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Data demonstrate that iduronate sulfatase plays a critical role during early vertebrate development and its downregulation may be responsible for severe developmental defects, including a misshapen trunk and abnormal craniofacial cartilages.
Study analyzed the genotype-phenotype relationship for 17 patients with mucopolysaccharidosis II and performed expression studies for 12 variants, nine of which have not been reported previously; speculated that very low or cell-type-specific IDS residual activity is sufficient to prevent the neuronal phenotype.
Study identified 16 novel mutations in the IDS gene and revealed that the severe type of mucopolysaccharidosis type II is strongly associated with large structural alteration of the gene.
Functional characterization of all the novel sequence variants identified in the study would be helpful to confirm the clinical significance and to determine the effect of these variations on the function of respective proteins (IDUA (show IDUA Proteins) and IDS)
Extensive iduronate 2-sulfatase (Hunter syndrome) (IDS) gene deletions were identified in four mucopolysaccharidosis type II (MPSII) patients.
This study evaluated a novel mutation in the IDS gene among 8 male Hunter syndrome patients; there was a quantitative deficiency of NK and B cell with normal responses in other immune parameters.
30 novel iduronate sulfatase mutations have been identified in mucopolysaccharidosis type II Latin American patients.
Identification of a splice site mutation in the IDS gene associated with mucopolysaccharidosis type II.
a novel (p.R468P) and five known (p.R88C, p.D148V, p.G224A, p.Y348X, and p.R468Q) IDS mutations were shown to result in proteins with little or no IDS activity and altered protein processing, when expressed in COS7 cells
A report of a novel IDS nonsense mutation resulting in mucopolysaccharidosis type II in several patients from a Chinese family.
genetically analyze patients with severe Hunter syndrome that showed a total deletion of the iduronate-2-sulphatase (IDS) gene
While the iduronate 2-sulfatase sp replacement results in increased enzyme secretion, the addition of the ApoB (show APOB Proteins)-BD allows efficient BBB transcytosis and restoration of sulphamidase (show SGSH Proteins) activity in the brain of treated mice.
Iduronate-2-sulfatase (IDS) is localized in lysosomes in pancreatic islet cells and expression is regulated by glucose. IDS has a potential role in the normal pathway of lysosomal degradation of secretory peptides.
Ids crossing the blood-brain barrier corrects CNS defects in MPSII mice.
Iduronate-2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in this X-chromosome gene that result in enzymatic deficiency lead to the sex-linked Mucopolysaccharidosis Type II, also known as Hunter Syndrome. Iduronate-2-sulfatase has a strong sequence similarity with human arylsulfatases A, B, and C, and human glucosamine-6-sulfatase. Multiple alternatively spliced transcript variants that encode different protein isoforms have been described.
iduronate 2-sulfatase (Hunter syndrome)
, iduronate 2-sulfatase
, iduronate 2-sulfatase-like
, alpha-L-iduronate sulfate sulfatase
, iduronate 2-sulfatase 14 kDa chain
, iduronate 2-sulfatase 42 kDa chain
, iduronate sulfatase