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Histochemical analysis of rat testicular glycoconjugates. 3. Non-reducing terminal residues in seminiferous tubules
Authors:Carolyn J P Jones  Christopher A Morrison and Robert W Stoddart
Institution:(1) Department of Pathological Sciences, University of Manchester, Oxford Road, M13 9PT Manchester, UK;(2) Department of Immunology, University of Manchester, Oxford Road, M13 9PT Manchester, UK;(3) Present address: Immunology Group, CIBA GEIGY Animal Health Ltd, Centre de Recherches Agricoles, CH-1566, St-Aubin (FR), Switzerland
Abstract:Summary Lectins of Helix pomatia (HPA), Glycine max (SBA), Vicia villosa (VVA), Dolichos biflorus (DBA), Ulex europaeus (UEA-1), Tetragonolobus purpureus (LTA), Griffonia simplicifolia (BSA-1B4), Maclura pomifera (MPA), Sambucus nigra (SNA) and Maackia amurensis (MAA) were used to explore the distribution of saccharides characteristic of non-reducing termini of O- and N-linked glycoprotein glycans in the seminiferous tubules of rat testis. Sialyl residues (both agr2,3- and agr2,6-linked, as shown by MAA and SNA respectively) and agr-l-fucosyl residues (shown by UEA-1 and LTA) were expressed on spermatogonia, spermatocytes and spermatozoa, but not on spermatids. In contrast, 2-deoxy-2-acetamido-agr-d-galactosyl termini were abundant on spermatozoa, but not on any of their precursors (as shown by HPA, SBA and VVA). All occurred on both O- and N-linked glycans.Sertoli cells expressed small amounts of fucose and agr2,3-linked sialic acid, and abundant agr2,6 sialyl residues, largely on N-glycans. agr-Galactosyl residues were readily detected on the tubular basement membrane, but not elsewhere.
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