Abstract
CURRENT emphasis in research on lysosomal storage diseases is directed towards enzyme replacement therapy (ERT) for these inherited enzyme deficiencies1–3. The rationale for ERT is based on the assumption that endocytosed enzyme would enter lysosomes and function in the degradation of accumulated substrates. However, inactivation of enzyme, immunological reactions and low cellular uptake have prevented successful application of this promising approach to therapy. Circumvention of these limitations requires the use of carriers which protect and stabilise replacement enzyme while enhancing uptake and subcellular distribution2–5. We report here the use of lipid vesicles (liposomes)6–9 as carriers for replacement enzyme in feline GM1 gangliosidosis fibroblasts which have deficient β-galactosidase (β-gal) activity and lysosomal storage of glycopeptides9–11. Our results demonstrate increased β-gal activity and corresponding catabolism of stored glycopeptides in feline GM1 gangliosidosis fibroblasts treated with liposomes containing β-gal.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Hers, H. G. & Van Hoof, F. Lysosomes and Storage Diseases 147–149 (Academic, New York, 1973).
Rietra, P. J. G. H., van den Burgh, F. A. J. M. & Tager, M. M. in Enzyme Therapy in Lysosomal Storage Diseases (eds Tager, J. M, Hooghwinkel, G. J. M & Daems, W. Th.) 53–79 (Eisevier, New York, 1974).
Desnick, R. J., Thorpe, S. R. & Fiddler, M. B. Physiol. Rev. 56, 57–99 (1976).
Hickman, S., Shapiro, L. J. & Neufeld, E. F. Biochem. biophys. Res. Commun. 57, 55–61 (1974).
Kaplan, A., Achord, D. T. & Sly, W. S. Proc. natn. Acad. Sci. U.S.A. 74, 2026–2030 (1977).
Bangham, A. D., Hill, M. W. & Miller, N. G. A. in Methods in Membrane Biology (ed Korn, E. D.) 1–100 (Plenum, New York, 1974).
Gregoriadis, G. New Engl. J. Med. 295, 704–710, 765–770 (1976).
Finkelstein, M. & Weissmann, G. J. Lipid Res. 19, 289–303 (1978).
Baker, H. J., Mole, J. A., Lindsey, J. R. & Creel, R. M. Fedn Proc. 35, 1193–1236 (1976).
Anderson, J. A., Mole, J. E. & Baker, H. J. Biochemistry 17, 467–473 (1978).
Reynolds, G. D. & Baker, H. J. Fedn Proc. 37, 745 (1978).
Paul, J. in Cell and Tissue Culture 1–100 (Churchill-Livingstone, New York, 1975).
Ho, M. W. & O'Brien, J. S. Clin. chim. Acta. 30, 531–534 (1970).
Lowry, O. H., Rosenbrough, N. J., Farr, A. L. & Randall, R. J. J. biol. Chem. 193, 265–275 (1951).
Callahan, J. W., Pinsky, L. & Wolfe, L. S. Biochem. Med. 4, 294–316 (1970).
Dawes, C. J. in Biological Techniques in Electron Microscopy 17–148 (Barnes and Noble, New York, 1971).
Callahan, J. W. & Wolfe, L. S. Biochim. biophys. Acta 215, 527–532 (1970).
Tsay, G. C., Dawson, G. & Li, Y. T. Biochim. biophys. Acta 385, 305–311 (1975).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
REYNOLDS, G., BAKER, H. & REYNOLDS, R. Enzyme replacement using liposome carriers in feline GM1 gangliosidosis fibroblasts. Nature 275, 754–755 (1978). https://doi.org/10.1038/275754a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/275754a0
This article is cited by
-
Mutation of the GM2 activator protein in a feline model of GM2 gangliosidosis
Acta Neuropathologica (2005)
-
Inherited metabolic disease in laboratory animals: a review
Journal of Inherited Metabolic Disease (1980)
-
Biochemistry and Genetics of gangliosidoses
Human Genetics (1979)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
