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Enhanced sialylation and in vivo efficacy of recombinant human α-galactosidase through in vitro glycosylation

Title
Enhanced sialylation and in vivo efficacy of recombinant human α-galactosidase through in vitro glycosylation
Authors
Sohn Y.Lee J.M.Park H.-R.Jung S.-C.Park T.H.Oh D.-B.
Ewha Authors
정성철
SCOPUS Author ID
정성철scopus
Issue Date
2013
Journal Title
BMB Reports
ISSN
1976-6696JCR Link
Citation
vol. 46, no. 3, pp. 157 - 162
Indexed
SCIE; SCOPUS; KCI WOS scopus
Abstract
Human α-galactosidase A (GLA) has been used in enzyme replacement therapy for patients with Fabry disease. We expressed recombinant GLA from Chinese hamster ovary cells with very high productivity. When compared to an approved GLA (agalsidase beta), its size and charge were found to be smaller and more neutral. These differences resulted from the lack of terminal sialic acids playing essential roles in the serum half-life and proper tissue targeting. Because a simple sialylation reaction was not enough to increase the sialic acid content, a combined reaction using galactosyltransferase, sialyltransferase, and their sugar substrates at the same time was developed and optimized to reduce the incubation time. The product generated by this reaction had nearly the same size, isoelectric points, and sialic acid content as agalsidase beta. Furthermore, it had better in vivo efficacy to degrade the accumulated globotriaosylceramide in target organs of Fabry mice compared to an unmodified version. © 2013 by the The Korean Society for Biochemistry and Molecular Biology.
DOI
10.5483/BMBRep.2013.46.3.192
Appears in Collections:
의학전문대학원 > 의학과 > Journal papers
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