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Of poly-A-acetyllactosamine

Murata T, Honda H, Hattori T, Usui T. Enzymatic synthesis of poly-A -acetyllactosamines as potential substrates for 23. [Pg.418]

Analysis of glycopeptides of different cell type in culture has revealed that at least small amounts of poly-A-acetyllactosamine chains are present in all cell lines analyzed [39], Interestingly, in the cells of neural origin the poly-A-acetyllactosamine glycans were mainly of the linear type, whereas those of other cell types were mainly branched. [Pg.60]

Labelling of the cell surface of PC 12 pheochromocytoma cells for the presence of poly-A-acetyllactosamine chains identifies a restricted number of glycoproteins as carriers of these glycans (Fig. 7). Induced neuronal differentiation of the cells in culture... [Pg.61]

In granulocytes, no branching of poly-Al-acetyllactosamines is observed, a 1-3-Fucosyltrans-ferase-catalyzed modification of the linear chains leads to the Lewis x antigen. If a2-3-sia-lyltransferase acts before fucosylation, sialyl Lewis x is formed. These carbohydrate stmc-tures are involved in a number of cell-cell interactions during the inflammatory response and... [Pg.1752]

The poly-iV-acetyllactosamine glycans were first discovered as constituents of N-glycans in erythrocytes [36] and teratocarcinoma cells [37], in which they represent a major fraction of the cell surface carbohydrates. In contrast, analysis of whole brain tissue does not indicate the presence of major amounts of poly-77-acetyllactosamine chains [15]. That poly-A -acetyllactosamine glycans do exist in brain tissue is suggested by their accumulation in GMl-gangliosidosis [38]. Small amounts are also present in the form of keratan sulfate as 0-mannose linked chains (see above). [Pg.60]

Fig. 5. Induction of poly-iV-acetyllactosamine expression in differentiating mouse neuroblastoma cells. N1E-115 neuroblastoma cells were grown in the undifferentiated form or induced to differentiate by serum starvation for ten days. The glycopeptides metabolically labelled with H-glucosamine were prepared by pronase digestion and fractionated by gel filtration on a column of Bio-Gel P-100. The poIy-fV-acetyllactosamine glycopeptides (poly-LacNAc) were eluted in the fractions indicated by the bar [39]. Fig. 5. Induction of poly-iV-acetyllactosamine expression in differentiating mouse neuroblastoma cells. N1E-115 neuroblastoma cells were grown in the undifferentiated form or induced to differentiate by serum starvation for ten days. The glycopeptides metabolically labelled with H-glucosamine were prepared by pronase digestion and fractionated by gel filtration on a column of Bio-Gel P-100. The poIy-fV-acetyllactosamine glycopeptides (poly-LacNAc) were eluted in the fractions indicated by the bar [39].
Pierce, M, J Arango (1986) Rous sarcoma virus-transformed baby hamster kidney cells express higher levels of asparagine-linked tri- and tetraantennary glycopeptides containing [GlcNAc-beta (1,6)Man-alpha (1,6)Man] and poly-A-acetyllactosamine sequences than baby hamster kidney cells. J Biol Chem 261 10772-10777... [Pg.155]

Kupper, C.E., Rosencrantz, R.R., Henssen, B., Pelantova, H., Thones, S., Drozdova, A., Kren, V., and Elling, L. (2012) Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment. Beilstein J. Org. Chem., 8, 712-725. [Pg.160]

Feizi, T., E.F. Hounsell, J. Alais, A. Veyrieres, and S. David. 1992. Further definition of the size of the blood group-I antigenic determinant using a chemically synthesised octasaccharide of poly-N-acetyllactosamine type. Carbohyd. Res. 10 289-297. [Pg.1824]

Do, K.-Y, Smith, D. F., and Cummings, R. D., 1990, LAMP-1 in Cho cells is a primary carrier of poly-N-acetyllactosamine chains and is bound preferentially by a mammalian S-type lectin, Biochem. Biophys. Res. Commun. 173 1123-1128. [Pg.186]


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