부산대학교 도서관

Aspartylglycosaminuria (AGU), a severe lysosomal storage disease, is caused by the deficiency of the lysosomal enzyme, glycosylasparaginase (GA), and accumulation of aspartylglucosamine (GlcNAc‐Asn) in tissues. Here we show that human leukocyte glycosylasparaginase can correct the metabolic defect in Epstein–Barr virus (EBV)‐transformed AGU lymphocytes rapidly and effectively by mannose‐6‐phosphate receptor‐mediated endocytosis or by contact‐mediated cell‐to‐cell transfer from normal EBV‐transformed lymphocytes, and that 2–7% of normal activity is sufficient to correct the GlcNAc‐Asn metabolism in the cells. Cell‐to‐cell contact is obligatory for the transfer of GA since normal transformed lymphocytes do not excrete GA into extracellular medium. The combined evidence indicates that cell‐to‐cell transfer of GA plays a main role in enzyme replacement therapy of AGU by normal lymphocytes.