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Literature summary for 3.1.6.13 extracted from

  • Muenzer, J.; Beck, M.; Eng, C.M.; Escolar, M.L.; Giugliani, R.; Guffon, N.H.; Harmatz, P.; Kamin, W.; Kampmann, C.; Koseoglu, S.T.; Link, B.; Martin, R.A.; Molter, D.W.; Munoz Rojas, M.V.; Ogilvie, J.W.; Parini, R.; Ramaswami, U.; Scarpa, M.; Schwartz, I.V.; Wood, R.E.; Wraith, E.
    Multidisciplinary management of Hunter syndrome (2009), Pediatrics, 124, e1228-e1239.
    View publication on PubMed
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Application

Application Comment Organism
medicine use of enzyme-replacement therapy with recombinant human iduronate-2-sulfatase as a specific treatment for Hunter syndrome. Reductions in liver and spleen volume and in urinary glycoaminoglycan excretion in patients treated with idursulfase. In clinical trials, idursulfase is well tolerated, but in in some patients life-threatening anaphylactic reactions during infusion of idursulfase Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome
-
 Homo sapiens 5764
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Synonyms

Synonyms Comment Organism
I2S
-
 Homo sapiens
iduronate-2-sulfatase
-
 Homo sapiens
idursulfase
-
 Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens