从选择、分化到黄体化的发育，卵泡液N-聚糖上的唾液酸化结构总体上减少。
