[Syntheses and biological activities of glycoconjugates].

This review describes the oligosaccharide syntheses and biological activities of glycosphingolipids, focusing especially on those found in invertebrates like millipedes, nematoda parasites, and cestoda parasites, and model compounds related to a major antigenic epitope against antibupleurum 2IIc/PG-1-IgG from antiulcer pectic polysaccharides. A novel and simple approach for the rational design of glycoclusters and glycodendrimers by coupling with a sugar unit and a cluster unit, was developed with beta-alanine derivatives used to construct the latter compounds.

Oligosaccharides and glycoconjugates in bovine milk and colostrum.

Oligosaccharides and glycoconjugates are some of the most important bioactive components in milk. A great deal of information is available on the biological function of the components from human milk. Their primary role seems to be in providing protection against pathogens by acting as competitive inhibitors for the binding sites on the epithelial surfaces of the intestine. Evidence is also available to support the role of some of these components as growth promoters for genera of beneficial microflora in the colon. Compared with human milk, levels of oligosaccharides in bovine milk are very low. Nevertheless, a number of neutral and acidic oligosaccharides have been isolated from bovine milk and characterised. The highest concentration of these molecules is found in early postparturition milk (colostrum). The chemical structure of the oligosaccharides and many of the glycoconjugates from bovine milk are similar to those in human milk. It is likely that bovine oligosaccharides and glycoconjugates can be used in milk products as bioactive components in human nutrition.

Specific glycoconjugates are present at the oolemma of the fertilization site in the egg of Discoglossus pictus (Anurans) and bind spermatozoa in an in vitro assay.

In the egg of the anuran Discoglossus pictus, the site of fertilization is restricted to the central portion of an animal hemisphere indentation (the dimple). Previous studies showed that the acrosome reaction of D. pictus sperm is triggered in the jelly, and yet sperm arrive at the dimple surface with the plasma membrane at an early stage of vesiculation. Reactivity of the dimple surface with specific lectins suggests that fucose might be utilized as a marker of glycoproteins located at the dimple surface. In this paper, proteins of the egg surface were labeled with the membrane impermeable sulfo-NHS-biotin. Four main bands of 200, 230, 260, and 270 kDa labeled only at the dimple surface, although they were detected in the cortex of the whole egg. The 270-kDa band reacted with Galanthus nivalis agglutinin only in the cortex of the dimple, suggesting that this band is differently glycosylated according to its localization. The alpha-l-fucose-specific lectin Ulex europaeus agglutinin I was utilized both in lectin blotting and in affinity chromatography and cross-reacted with the 200- and 270/260-kDa bands. Furthermore, two polypeptides were obtained by exposure of intact eggs to lysylendoproteinase C. They were also reactive to Ulex europaeus agglutinin I. The 200- and 270/260-kDa bands were eluted from the acrylamide gels and adsorbed to polystyrene beads. An assay for sperm binding to 200-kDa glycoprotein-bound beads was developed. Sperm stuck to the beads before but not after Ca-ionophore treatment. When the beads were coated with the 270/260-kDa glycoproteins, binding occurred after ionophore treatment. In these assays, the 200- and 270/260-kDa glycoproteins competitively inhibited sperm binding to the beads coated with the corresponding glycoprotein. These results indicate that the assayed glycoproteins, located either in the glycocalyx or in the plasma membrane of the fertilization site, are involved in sperm binding.