Glycobiology vol 3 no 4 pp. 339-348, 1993
© 1993
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Comparative analysis of the N-glycans of rat, mouse and human Thy-1. Site-specific oligosaccharide patterns of neural Thy-1, a member of the immunoglobulin superfamily
1MRC Cellular Immunology Unit, Sir William Dunn School of Pathology, University of Oxford South Parks Road, Oxford, OX1 3RE
2Oxford GlycoSystems Ltd Abingdon, Oxon., OX14 1RG
3Glycobiology Institute, Department of Biochemistry, University of Oxford South Parks Road, Oxford, OX1 3QU
4MRC Immunochemistry Unit, Department of Biochemistry, University of Oxford South Parks Road, Oxford, OX1 3QU
5Division of Cell and Molecular Biology, Institute of Child Health 30 Guilford Street, London WC1N 1EH, UK
7To whom correspondence should be addressed
Received on December 14, 1992; revised on April 13, 1993; accepted on April 14, 1993
Protein structure and tissue type are known to influence glycosylation of proteins. We have previously investigated the N-glycans at each of the three glycosylation sites of the cell surface glycoprotein Thy-1 when isolated from rat brain and thymocytes. Here we report a comparative analysis of the site-specific N-glycosylation patterns from rat (Asn 23, 74, 98), mouse (Asn 23, 75, 99) and human (Asn 23, 60, 100) neural Thy-1. Despite considerable differences in amino acid sequence, the results show a remarkable conservation of the pattern of N-glycans at corresponding sites between the three species, as judged by chromatographic comparisons and glycosidase susceptibility. This is particularly marked for sites at Asn 74/75 in rat/mouse and the equivalent site at 60 in human Thy-1, as well as for sites at Asn 98/99 and 100, respectively. The sites at Asn 23 in rat/mouse also contained almost identical glycosylation paterns, but at this site human Thy-1 showed significantly different glycosylation patterns. These site glycosylation patterns are discussed in relation to the likely accessibility of the oligosaccharides for processing. It is known that within a species, the glycosylation of Thy-1 is tissue specific; therefore, this degree of conservation of glycosylation of Thy-1 expressed in the same tissue in different species is all the more striking, given the known variation between species in the amino acid sequence of Thy-1. It is therefore proposed that neural cells have a particular requirement for specific surface carbohydrates and that the Thy-1 polypep-tide serves as an appropriate carrier for these structures.
glycosylation site-specific Thy-1
6Present address: Institute for Biomedical Science, Division of Molecular Pathology, Windeger Building, University College Medical School, London W1P 6DB, UK
8Dedicated to Professor Alan F. Williams
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