EC Number   |
Application |
Reference |
|---|
   3.10.1.1 | diagnostics |
a fluorimetric SGSH activity assay is commonly used to examine cells of mucopolysaccharidosis type IIIA patients for N-sulfoglucosamine sulfohydrolase activity, modification of the method for brain homogenates and definition of the parameters for assay linearity, overview |
734695 |
| 3.10.1.1 | drug development |
the enzyme is a target for the development of structure-based drug design for the devastating neurodegenerative disorder mucopolysaccharidosis type IIIA or Sanfilippo A syndrome |
733005 |
| 3.10.1.1 | medicine |
administration of recombinant human heparan-N-sulfatase via intrathecal drug delivery device appears generally safe and well tolerated in patients with mucopolysaccharidosis IIIA. Treatment results in consistent declines in heparan sulfate in cerebrospinal fluid, suggesting in vivo activity in the relevant anatomical compartment |
757672 |
| 3.10.1.1 | medicine |
enzyme-replacement or gene-replacement therapy |
288766, 288768 |
| 3.10.1.1 | medicine |
enzyme-replacement therapy from birth delays the development of behavior and learning problems in mucopolysaccharidosis type IIIA mice. Recombinant human sulfamidase administered to mucopolysaccharidosis type IIIA mice |
670475 |
| 3.10.1.1 | medicine |
intracerebral injection of recombinant human sulfamidase delays neuropathology in murine MPS-IIIA. Treatment reduces vacuolation and gliosis and delays the onset of ubiquitin-positive neurodegenerative changes in widespread areas of mucopolysaccharidosis type IIA brain, assessed at 24 weeks of age |
670278 |
| 3.10.1.1 | medicine |
intrathecal administration of recombinant human heparan-N-sulfatase reduces heparan sulfate and glycosaminoglycan levels in treated patients |
757675 |
| 3.10.1.1 | medicine |
mucopolysaccharidosis type IIIA (MPS IIIA, Sanfilippo A) is a neurodegenerative lysosomal storage disorder caused by the deficiency of sulphamidase enzyme (SGSH) leading to accumulation of heparan sulfate. Primary stored heparan sulfate and other glycosaminoglycans possibly accumulated through a secondary storage in brain, liver, kidney and lung of MPS IIIA mouse model is quantitatively and structurally characterized. The analysis is also performed in MPS IIIA mice upon the intravenous treatment with an engineered human sulphamidase (chimeric hSGSH) capable to increase its secretion from the liver and to cross the bloodbrain barrier. MPS IIIA animals show a huge accumulation of heparan sulfate, from about 15 up to about 24times higher than wild type and also of hyaluronic acid (from 2.5 up to about 5.0times more) and chondroitin sulfate/dermatan sulfate (from about 2 up to about 5times more) in all studied organs. A significant increase in the overall heparan sulfate charge density is observed and in particular of 2-O-sulfation in MPS IIIA mice organs. 8 months after a systemic treatment with an engineered SGSH, the enzyme is highly efficient in the reduction of all accumulated glycosaminoglycans in liver, brain and lung up to values of wild type mice. Even if reduced, glycosaminoglycans levels still remain significantly elevated in kidney. The data obtained by analysis of glycosaminoglycans in the different organs of affected and treated animals with chimeric human sulphamidase enzyme may have implications for the evaluation of an effective therapeutic option of MPS IIIA and for the reduction of related neuropathology |
757569 |
| 3.10.1.1 | medicine |
mucopolysaccharidosis type IIIA is caused by a deficiency in sulphamidase |
699132 |
| 3.10.1.1 | medicine |
recombinant murine sulfamidase is able to correct the storage phenotype of mucopolysaccharidosis type IIIA fibroblasts after endocytosis via the mannose-6-phosphate receptor |
670279 |
