Analysis of differential glycosylation patterns of human FSH
Chambers, Carrie Anne
Bousfield, George R.
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Chambers, Carrie, Shuai, Bin and George Bousfield (2009). Analysis of Differential Glycosylation Patterns of Human FSH . In Proceedings: 5th Annual Symposium: Graduate Research and Scholarly Projects. Wichita, KS: Wichita State University, p. 20-21
Follicle stimulating hormone (FSH) is a glycoprotein hormone with two subunits, a and ß, and is required for gamete development. Our data suggest that estrogen is responsible for inhibiting the glycosylation of FSHß in reproductive-age women, thus producing a di-glycosylated FSH with higher biological activity than the tetra-glycosylated form. The difference in glycosylation of two subunits is suspected to be due to activity of different oligosaccharyltransferase(OST) isoforms. OSTs are responsible for the first step in N-glycosylation. Factors including signal peptide hydrophobicity of a and ß maybe contribute to selective usage of OST, and hence modulate N-glycosylation. Therefore our hypothesis is that N-glycosylation of FSH subunits is regulated by the differential interactions between OST isoforms and the signal peptides of each subunit, and the differential interaction is modulated by hormones such as estrogen. To test our hypothesis, we will genetically engineer chimeric hFSH subunits by swapping the signal peptide sequences of a and ß. Constructs with the chimeric sequences will be introduced into immortalized gonadotrope cell lines. FSH glycoforms expressed in the cell lines will be examined using Western Blot. If our hypothesis is correct, then we would expect to detect unglycosylated a subunit in the transfected cell lines. Different hormones such as estrogen will be used to treat the cell lines and the difference in FSH subunit glycosylation will be examined
Paper presented to the 5th Annual Symposium on Graduate Research and Scholarly Projects (GRASP) held at the Hughes Metropolitan Complex, Wichita State University, May 1, 2009.
Research completed at the Department of Biological Sciences, College of Liberal Arts and Sciences