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

doi:10.1016/j.mce.2006.02.017

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 journal › Article › peer-review

60 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 M_r hFSHβ band from the non-glycosylated 21,000 M_r FSHβ band. Postmenopausal urinary hFSH preparations possessed 75-95% 24,000 M_r hFSHβ, while pituitary hFSH immunopurified from 21- to 43-year-old females and 21-43-year-old males possessed only 35-40% 24,000 M_r hFSHβ. The pituitary hFSH from a postmenopausal woman on estrogen replacement was 75% 21,000 M_r hFSHβ. Other immunopurified postmenopausal pituitary hFSH preparations possessed 50-60% 21,000 M_r hFSHβ. Gel filtration removed predominantly 21,000 M_r 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 language	English (US)
Pages (from-to)	40-48
Number of pages	9
Journal	Molecular and Cellular Endocrinology
Volume	260-262
DOIs	https://doi.org/10.1016/j.mce.2006.02.017
State	Published - Jan 2 2007

Keywords

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

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Endocrinology

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10.1016/j.mce.2006.02.017

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@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.}",

note = "Funding Information: We thank Dr. Cindy Bethea, Oregon National Primate Research Center, and Dr. Tony Plant, University of Pittsburg School of Medicine, for the gifts of monkey pituitary glands. The project described was supported by NIH Grant Numbers P20 RR16475 from the INBRE Program and P20 RR017708 from the COBRE Program of the National Center for Research Resources, the National Science Foundation under EPS-9874732, and matching support from the State of Kansas. Waters-Micromass TofSpec mass spectrometer was obtained by a grant from Biotechnology and Biological Sciences Research Council (J.D.H.).",

year = "2007",

month = jan,

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",

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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.

N1 - Funding Information: We thank Dr. Cindy Bethea, Oregon National Primate Research Center, and Dr. Tony Plant, University of Pittsburg School of Medicine, for the gifts of monkey pituitary glands. The project described was supported by NIH Grant Numbers P20 RR16475 from the INBRE Program and P20 RR017708 from the COBRE Program of the National Center for Research Resources, the National Science Foundation under EPS-9874732, and matching support from the State of Kansas. Waters-Micromass TofSpec mass spectrometer was obtained by a grant from Biotechnology and Biological Sciences Research Council (J.D.H.).

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

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U2 - 10.1016/j.mce.2006.02.017

DO - 10.1016/j.mce.2006.02.017

M3 - Article

C2 - 17079072

AN - SCOPUS:33751256292

SN - 0303-7207

VL - 260-262

SP - 40

EP - 48

JO - Molecular and Cellular Endocrinology

JF - Molecular and Cellular Endocrinology

ER -

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

Abstract

Keywords

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