The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
N-butyldeoxynojirimycin is a novel inhibitor of glycolipid biosynthesis.
Open accessAbstract
The imino sugar deoxynojirimycin and its alkylated derivatives are inhibitors of the N-linked oligosaccharide processing enzymes alpha-glucosidase I and II. These compounds are glucose analogues and have the potential to inhibit both glucosidases and glucosyltransferases. However, to date there has been no report of deoxynojirimycin or similar analogues inhibiting a mammalian glucosyltransferase. We have investigated the effects of deoxynojirimycin and its alkylated derivatives on the biosynthesis of glycolipids in HL-60 cells. We have found that the N-butyl and N-hexyl derivatives of deoxynojirimycin, but not deoxynojirimycin itself, are novel inhibitors of the glucosyltransferase-catalyzed biosynthesis of glucosylceramide. This results in the inhibition of biosynthesis of all glucosylceramide-based glycosphingolipids. We have investigated the ability of one of these compounds, N-butyldeoxynojirimycin, to offset glucosylceramide accumulation in an in vitro Gaucher's disease model. This compound prevents lysosomal glycolipid storage and offers a novel therapeutic approach for the management of this and other glycolipid storage disorders.
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Saunier, B., Kilker, R. D., Tkacz, J. S., Quaroni, A., & Herscovics, A. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45358-1 · Cited by 283
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Metadata
- Authors
- Platt, F. M., Neises, G. R., Dwek, R. A., & Butters, T. D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1994-03
- Volume
- 269
- Issue
- 11
- Pages
- 8362-8365
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1485152739
- Cited by
- 455
- References
- 1
- FWCI
- 4.48
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Platt, F. M., Neises, G. R., Dwek, R. A., & Butters, T. D. (1994). N-butyldeoxynojirimycin is a novel inhibitor of glycolipid biosynthesis. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)37202-2
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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