Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1.

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Abstract
To examine the extent to which protein structure and tissue‐type influence glycosylation, we have determined the oligosaccharide structures at each of the three glycosylation sites (Asn‐23, 74 and 98) of the cell surface glycoprotein Thy‐1 isolated from rat brain and thymus. The results show that there is tissue‐specificity of glycosylation and that superimposed on this is a significant degree of site‐specificity. On the basis of the site distribution of oligosaccharides, we find that no Thy‐1 molecules are in common between the two tissues despite the amino acid sequences being identical. We suggest, therefore, that by controlling N‐glycosylation a tissue creates an unique set of glycoforms (same polypeptide but with oligosaccharides that differ either in sequence or disposition). The structures at each of the three sites were also determined for the thymocyte Thy‐1 that binds to lentil lectin (Thy‐1 L+) and for that which does not (Thy‐1 L‐). Segregation of intact thymus Thy‐1 into two distinct sets of glycoforms by lentil lectin was found to be due to the structures at site 74. Analysis of oligosaccharide structures at the ‘passenger’ sites (23 and 98) suggests that either Thy‐1 L+ and Thy‐1 L‐ molecules are made in different cell‐types or that the biosynthesis of oligosaccharides at one site is influenced by the glycosylation at other sites.