George R. Bousfield, Ph.D.

Dr. Lawrence M. Jones Distinguished Professor
Core Laboratory Director
Department of Biological Sciences, Wichita State University

Ph.D., Indiana University, 1981
Postdoctoral, The University of Texas MD Anderson Hospital, 1981-1983

My laboratory is interested in the structure-function relations of the gonadotropins. These are members of the glycoprotein hormone family, which consists of the three gonadotropins, luteinizing hormone (LH), follicle-stimulating hormone (FSH), and chorionic gonadotropin (CG). The fourth member of this protein family is thyroid stimulating hormone (TSH). Together, the glycoprotein hormones form a unique subset of the cystine knot growth factor superfamily. While most other superfamily members are located at the C-terminal end of a larger precursor from which they are cleaved, and the N-terminal portion then acts as a regulatory factor, the glycoprotein subunits consist of only the cystine knot domains. The subunits are dissimilar proteins, a common alpha subunit that is differentially glycosylated in each hormone, as well as a hormone-specific beta subunit. Another unusual facet of glycoprotein hormone structure-function is these hormones are decorated with N-linked and sometimes O-linked glycans, which are necessary for function. The glycans can determine metabolic clearance rates of the hormones and at least some of them are necessary for biological activity, although the mechanism is unknown. Glycosylation varies in two ways: microheterogeneity and macroheterogeneity. The former results from a population of 2-105 glycans found at each N- or O-glycosylation site, while the latter results from partial glycosylation of the hormone-specific beta subunit. In humans an interesting pattern of glycosylation is found in FSH. The alpha subunit is always N-glycosylated, while the FSHΒ subunit appears to be glycosylated in an all-or-none manner. This produces a FSH glycoform that possesses four N-glycans that we call tetra-glycosylated hFSH and another form that possesses only the alpha subunit N-glycans that we call di-glycosylated hFSH. In young women, di-glycosylated hFSH is the more abundant glycoform present in the pituitary gland, however, there appears to be a progressive loss of this glycoform with increasing age. We are interested in determining if this can be used as a marker for reproductive aging.

Selected Publications

Irungu, J.A., Dalpathado, D.S., Go, E.P., Jiang, H., Ha, H.-V., Bousfield, G.R., and Desaire, H., A Method for Characterizing Sulfated Glycoproteins in a Glycosylation Site-Specific Fashion, Using Ion-Pairing and Tandem Mass Spectrometry, Anal. Chem. 78: 11801-1190, 2006

Dalpathado, D.S., Irungu, J.A., Go, E.P., Butnev, V.Y., Norton, K., Bousfield, G.R., and Desaire, H. Comparative glycomics of the glycoprotein follicle-stimulating hormone (FSH): Glycopeptide analysis of isolates from two mammalian species, Biochemistry, 45:8665-8673, 2006

Bousfield, G.R., Butnev, V.Y., Walton, W.J., Nguyen, V.T., Huneidi, J., Singh, V., Kolli, K., Harvey, D.J., and Rance, N.E., All-or-None N-Glycosylation in Primate Follicle-Stimulating Hormone Beta-Subunits, Mol. Cell. Endocrinol. 260-262:  40-48, 2007

Jablonka-Shariff , A, Roser, J.F., Bousfield, G.R., Wolfe, M.W., Sibley, L.E., Colgin, M., and Boime, I., Expression And Bioactivity Of A Single Chain Recombinant Equine Luteinizing Hormone (ReLH), Theriogenology  67:  311-320, 2007

Bousfield, G.R., Butnev, V.Y., Bidart, J.M., Dalpathado, D., Irungu, J., and Desaire, H., Chromatofocusing fails to separate hFSH isoforms on the basis of glycan structure, Biochemistry 47:  1708-1720, 2008.

Ulloa-Aguirre, A., Dias, J.A,. and Bousfield, G.R. Gonadotropins and the importance of glycosylation, In: Walsh, G. (ed) Posttranslational Modifications of Protein Biopharmaceuticals, pp 109-147, 2009.

Wehbi, V., Tranchant, T., Durand, G., Musnier, A., Decourtye, J., Piketty, V., Butnev, V.Y., Bousfield, G.R., Crepieux, R., Maurel, M.C., and Reiter, E. Partially deglycosylated equine LH preferentially activates Beta-arrestin-dependent signaling at the follicle-stimulating hormone receptor, Mol. Endocrinol.  24: 561-573, 2010. 

Visvanathan, M., Siddam, S.R., Lee, I.H., Lushington, G.H., Bousfield, G.R.  GlycomicsDB - a data integration platform for glycans and their structures. Open Med. Inform. J.  5:  9-16, 2011. PMC3098536

Bousfield, G.R. and Dias, J.A., Synthesis and secretion of gonadotropins including structure-function correlates. Rev. Endocr. Metab. Disord. 12(4):  289-302, 2011.

Ulloa-Aguirre, A., Dias, J.A., George R. Bousfield, G.R., Huhtaniemi,I.,  and Reiter, E. Trafficking of the Follitropin Receptor. Meth. Enzymol. 251:  17-45, 2013.

Bousfield, G.R., Butnev, V.Y., Butnev, V.Y., Hiromasa, Y., Harvey, D.J., and May, J.V. Hypo-glycosylated human follicle-stimulating hormone (hFSH21/18) is much more active in vitro than fully-glycosylated hFSH (hFSH24), Mol. Cell. Endocrinol. 382:  989-997, 2014

Last modified: Jun 29, 2017


George R. Bousfield, Ph.D.
Dr. Lawrence M. Jones Distinguished Professor
Core Laboratory Director