Evolutionary conservation of the sulfated oligosaccharides on vertebrate glycoprotein hormones that control circulatory half-life

S. M. Manzella, S. M. Dharmesh, M. C. Beranek, P. Swanson, J. U. Baenziger

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35 Scopus citations

Abstract

The circulatory half-life of the mammalian glycoprotein hormone lutropin is controlled by its unique Asn-linked oligosaccharides, which terminate with the sequence SO4-4-GalNAcβ1,4GlcNAc. A cluster of basic amine acids essential for recognition of the α subunit by the glycoprotein hormone:N- acetylgalactosaminyltransferase is located within two turns of an α helix (Mengeling, B. J., Manzella, S. M., and Baenziger, J. U. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 502-506). The amino acids within this region are virtually invariant in the a subunits of all vertebrates, indicating that the recognition determinant utilized by the N-acetylgalactosaminyltransferase has been conserved in species ranging from teleost fish to mammals. We demonstrate that the glycoprotein hormone:N-acetylgalactosaminyltransferase and the N-acetylgalactosamine-4-sulfotransferase responsible for the synthesis of these unique sulfated oligosaccharides are expressed in the pituitaries of vertebrates ranging from teleost fish to mammals. Furthermore, we show that Asn-linked oligosaccharides terminating with SO4-4- GalNAcβ1,4GlcNAc are present on the α and β subunits of the salmon glycoprotein hormone GTH II. Asn-linked oligosaccharides terminating with SO4-4-GalNAcβ1,4GlcNAc are unique structural features of the glycoprotein hormones that have been conserved during vertebrate evolution, suggesting they are critical for the expression of hormone biologic activity.

Original languageEnglish
Pages (from-to)21665-21671
Number of pages7
JournalJournal of Biological Chemistry
Volume270
Issue number37
DOIs
StatePublished - 1995

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