Elongation of N-acetyllactosamine repeats in diantennary oligosaccharides.

Abstract

Glycosylated [Asn22]lysozyme has been shown to contain N-acetyllactosamine repeats when expressed in chinese hamster ovary (CHO) cells. We find that the major portion of N-acetyllactosamine repeats are associated with diantennary oligosaccharides. In Lec2 CHO cells, which are deficient in sialylation, glycosylated lysozyme is synthesized with increased contents of N-acetyllactosamine repeats terminating in beta-galactosyl residues. In the Lec2 cells and the parental CHO cell line, Pro 5, only a minor portion of the oligosaccharides in lysozyme are of the triantennary type. Previously, it has been shown that the synthesis of N-acetyllactosamine repeats in Asn-linked oligosaccharides is enhanced by an increase in the activity of the elongating beta-N-acetylglucosaminyl transferase and by the synthesis of beta-1,6-linked antennae. The results with glycosylated lysozyme suggest that glycoproteins bearing diantennary oligosaccharides can contain several N-acetyllactosamine repeats and that the number of the latter can be increased by decreasing the activity of the capping sialyl transferases.