EC Number   |
General Information |
Reference |
|---|
   3.1.6.13 | malfunction |
downregulation of IDS may be responsible for severe early developmental defects, including a misshapen trunk and abnormal craniofacial cartilages, which is mediated by depauperation of sox10-expressing neural crest cell precursors, which is reverted through the administration of the recombinant enzyme |
709793 |
| 3.1.6.13 | malfunction |
Hunter syndrome is caused by a deficiency of the lysosomal enzyme iduronate-2-sulfatase. In the absence of sufficient enzyme activity, glycosaminoglycans accumulate in the lysosomes. Complete deletions of the I2S gene (IDS) always result in a severe phenotype, as do complex rearrangements of IDS. Several missense mutations are associated with a severe phenotype (p.R468Q,89-94 p.R468W,95-99 and p.S333L96,100), although each one has in patients with an intermediate or attenuated phenotypes. The mutation c.1122C3T (which creates an alternate splice site with the loss of 20 amino acids) is primarily associated with the attenuated phenotype |
710212 |
| 3.1.6.13 | malfunction |
iduronate-2-sulfate sulfatase, IDS, deficiency causes the Hunter syndrome ormucopolysaccharidosis type II |
715792 |
| 3.1.6.13 | malfunction |
Italian Hunter syndrome patients show a lack of concordance between IDS genomic DNA and cDNA: presence of wild-type IDS sequence as well as the mutated sequence in cDNA from one or more tissues, but no wild-type IDS sequence is evident in the genomic DNAs derived from these patients, a correction mechanism such as RNA editing may potentially account for this. These Hunter syndrome patients are hemizygous respectively for a nonsense mutation (c.22C>T,p.R8X) and a frameshift micro-insertion (c.10insT,p.P4Sfs) in their genomic DNA. Since both p.R8X mutations are inherited from carrier mothers, somatic mosaicism can be excluded |
708665 |
| 3.1.6.13 | malfunction |
mucopolysaccharidosis, MPS, type II is caused by mutations in the lysosomal enzyme, iduronate-2-sulfatase. MPS-II affects the brain and enzyme replacement therapy is ineffective for the brain, because the enzyme does not cross the blood-brain barrier |
714554 |
| 3.1.6.13 | more |
development of an expression system for human recombinant IDS in Pichia pastoris and of a detection method for enzyme detection during production and purification processes, which can be used also to measure the enzyme in human fluids, immunoquantification assay using rabbit IgG and chicken IgY, overview |
715792 |
| 3.1.6.13 | physiological function |
a 6-year-old male suffering from a severe type of Hunter disease (deficiency of IDS) with cord blood stem cell transplantation died at 10 months post-therapy due to a laryngeal post-transplantation lymphoproliferative disorder |
709970 |
| 3.1.6.13 | physiological function |
a deficiency of iduronate-2-sulfatase causes mucopolysaccharidosis type II (Hunter syndrome), which is a progressive, multisystemic disease: patients with the severe form of the disease have cognitive impairment and typically die in the second decade of life, whereas patients with the less severe form do not experience significant cognitive involvement and may survive until the fifth or sixth decade of life |
709386 |
| 3.1.6.13 | physiological function |
HIRMAb-IDS fusion protein crosses the blood-brain barrier on the endogenous insulin receptor and acts as a molecular Trojan horse to ferry the IDS into brain. The fusion protein is taken up by Hunter fibroblasts, and the accumulation of glycosoaminoglycans in fibroblasts null for the sulfatase is decreased 84% by treatment with the fusion protein. The fusion protein heavy chain reacts with antibodies to both human IgG and human IDS. The fusion protein is a bifunctional molecule and binds both the HIR extracellular domain with comparable affinity to the chimeric HIRMAb and has high IDS enzyme activity |
707600 |
| 3.1.6.13 | physiological function |
iduronate sulfatase plays a critical role during early vertebrate developments |
709793 |
