Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/7443
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dc.contributor.authorPerkins, K.en
dc.contributor.authorByers, S.en
dc.contributor.authorYogalingam, G.en
dc.contributor.authorWeber, B.en
dc.contributor.authorHopwood, J.en
dc.date.issued1999en
dc.identifier.citationJournal of Biological Chemistry, 1999; 274(52):37193-37199en
dc.identifier.issn0021-9258en
dc.identifier.issn1083-351Xen
dc.identifier.urihttp://hdl.handle.net/2440/7443-
dc.description.abstractMucopolysaccharidosis IIIA (MPS-IIIA) is an autosomal recessive lysosomal storage disorder caused by the deficiency of sulfamidase (NS; EC 3.10.1.1), resulting in defective degradation and storage of heparan sulfate. This paper reports the production and characterization of monoclonal and polyclonal antibodies against recombinant human sulfamidase (rhNS) to quantitate and characterize normal and mutant sulfamidase produced from the wild type NS expression vector. Glycosylation and phosphorylation studies of immunoprecipitated rhNS show that all five potential glycosylation sites are utilized, with three high mannose/hybrid oligosaccharides and two simpler chains, with at least one functional mannose 6-phosphate group. An NS quantification system was developed to determine the effect of the three most common and severe patient mutations: S66W (Italy), R74C (Poland), and R245H (The Netherlands). The quantity and specific activity of expressed mutant rhNS was significantly lower than expressed normal rhNS, with 0.3, 0.2, and 0.05% of normal rhNS produced and 15, 17, and 83% of normal specific activity for S66W, R74C, and R245H observed, respectively. The recent structural elucidation of N-acetylgalactosamine-4-sulfatase was utilized to postulate the effect on the structure-function relationship of NS. The characterization of normal and mutated rhNS has relevance for efficient diagnosis and therapeutic developments for MPS-IIIA patients.en
dc.language.isoenen
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INCen
dc.subjectCHO Cells; Animals; Humans; Mucopolysaccharidosis III; Hydrolases; Recombinant Proteins; Glycosylation; Phosphorylation; Phenotype; Mutation; Cricetinaeen
dc.titleExpression and characterization of wild type and mutant recombinant human sulfamidase - Implications for Sanfilippo (mucopolysaccharidosis IIIA) syndromeen
dc.typeJournal articleen
dc.identifier.rmid0030005560en
dc.identifier.doi10.1074/jbc.274.52.37193en
dc.identifier.pubid69566-
pubs.library.collectionPaediatrics publicationsen
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
dc.identifier.orcidByers, S. [0000-0001-5576-3636]en
Appears in Collections:Paediatrics publications

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