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 journalArticle

45 Citations (Scopus)

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

Fingerprint

Human Follicle Stimulating Hormone
Glycosylation
Follicle Stimulating Hormone
Primates
Carbohydrates
Estrogen Replacement Therapy
Transferases

Keywords

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

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Cite this

All-or-none N-glycosylation in primate follicle-stimulating hormone β-subunits. / Bousfield, George R.; Butnev, Vladimir Y.; Walton, Wendy J.; Nguyen, Van T.; Huneidi, Jennifer; Singh, Vinod; Kolli, V. S Kumar; Harvey, David J.; Rance, Naomi E.

In: Molecular and Cellular Endocrinology, Vol. 260-262, 02.01.2007, p. 40-48.

Research output: Contribution to journalArticle

Bousfield, GR, Butnev, VY, Walton, WJ, Nguyen, VT, Huneidi, J, Singh, V, Kolli, VSK, Harvey, DJ & Rance, NE 2007, 'All-or-none N-glycosylation in primate follicle-stimulating hormone β-subunits', Molecular and Cellular Endocrinology, vol. 260-262, pp. 40-48. https://doi.org/10.1016/j.mce.2006.02.017
Bousfield, George R. ; Butnev, Vladimir Y. ; Walton, Wendy J. ; Nguyen, Van T. ; Huneidi, Jennifer ; Singh, Vinod ; Kolli, V. S Kumar ; Harvey, David J. ; Rance, Naomi E. / All-or-none N-glycosylation in primate follicle-stimulating hormone β-subunits. In: Molecular and Cellular Endocrinology. 2007 ; Vol. 260-262. pp. 40-48.
@article{96c85332d4f14f5c8a8a0df974702eac,
title = "All-or-none N-glycosylation in primate follicle-stimulating hormone β-subunits",
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.",
keywords = "All-or-none pattern, Follicle-stimulating hormone, N-Glycosylation",
author = "Bousfield, {George R.} and Butnev, {Vladimir Y.} and Walton, {Wendy J.} and Nguyen, {Van T.} and Jennifer Huneidi and Vinod Singh and Kolli, {V. S Kumar} and Harvey, {David J.} and Rance, {Naomi E}",
year = "2007",
month = "1",
day = "2",
doi = "10.1016/j.mce.2006.02.017",
language = "English (US)",
volume = "260-262",
pages = "40--48",
journal = "Molecular and Cellular Endocrinology",
issn = "0303-7207",
publisher = "Elsevier Ireland Ltd",

}

TY - JOUR

T1 - All-or-none N-glycosylation in primate follicle-stimulating hormone β-subunits

AU - Bousfield, George R.

AU - Butnev, Vladimir Y.

AU - Walton, Wendy J.

AU - Nguyen, Van T.

AU - Huneidi, Jennifer

AU - Singh, Vinod

AU - Kolli, V. S Kumar

AU - Harvey, David J.

AU - Rance, Naomi E

PY - 2007/1/2

Y1 - 2007/1/2

N2 - 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.

AB - 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.

KW - All-or-none pattern

KW - Follicle-stimulating hormone

KW - N-Glycosylation

UR - http://www.scopus.com/inward/record.url?scp=33751256292&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33751256292&partnerID=8YFLogxK

U2 - 10.1016/j.mce.2006.02.017

DO - 10.1016/j.mce.2006.02.017

M3 - Article

C2 - 17079072

AN - SCOPUS:33751256292

VL - 260-262

SP - 40

EP - 48

JO - Molecular and Cellular Endocrinology

JF - Molecular and Cellular Endocrinology

SN - 0303-7207

ER -