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A biochemical and physicochemical comparison of two recombinant enzymes used for enzyme replacement therapies of hunter syndrome.

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dc.contributor.authorChung, YK-
dc.contributor.authorSohn, YB-
dc.contributor.authorSohn, JM-
dc.contributor.authorLee, J-
dc.contributor.authorChang, MS-
dc.contributor.authorKwun, Y-
dc.contributor.authorKim, CH-
dc.contributor.authorLee, JY-
dc.contributor.authorYook, YJ-
dc.contributor.authorKo, AR-
dc.contributor.authorJin, DK-
dc.date.accessioned2016-11-23T03:46:51Z-
dc.date.available2016-11-23T03:46:51Z-
dc.date.issued2014-
dc.identifier.issn0282-0080-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/12977-
dc.description.abstractMucopolysaccharidosis II (MPS II, Hunter syndrome; OMIM 309900) is an X-linked
lysosomal storage disease caused by a deficiency in the enzyme
iduronate-2-sulfatase (IDS), leading to accumulation of glycosaminoglycans
(GAGs). For enzyme replacement therapy (ERT) of Hunter syndrome, two recombinant
enzymes, idursulfase (Elaprase((R)), Shire Human Genetic Therapies, Lexington,
MA) and idursulfase beta (Hunterase((R)), Green Cross Corporation, Yongin,
Korea), are currently available in Korea. To compare the biochemical and
physicochemical differences between idursulfase and idursulfase beta, we examined
the formylglycine (FGly) content, specific enzyme activity, mannose-6-phosphate
(M6P) content, sialic acid content, and in vitro cell uptake activity of normal
human fibroblasts of these two enzymes.The FGly content, which determines the
enzyme activity, of idursulfase beta was significantly higher than that of
idursulfase (79.4 +/- 0.9 vs. 68.1 +/- 2.2 %, P < 0.001). In accordance with the
FGly content, the specific enzyme activity of idursulfase beta was significantly
higher than that of idursulfase (42.6 +/- 1.1 vs. 27.8 +/- 0.9 nmol/min/mug
protein, P < 0.001). The levels of M6P and sialic acid were not significantly
different (2.4 +/- 0.1 vs 2.4 +/- 0.3 mol/mol protein for M6P and 12.3 +/- 0.7
vs. 12.4 +/- 0.4 mol/mol protein for sialic acid). However, the cellular uptake
activity of the normal human fibroblasts in vitro showed a significant difference
(Kuptake, 5.09 +/- 0.96 vs. 6.50 +/- 1.28 nM protein, P = 0.017).In conclusion,
idursulfase beta exhibited significantly higher specific enzyme activity than
idursulfase, resulting from higher FGly content. These biochemical differences
may be partly attributed to clinical efficacy. However, long-term clinical
evaluations of Hunter syndrome patients treated with these two enzymes will be
needed to demonstrate the clinical implications of significant difference of the
enzyme activity and the FGly content.
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dc.formatapplication/pdf-
dc.language.isoen-
dc.subject.MESHAlanine-
dc.subject.MESHAnimals-
dc.subject.MESHCHO Cells-
dc.subject.MESHCricetinae-
dc.subject.MESHCricetulus-
dc.subject.MESHEnzyme Replacement Therapy-
dc.subject.MESHFibroblasts-
dc.subject.MESHGlycine-
dc.subject.MESHHumans-
dc.subject.MESHIduronate Sulfatase-
dc.subject.MESHMannosephosphates-
dc.subject.MESHMucopolysaccharidosis II-
dc.subject.MESHN-Acetylneuraminic Acid-
dc.subject.MESHRecombinant Fusion Proteins-
dc.titleA biochemical and physicochemical comparison of two recombinant enzymes used for enzyme replacement therapies of hunter syndrome.-
dc.typeArticle-
dc.identifier.pmid24781369-
dc.identifier.urlhttp://link.springer.com/article/10.1007%2Fs10719-014-9523-0-
dc.contributor.affiliatedAuthor손, 영배-
dc.type.localJournal Papers-
dc.identifier.doi10.1007/s10719-014-9523-0-
dc.citation.titleGlycoconjugate journal-
dc.citation.volume31-
dc.citation.number4-
dc.citation.date2014-
dc.citation.startPage309-
dc.citation.endPage315-
dc.identifier.bibliographicCitationGlycoconjugate journal, 31(4). : 309-315, 2014-
dc.identifier.eissn1573-4986-
dc.relation.journalidJ002820080-
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Journal Papers > School of Medicine / Graduate School of Medicine > Medical Genetics
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