Effects of preventing O-glycosylation on the secretion of human chorionic gonadotropin in Chinese hamster ovary cells

M. M. Matzuk, M. Krieger, Christopher Corless, I. Boime

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Abstract

Human chorionic gonadotropin (hCG) is a member of a family of heterodimeric glycoprotein hormones that have a common α subunit but differ in their hormone-specific β subunits. The β subunit of hCG (hCGβ) is unique among the β subunits in that it contains four mucin-like O-linked oligosaccharides attached to a carboxyl-terminal extension. To study the effects of O-glycosylation on the secretion and assembly of hCG, expression vectors containing either the hCGβ gene alone or together with the hCGα gene were transfected into a mutant Chinese hamster ovary cell line, ldlD, which exhibits a reversible defect in O-glycosylation. Our results reveal that hCGβ can be secreted normally in the absence of its O-linked oligosaccharides. hCGβ devoid of O-linked carbohydrate can also combine efficiently with hCGα and be secreted as an intact dimer. We conclude that in Chinese hamster ovary cells, the hcGβ O-linked chains play no role in the assembly and secretion of hCG. The normal and O-linked oligosaccharide-deficient forms of hCG secreted by these cells should prove useful in examining the role of O-linked chains on the biological function of hCG.

Original languageEnglish (US)
Pages (from-to)6354-6358
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number18
StatePublished - 1987
Externally publishedYes

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Chorionic Gonadotropin
Cricetulus
Glycosylation
Ovary
Oligosaccharides
Hormones
Mucins
Genes
Glycoproteins
Carbohydrates
Cell Line

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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title = "Effects of preventing O-glycosylation on the secretion of human chorionic gonadotropin in Chinese hamster ovary cells",
abstract = "Human chorionic gonadotropin (hCG) is a member of a family of heterodimeric glycoprotein hormones that have a common α subunit but differ in their hormone-specific β subunits. The β subunit of hCG (hCGβ) is unique among the β subunits in that it contains four mucin-like O-linked oligosaccharides attached to a carboxyl-terminal extension. To study the effects of O-glycosylation on the secretion and assembly of hCG, expression vectors containing either the hCGβ gene alone or together with the hCGα gene were transfected into a mutant Chinese hamster ovary cell line, ldlD, which exhibits a reversible defect in O-glycosylation. Our results reveal that hCGβ can be secreted normally in the absence of its O-linked oligosaccharides. hCGβ devoid of O-linked carbohydrate can also combine efficiently with hCGα and be secreted as an intact dimer. We conclude that in Chinese hamster ovary cells, the hcGβ O-linked chains play no role in the assembly and secretion of hCG. The normal and O-linked oligosaccharide-deficient forms of hCG secreted by these cells should prove useful in examining the role of O-linked chains on the biological function of hCG.",
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T1 - Effects of preventing O-glycosylation on the secretion of human chorionic gonadotropin in Chinese hamster ovary cells

AU - Matzuk, M. M.

AU - Krieger, M.

AU - Corless, Christopher

AU - Boime, I.

PY - 1987

Y1 - 1987

N2 - Human chorionic gonadotropin (hCG) is a member of a family of heterodimeric glycoprotein hormones that have a common α subunit but differ in their hormone-specific β subunits. The β subunit of hCG (hCGβ) is unique among the β subunits in that it contains four mucin-like O-linked oligosaccharides attached to a carboxyl-terminal extension. To study the effects of O-glycosylation on the secretion and assembly of hCG, expression vectors containing either the hCGβ gene alone or together with the hCGα gene were transfected into a mutant Chinese hamster ovary cell line, ldlD, which exhibits a reversible defect in O-glycosylation. Our results reveal that hCGβ can be secreted normally in the absence of its O-linked oligosaccharides. hCGβ devoid of O-linked carbohydrate can also combine efficiently with hCGα and be secreted as an intact dimer. We conclude that in Chinese hamster ovary cells, the hcGβ O-linked chains play no role in the assembly and secretion of hCG. The normal and O-linked oligosaccharide-deficient forms of hCG secreted by these cells should prove useful in examining the role of O-linked chains on the biological function of hCG.

AB - Human chorionic gonadotropin (hCG) is a member of a family of heterodimeric glycoprotein hormones that have a common α subunit but differ in their hormone-specific β subunits. The β subunit of hCG (hCGβ) is unique among the β subunits in that it contains four mucin-like O-linked oligosaccharides attached to a carboxyl-terminal extension. To study the effects of O-glycosylation on the secretion and assembly of hCG, expression vectors containing either the hCGβ gene alone or together with the hCGα gene were transfected into a mutant Chinese hamster ovary cell line, ldlD, which exhibits a reversible defect in O-glycosylation. Our results reveal that hCGβ can be secreted normally in the absence of its O-linked oligosaccharides. hCGβ devoid of O-linked carbohydrate can also combine efficiently with hCGα and be secreted as an intact dimer. We conclude that in Chinese hamster ovary cells, the hcGβ O-linked chains play no role in the assembly and secretion of hCG. The normal and O-linked oligosaccharide-deficient forms of hCG secreted by these cells should prove useful in examining the role of O-linked chains on the biological function of hCG.

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