Comparative Glycomics of the Glycoprotein Follicle Stimulating Hormone:  Glycopeptide Analysis of Isolates from Two Mammalian Species

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...

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Bibliographic Details
Published in:Biochemistry (Easton) 2006-07, Vol.45 (28), p.8665-8673
Main Authors: Dalpathado, Dilusha S, Irungu, Janet, Go, Eden P, Butnev, Vladimir Y, Norton, Katie, Bousfield, George R, Desaire, Heather
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Follicle Stimulating Hormone - chemistry
Follicle Stimulating Hormone, beta Subunit - chemistry
Fourier Analysis
Glycopeptides - chemistry
Glycoprotein Hormones, alpha Subunit - chemistry
Glycoproteins - chemistry
Glycosylation
Horses
Humans
Mass Spectrometry
Molecular Sequence Data
Polysaccharides - analysis
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Summary: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 β 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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi060435k