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N-acetylglucosaminidase, alpha

alpha-N-acetylglucosaminidase, NAGLU
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: HAD, ACID, AGE, CAN, V1a
Papers on alpha-N-acetylglucosaminidase
Mucopolysaccharidosis IIIB confers enhanced neonatal intracranial transduction by AAV8 but not 5, 9 or rh10.
Heldermon et al., Gainesville, United States. In Gene Ther, Jan 2016
UNASSIGNED: Sanfilippo syndrome type B (MPS IIIB) is a lysosomal storage disease resulting from deficiency of N-acetyl-glucosaminidase (NAGLU) activity.
A GLP-compliant toxicology and biodistribution study: systemic delivery of a rAAV9 vector for the treatment of mucopolysaccharidosis IIIB.
Fu et al., Columbus, United States. In Hum Gene Ther Clin Dev, Jan 2016
UNASSIGNED: No treatment is currently available for mucopolysaccharidosis (MPS) IIIB, a neuropathic lysosomal storage disease due to defect in α-N-acetylglucosaminidase (NAGLU).
A GLP-Compliant Toxicology and Biodistribution Study: Systemic Delivery of an rAAV9 Vector for the Treatment of Mucopolysaccharidosis IIIB.
Fu et al., Columbus, United States. In Hum Gene Ther Clin Dev, Dec 2015
No treatment is currently available for mucopolysaccharidosis (MPS) IIIB, a neuropathic lysosomal storage disease due to defect in α-N-acetylglucosaminidase (NAGLU).
Sanfilippo syndrome: Overall review.
Couce et al., Barakaldo, Spain. In Pediatr Int, Jun 2015
Enzyme activity of the different enzymes in blood serum, leukocytes or fibroblasts, and mutational analysis for SGSH, NAGLU, HGSNAT or GNS genes are required to confirm diagnosis and differentiate four subtypes of MPS III.
Adult-onset painful axonal polyneuropathy caused by a dominant NAGLU mutation.
Brais et al., Montréal, Canada. In Brain, Jun 2015
Segregation analysis in all 45 recruited individuals has shown that only the p.Ile403Thr variant in the α-N-acetyl-glucosaminidase (NAGLU) gene segregates with the disease.
Biochemical, histological and functional correction of mucopolysaccharidosis type IIIB by intra-cerebrospinal fluid gene therapy.
Bosch et al., Paris, France. In Hum Mol Genet, May 2015
To overcome these limitations, we delivered AAV9 vectors encoding for α-N-acetylglucosaminidase (NAGLU) to the Cerebrospinal Fluid (CSF) of MPSIIIB mice with the disease already detectable at biochemical, histological and functional level.
Electrophysiological and Histological Characterization of Rod-Cone Retinal Degeneration and Microglia Activation in a Mouse Model of Mucopolysaccharidosis Type IIIB.
Wu et al., Houston, United States. In Sci Rep, 2014
Here we sought to study the underlying retinal functional and morphological changes associated with MPS IIIB disease progression using the established model of MPS IIIB, the B6.129S6-Naglu(tm1Efn)/J mouse line.
The Murine Model of Mucopolysaccharidosis IIIB Develops Cardiopathies over Time Leading to Heart Failure.
Pavone et al., Napoli, Italy. In Plos One, 2014
Mucopolysaccharidosis (MPS) IIIB is a lysosomal disease due to the deficiency of the enzyme α-N-acetylglucosaminidase (NAGLU) required for heparan sulfate (HS) degradation.
Delivery of an enzyme-IGFII fusion protein to the mouse brain is therapeutic for mucopolysaccharidosis type IIIB.
Neufeld et al., Los Angeles, United States. In Proc Natl Acad Sci U S A, 2014
The cause is mutation in the gene encoding α-N-acetylglucosaminidase (NAGLU), deficiency of NAGLU, and accumulation of heparan sulfate.
Mucopolysaccharidosis III (Sanfilippo Syndrome)- disease presentation and experimental therapies.
