Title : Comparative glycomics of the
glycoprotein follicle stimulating hormone :
glycopeptide analysis of isolates from two mammalian species
Abstract :
- 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 beta subunit ( Asn7 ) of hFSH all other sites in both species have sulfated glycoforms
- Also, glycoforms at Asn52 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