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J. Biol. Chem., Vol. 268, Issue 2, 795-802, 01, 1993
PL Smith, GR Bousfield, S Kumar, D Fiete and JU Baenziger
Equine chorionic gonadotropin (eCG) and lutropin (eLH) are heterodimeric
glycoprotein hormones which are synthesized in the placenta and pituitary,
respectively. The beta subunits of eCG and eLH, like their alpha subunits,
arise from a single gene and have identical amino acid sequences. In
contrast, the beta subunits of CG and LH in primates arise from different
genes and differ in sequence. We have examined the structures of the
Asn-linked oligosaccharides on eCG and eLH. eCG bears di- and tri-branched
Asn-linked oligosaccharides terminating with Sia alpha 2,3 or 6Gal beta
1,4GlcNAc. In contrast, > 72% of the Asn-linked oligosaccharides on eLH
have 1 or 2 branches terminating with the sequence SO4-4-GalNAc beta
1,4GlcNAc. The nonsulfated oligosaccharides on eLH are neutral (6% of the
total) or have branches terminating with sialic acid-Gal (22% of the
total). Since the alpha and beta subunits of eCG and eLH both contain the
tripeptide motif, Pro-Xaa-Arg/Lys, recognized by the glycoprotein
hormone-specific GalNAc-transferase found in pituitary, expression of the
GalNAc- and sulfotransferases must differ in the placenta and pituitary.
eLH, but not eCG, is bound by the hepatic endothelial cell receptor
specific for the sequence SO4-4-GalNAc beta 1,4GlcNAc. As a result, eLH is
removed from the circulation 5.7-fold more rapidly than eCG and is
selectively localized to the liver. Since the major structural difference
between eCG and eLH is in the terminal glycosylation of their Asn-linked
oligosaccharides and this has a major impact on circulatory half-life, it
is likely that the difference in circulatory half-life defines the
functional difference between eCG and eLH.
Equine lutropin and chorionic gonadotropin bear oligosaccharides terminating with SO4-4-GalNAc and Sia alpha 2,3Gal, respectively
Department of Pathology, Washington University School of Medicine, St. Louis, Missouri 63110.
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