Heldermon et al., In Pediatr Endocrinol Rev, 2014
Sanfilippo Syndrome or Mucopolysaccharidosis Ill (MPS Ill) is a group of lysosomal storage diseases resulting from a deficiency of one of four lysosomal enzymes: Type A - heparan N-sulfatase (SGSH), Type B - a-N-acetylglucosaminidase (NAGLU), Type C - acetyl CoA a-glucosaminide acetyltransferase (HGSNAT) and Type D - N-acetylglucosamine-6-sulfatase (GNS).
"Genotype-first" approaches on a curious case of idiopathic progressive cognitive decline.
Wang et al., Guangzhou, China. In Bmc Med Genomics, 2013
Biochemical tests confirmed the complete loss of activity of alpha-N-acetylglucosaminidase (encoded by NAGLU) in blood, as well as significantly elevated dermatan sulfate and heparan sulfate in urine.
Repeated administrations of human umbilical cord blood cells improve disease outcomes in a mouse model of Sanfilippo syndrome type III B.
Sanberg et al., Tampa, United States. In Cell Transplant, 2013
Sanfilippo syndrome type III B (MPS III B) is an inherited disorder characterized by a deficiency of α-N-acetylglucosaminidase (Naglu) enzyme leading to accumulation of heparan sulfate in lysosomes and severe neurological deficits.
Genetic and pathological links between Parkinson's disease and the lysosomal disorder Sanfilippo syndrome.
Spillantini et al., Cambridge, United Kingdom. In Mov Disord, 2012
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.
Neuroblastoma amplified sequence gene is associated with a novel short stature syndrome characterised by optic nerve atrophy and Pelger-Huët anomaly.
Onodera et al., Yakutsk, Russia. In J Med Genet, 2010
These findings suggest that function of NBAS may associate with the pathogenesis of short stature syndrome as well as optic atrophy and Pelger-Huet anomaly.
Identification and characterization of a novel homozygous deletion in the alpha-N-acetylglucosaminidase gene in a patient with Sanfilippo type B syndrome (mucopolysaccharidosis IIIB).
Maystadt et al., Greenwood, United States. In Mol Genet Metab, 2010
We have identified an 1146 bp intragenic deletion of the NAGLU gene within consanguineous parents having two children affected with Sanfilippo syndrome type B.
Voltage-gated sodium channel expression in rat spiral ganglion neurons.
Grubb et al., Leicester, United Kingdom. In Mol Cell Neurosci, 2009
Data demonstrate predominant localisation of Na(V)1.6 and Na(V)1.7 on SGN cell bodies and Na(V)1.1 on axonal processes in rat brain.
Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases.
Braulke et al., Hamburg, Germany. In Biol Chem, 2009
The phosphorylation of man- nose residues on high mannose-type oligosaccharides of newly synthesized lysosomal enzymes is catalyzed by two multimeric enzymes, GlcNAc-1-phosphotransferase and GlcNAc-1-phosphodiester-alpha-N-acetylglucosaminidase, allowing the binding to two distinct Man6P receptors in the Golgi apparatus.
Molecular cloning of t(2;7)(p24.3;p14.2), a novel chromosomal translocation in myelodysplastic syndrome-derived acute myeloid leukemia.
Imoto et al., Yokohama, Japan. In J Hum Genet, 2009
Defects in NAG-ELMO1 is associated with leukemic progression.
Sanfilippo syndrome type C: mutation spectrum in the heparan sulfate acetyl-CoA: alpha-glucosaminide N-acetyltransferase (HGSNAT) gene.
Pshezhetsky et al., Montréal, Canada. In Hum Mutat, 2009
which catalyzes transmembrane acetylation of the terminal glucosamine residues of heparan sulfate prior to their hydrolysis by alpha-N-acetylglucosaminidase.
Molecular genetics of mucopolysaccharidosis type IIIA and IIIB: Diagnostic, clinical, and biological implications.
Hopwood et al., Adelaide, Australia. In Hum Mutat, 2001
Molecular genetics of mucopolysaccharidosis type IIIA and IIIB: Diagnostic, clinical, and biological implications
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