PubMed · 2734
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M D Ward, E R Squibb. 1975. Proceedings: A nystatin-acid solid state interaction study.. https://pubmed.ncbi.nlm.nih.gov/2734/
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Recognition of defined carbohydrate structures by boar sperm was studied on the basis of oligosaccharide structures of porcine zona pellucida glycoproteins so far elucidated. Boar sperm abundantly adhered to fetuin-Sepharose beads, moderately to asialofetuin-Sepharose beads, but not at all to galactosidase (beta1-4-linkage-specific)-digested asialofetuin-Sepharose beads. The sperm also adhered to Le(x) oligosaccharide probe-coupled avidin-Sepharose beads. These adhesive activities were retained in the medium containing EDTA instead of calcium ion but abolished after induction of acrosome reaction by preincubation of sperm with calcium ionophore. Inhibition study of sperm adhesion to the beads by soluble ligands demonstrated that boar sperm express at least two kinds of carbohydrate recognition molecules, one recognizing both sialyl and nonsialyl N-acetyllactosamines but not the Le(x) structure and the other recognizing the Le(x) structure but not N-acetyllactosamines. Sperm binding to the zona pellucida on fixed porcine oocytes was inhibited by N-glycans of fetuin and their asialo form but not by the asialo, agalacto-N-glycans. Finally, dextran-based multivalent oligosaccharide polymers were prepared and their inhibitory activities in sperm-oocyte binding were examined. The result indicated that the polymer composed of fetuin N-glycans, its asialo-N-glycans, or lacto-N-fucopentaose III causes a remarkable inhibition at the oligosaccharide-based concentration of 50 microM. Thus, boar sperm are suggested to express multiple carbohydrate recognition molecules which may be involved in the sperm-egg interaction.
Conjugates of antiviral and antiblastic nucleoside analogs (NAs) with galactosyl-terminating peptides selectively enter hepatocytes after binding of the carrier galactose residues to the asialoglycoprotein receptor. Since NAs, when set free from the carrier within hepatocytes, partly exit from these cells into the bloodstream, we considered the possibility that administration of galactosyl-terminating conjugates of NAs could result in plasma concentrations of these drugs that would be higher in liver sinusoids than in capillaries of other organs. In the present study we demonstrated the validity of this hypothesis. We injected rats with a conjugate of adenine arabinoside (ara-A) with lactosaminated poly-L-lysine and found that the plasma concentrations of ara-A were >2-fold higher in blood of liver than in systemic circulation. Liver blood was collected from the inferior vena cava after closing below and above the outflows of the hepatic veins. The present result suggests that conjugation with galactosyl-terminating peptides might be a way to selectively increase the concentrations of NAs not only in hepatocytes, which have the asialoglycoprotein receptor, but also in cells infiltrating the liver, such as neoplastic cells of micrometastases nourished by hepatic sinusoids.
E-selectin is a cytokine-inducible, calcium-dependent endothelial cell adhesion molecule that plays a critical role in the leucocyte-endothelium interaction during inflammation and is thought to contribute to the metastatic dissemination of tumour cells. Like the other selectins, E-selectin binds to ligands carrying the tetrasaccharide sialyl-Lewis x (NeuAcalpha2,3Galbeta1,4[Fucalpha1, 3]GlcNAc)1 or its isomer sialyl-Lewis a (NeuAcalpha2, 3Galbeta1, 3[Fucalpha1,4]GlcNAc). We examined the effect of expressing the H-type alpha(1,2)-fucosyltransferase or the alpha(2, 6)-sialyltransferase on the synthesis of sialyl-Lewis x by alpha(1, 3)fucosyltransferase. We found that H-type alpha(1, 2)-fucosyltransferase but not alpha(2,6)-sialyltransferase, strongly inhibited sialyl-Lewis x expression and E-selectin adhesion. We assume that H-type alpha(1,2)-fucosyltransferase competes with the endogenous alpha(2,3)-sialyltransferase for the N-acetyllactosamine structures assigned to further serve as acceptors for alpha(1, 3)fucosyltransferase.