Differential processing of Asn-linked oligosaccharides on pituitary glycoprotein hormones: implications for biologic function

Eric D. Green, Irving Boime, Jacques U. Baenziger

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

Luteinizing hormone, follicle-stimulating hormone, and thyroid-stimulating hormone from pituitary and chorionic gonadotropin from placenta are a family of glycoproteins, each consisting of an α and β subunit. Within an animal species, the α subunit of all four hormones contains the identical amino acid sequence, while each β subunit is distinct and confers biologic specificity to the hormone dimer. Despite sharing common α subunits, these hormones bear Asn-linked oligosaccharides which differ in structure. Whereas chorionic gonadotropin contains exclusively neutral and sialylated oligosaccharides, the pituitary hormones bear neutral, sialylated, sulfated, and sialylated/sulfated structures. The sulfated oligosaccharides are unique in structure and are more prevalent on certain pituitary hormones, indicating that the synthesis of these unusual oligosaccharides is tightly regulated. The differences in oligosaccharide structures in conjunction with the highly specific endocrine responses elicited by these hormones, suggest an important functional role for the oligosaccharides, such as metabolic clearance, control of hormone response, modulation of hormone potency, and/or intracellular sorting of hormones into separate secretory granules.

Original languageEnglish
Pages (from-to)81-100
Number of pages20
JournalMolecular and Cellular Biochemistry
Volume72
Issue number1-2
DOIs
StatePublished - Nov 1986

Keywords

  • glycoprotein
  • hormone
  • oligosaccharides
  • pituitary
  • sialylation
  • sulfation

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