Comparative glycomics of the glycoprotein follicle stimulating hormone: Glycopeptide analysis of isolates from two mammalian species
Comparative glycomics of the glycoprotein follicle stimulating hormone: Glycopeptide analysis of isolates from two mammalian species
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DOI：
10.1021/bi060435k
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发表时间：
2006-07-18
期刊：
影响因子：
2.9
通讯作者：
Desaire, Heather
中科院分区：
文献类型：
--
作者：
Dalpathado, Dilusha S.;Irungu, Janet;Desaire, Heather
卵泡刺激素（FSH）是调节性腺功能的重要激素之一。这种激素是糖基化的，聚糖极大地影响生物学特性。在本研究中，马和人垂体促卵泡激素（eFSH和hFSH）的带负电荷的糖肽已被其特征在于在糖基化位点特异性的方式使用FT-ICR-MS和Edman测序。在每个糖基化位点的聚糖分布的特征模式已被推导出来，并在马和人FSH制剂之间进行比较。这些数据表明，位点特异性差异之间存在的人和马FSH的糖型。例如，除了hFSH亚基（Asn（7））中的一个位点外，两种物种中的所有其他位点都具有硫酸化糖型。hFSH的Asn（52）位点糖型均为复合型，而eFSH的Asn（52）位点糖型既有复合型又有杂合型。与前者相比，后者位点中硫酸化聚糖的百分比也更高。这是首次以糖基化位点特异性方式表征该激素聚糖的研究，这些数据可用于开始糖基化结构与激素功能之间的相关性研究。
Follicle stimulating hormone (FSH) is one of the important hormones that regulate gonadal functions. This hormone is glycosylated, and the glycans greatly influence the biological properties. In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing. The characteristic pattern of glycan distribution at each glycosylation site has been deduced and compared between horse and human FSH preparations. The data suggest that site-specific differences exist between glycoforms of human and equine FSH. For instance, except for one site in the, subunit (Asn(7)) of hFSH all other sites in both species have sulfated glycoforms. Also, glycoforms at Asn(52) of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site. There is also a higher percentage of sulfated glycans in the latter site compared to the former. This is the first study that characterizes the glycans from this hormone in a glycosylation site-specific manner, and these data can be used to begin correlative studies between glycosylation structure and hormone function.