Synthesis of phosphorylated oligosaccharides in lysozyme is enhanced by fusion to cathepsin D.

摘要: Chinese hamster ovary cells transfected with human lysozyme cDNA encoding Asn instead of Gly22 synthesize a mutant lysozyme, [Asn22]lysozyme, about 60% the molecules bearing carbohydrate. This carbohydrate is predominantly complex type and contains varied number lactosamine repeats. In this study we show that glycosylation [Asn22] fused to cathepsin D altered relative [Asn22]lysozyme alone. The fusion protein synthesized as 66-kDa precursor cleaved enzymatically active antigenically positive lysozyme. As compared moiety shows an increased N-glycosylation decreased synthesis Cleavage L has revealed portion secreted bears intracellularly released trimmed oligosaccharides. presence NH4Cl lysosomal targeting inhibited. then enriched in phosphorylated high mannose oligosaccharides their moiety. Our results indicate processing including 6-phosphate residues repeats, by attached D. phosphorylation on very efficient concerned molecules.