Glycobiology Advance Access originally published online on March 19, 2004
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Glycobiology vol 14 no 4 pp. 365-372, 2004
Glycobiology vol. 14 no. 4 © Oxford University Press 2004; all rights reserved.
Donor specificity in the glycosylation of Tamm-Horsfall glycoprotein: Conservation of the Sda determinant in pairs of twins
Bijvoet Center, Department of Bio-Organic Chemistry, Section of Glycoscience and Biocatalysis, Utrecht University, Padualaan 8, NL-3584 CH Utrecht, The Netherlands
Received on December 19, 2003; revised on January 22, 2004; accepted on January 27, 2004
The content of the Sda determinant in urinary human Tamm-Horsfall glycoprotein (THp) has been reported to be donor-specific. This feature was further addressed by investigating THp from genetically identical individuals. To this end, THp was isolated from the urine of two monozygotic pairs of twins (A and B). The four samples (THp A1, A2, B1, and B2) were subjected to endo-ß-galactosidase from Bacteroides fragilis leading to the liberation of the Neu5Ac(
2-3)Gal (ß1-4)GlcNAc(ß1-3)Gal and Neu5Ac(
2-3)[GalNAc(ß1-4)] Gal(ß1-4)GlcNAc(ß1-3)Gal (Sda epitope) motifs, both located at the nonreducing termini of complex type N-glycans. The isolated mixtures of oligosaccharides were analyzed for the absolute and relative amounts of the two oligosaccharides. The obtained data clearly indicate that in THp A1 and A2, and in THp B1 and B2, the molar ratios of the tetra- and Sda pentasaccharide are identical for a pair of twins. This conservation of molar ratios points to an identical relative expression of ß-1,4-N-acetylgalactosaminyltransferase activity involved in the biosynthesis of the Sda determinant. Apparently, the degree of conversion of the tetrasaccharidic Sda precursor into the final pentasaccharidic Sda form can be considered to result from a very closely related pattern of glycosylation for genetically homogeneous individuals.
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