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

Research output: Contribution to journalArticlepeer-review

59 Scopus citations


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
StatePublished - Jan 2 2007


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

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology


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