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In the 1-h test, MPS IIIB mice were hyperactive, with increased rapid exploratory behaviour and reduced immobility time.
Disruption of the Naglu gene responsible for heparan sulfate degradation results in substantial changes in expression of genes related to neural cell growth and function.
Our results demonstrate the advantages of intravenously administering hUCB cells into a mouse model of Sanfilippo Syndrome type B, the advantages probably a result of Naglu delivery to enzyme-deficient organs.
CSF (zeige CSF2 Antikörper) enzyme activity levels for either SGSH (zeige SGSH Antikörper) (in MPS IIIA subjects) or NAGLU (in MPS IIIB) significantly differed from normal controls. Several other behavioral or functional measures were found to be uninformative in this population, including timed functional motor tests.
Mutation in NAGLU gene is associated with atypical mucopolysaccharidosis IIIB.
in the current meta-analysis, based on ten prospective studies involving 29366 participants, we evaluated the role of urinary tubular injury markers (NGAL (zeige LCN2 Antikörper), KIM-1 (zeige HAVCR1 Antikörper) and NAG) in predicting clinical outcomes including CKD stage 3, end stage renal disease and mortality.
Mutations in NAGLU gene is associated with idiopathic progressive cognitive decline.
Plasma NAG correlates with gastrointestinal cancer outcomes.
study reports that carriers from two families of a severe pathogenic mutation in NAGLU develop a late dominant painful axonal sensory neuropathy.
A modified recombinant NAGLU fused to the receptor-binding motif of insulin-like growth factor (IGF)-II enhances its ability to enter cells using the mannose 6-phosphate receptor, which is the receptor for IGF-II at a different binding site.
The research may enrich the mutation spectrum of the NAGLU gene in the Chinese population and help us further in understanding the pathogenesis of MPS IIIB.
Urinary NAG/Cr may be a useful surrogate marker for renal function in ADPKD patients.
This study suggests a possible role of NAGLU in susceptibility to PD while extending evidence for alpha-synuclein aggregation in the brain in lysosomal storage disorders.
This gene encodes an enzyme that degrades heparan sulfate by hydrolysis of terminal N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides. Defects in this gene are the cause of mucopolysaccharidosis type IIIB (MPS-IIIB), also known as Sanfilippo syndrome B. This disease is characterized by the lysosomal accumulation and urinary excretion of heparan sulfate.
, N-acetylglucosaminidase, alpha-
, N-acetylglucosaminidase, alpha- (Sanfilippo disease IIIB)
, alpha-N-acetylglucosaminidase, lysosomal