All-or-none N-glycosylation in primate follicle-stimulating hormone β-subunits

George R. Bousfield, Vladimir Y. Butnev, Wendy J. Walton, Van T. Nguyen, Jennifer Huneidi, Vinod Singh, V. S.Kumar Kolli, David J. Harvey, Naomi E. Rance

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46 Scopus citations

Abstract

Human FSH exists as two major glycoforms designated, tetra-glycosylated and di-glycosylated hFSH. The former possesses both α- and β-subunit carbohydrates while the latter possesses only α-subunit carbohydrate. Western blotting differentiated the glycosylated, 24,000 Mr hFSHβ band from the non-glycosylated 21,000 Mr FSHβ band. Postmenopausal urinary hFSH preparations possessed 75-95% 24,000 Mr hFSHβ, while pituitary hFSH immunopurified from 21- to 43-year-old females and 21-43-year-old males possessed only 35-40% 24,000 Mr hFSHβ. The pituitary hFSH from a postmenopausal woman on estrogen replacement was 75% 21,000 Mr hFSHβ. Other immunopurified postmenopausal pituitary hFSH preparations possessed 50-60% 21,000 Mr hFSHβ. Gel filtration removed predominantly 21,000 Mr free hFSHβ and reduced its abundance to 13-22% in postmenopausal pituitary hFSH heterodimer preparations. A major regulatory mechanism for FSH glycosylation involves control of β-subunit N-glycosylation, possibly by inhibition of oligosaccharyl transferase. Two primate species exhibited the same all-or-none pattern of pituitary FSHβ glycosylation.

Original languageEnglish (US)
Pages (from-to)40-48
Number of pages9
JournalMolecular and Cellular Endocrinology
Volume260-262
DOIs
StatePublished - Jan 2 2007

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Keywords

  • All-or-none pattern
  • Follicle-stimulating hormone
  • N-Glycosylation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology

Cite this

Bousfield, G. R., Butnev, V. Y., Walton, W. J., Nguyen, V. T., Huneidi, J., Singh, V., Kolli, V. S. K., Harvey, D. J., & Rance, N. E. (2007). All-or-none N-glycosylation in primate follicle-stimulating hormone β-subunits. Molecular and Cellular Endocrinology, 260-262, 40-48. https://doi.org/10.1016/j.mce.2006.02.017