M. Hummel et al., ELONGATION OF N-ACETYLLACTOSAMINE REPEATS IN DIANTENNARY OLIGOSACCHARIDES, European journal of biochemistry, 245(2), 1997, pp. 428-433
Glycosylated [Asn22]lysozyme has been shown to contain N-acetyllactosa
mine repeats when expressed in chinese hamster ovary (CHO) cells. We f
ind that the major portion of N-acetyllactosamine repeats are associat
ed with diantennary oligosaccharides. In Led CHO cells, which are defi
cient in sialylation, glycosylated lysozyme is synthesized with increa
sed contents of N-acetyllactosamine repeats terminating in beta-galact
osyl 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-acetylglucosa
minyl transferase and by the synthesis of beta-1,6-linked antennae. Th
e results with glycosylated lysozyme suggest that glycoproteins bearin
g diantennary oligosaccharides can contain several N-acetyllactosamine
repeats and that the number of the latter can be increased by decreas
ing the activity of the capping sialyl transferases.