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Evolutionary conservation of the sulfated oligosaccharides on vertebrate glycoprotein hormones that control circulatory half-life.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1995 Sep 15; Vol. 270 (37), pp. 21665-71. - Publication Year :
- 1995
-
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-GalNAc beta 1,4GlcNAc. A cluster of basic amino acids essential for recognition of the alpha subunit by the glycoprotein hormone:N-acetylgalactosaminyltransferase is located within two turns of an alpha 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 alpha 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-GalNAc beta 1,4GlcNAc are present on the alpha and beta subunits of the salmon glycoprotein hormone GTH II. Asn-linked oligosaccharides terminating with SO4-4-GalNAc beta 1,4GlcNAc 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.
- Subjects :
- Amino Acid Sequence
Animals
Carbohydrate Conformation
Carbohydrate Sequence
Chickens
Chorionic Gonadotropin metabolism
Conserved Sequence
Half-Life
Humans
Molecular Sequence Data
Oligosaccharides isolation & purification
Oncorhynchus kisutch
Protein Structure, Secondary
Rana catesbeiana
Rats
Substrate Specificity
Sulfates analysis
Transferrin metabolism
Turtles
Vertebrates
Biological Evolution
Glycoprotein Hormones, alpha Subunit chemistry
Glycoprotein Hormones, alpha Subunit metabolism
Luteinizing Hormone chemistry
Luteinizing Hormone metabolism
N-Acetylgalactosaminyltransferases metabolism
Oligosaccharides chemistry
Pituitary Gland metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 270
- Issue :
- 37
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 7545167
- Full Text :
- https://doi.org/10.1074/jbc.270.37.21665