Human leukocyte glycosylasparaginase: Cell-to-cell transfer and properties in correction of aspartylglycosaminuria

2Citations
Citations of this article
5Readers
Mendeley users who have this article in their library.

Abstract

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. © 2001 Federation of European Biochemical Societies.

Cite

CITATION STYLE

APA

Dunder, U., & Mononen, I. (2001). Human leukocyte glycosylasparaginase: Cell-to-cell transfer and properties in correction of aspartylglycosaminuria. FEBS Letters, 499(1–2), 77–81. https://doi.org/10.1016/S0014-5793(01)02526-1

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free