TY - JOUR
T1 - Differential processing of Asn-linked oligosaccharides on pituitary glycoprotein hormones
T2 - implications for biologic function
AU - Green, Eric D.
AU - Boime, Irving
AU - Baenziger, Jacques U.
PY - 1986/11
Y1 - 1986/11
N2 - 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.
AB - 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.
KW - glycoprotein
KW - hormone
KW - oligosaccharides
KW - pituitary
KW - sialylation
KW - sulfation
UR - http://www.scopus.com/inward/record.url?scp=0022858517&partnerID=8YFLogxK
U2 - 10.1007/BF00230637
DO - 10.1007/BF00230637
M3 - Article
C2 - 3102943
AN - SCOPUS:0022858517
SN - 0300-8177
VL - 72
SP - 81
EP - 100
JO - Molecular and Cellular Biochemistry
JF - Molecular and Cellular Biochemistry
IS - 1-2
ER -