3.1.6.12: N-acetylgalactosamine-4-sulfatase
This is an abbreviated version!
For detailed information about N-acetylgalactosamine-4-sulfatase, go to the full flat file.
Word Map on EC 3.1.6.12
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3.1.6.12
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mucopolysaccharidosis
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lysosomal
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maroteaux-lamy
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glycosaminoglycans
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arylsulfatase
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dermatan
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feline
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rhasb
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medicine
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galsulfase
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sulfatases
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stair
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enzyme-replacement
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mps-vi
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dysostosis
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diagnostics
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nutrition
- 3.1.6.12
- mucopolysaccharidosis
- lysosomal
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maroteaux-lamy
- glycosaminoglycans
- arylsulfatase
- dermatan
- feline
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rhasb
- medicine
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galsulfase
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sulfatases
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stair
-
enzyme-replacement
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mps-vi
- dysostosis
- diagnostics
- nutrition
Reaction
Synonyms
4-sulfatase, 4-sulphatase, acetylgalactosamine 4-sulfatase, ARSB, arylsulfatase B, ASB, chondroitinase, chondroitinsulfatase, chondrosulfatase, G4S, gastric chondrosulfohydrolase, N-acetylgalactosamine 4-sulfatase, N-acetylgalactosamine 4-sulfate sulfohydrolase, N-acetylgalactosamine-4-sulfatase, N-acetylgalactosamine-4-sulphatase, sulfatase, acetylgalactosamine 4-
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General Information on EC 3.1.6.12 - N-acetylgalactosamine-4-sulfatase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
metabolism
modification of expression of the enzyme regulates the content of chondroitin sulfate
physiological function
additional information
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a relatively high rate of immunotolerance towards recombinant human N-acetylgalactosamine-4-sulfatase can be achieved in MPS-VI cats with a shortcourse tolerisation regimen ultimately permitting removal of lysosomal storage within the dura mater with the use of intrathecal therapy
malfunction
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ARSB mutations are involved in mucopolysaccharidosis type VI, i.e. MPS VI, Maroteaux-Lamy syndrome
malfunction
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arylsulfatase B is associated with the lysosomal storage disease mucopolysaccharidosis VI
malfunction
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ASB-deficient cells accumulate dermatan sulfate and chondroitin sulfate, which may be partially hydrolyzed by other lysosomal hydrolases
malfunction
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mucopolysaccharidosis type VI, i.e. MPS VI or Maroteaux-Lamy syndrome, is a lysosomal storage disease in which deficient activity of the enzyme N-acetylgalactosamine 4-sulfatase impairs the stepwise degradation of the glycosaminoglycan dermatan sulfate
malfunction
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mucopolysaccharidosis VI, MPS VI or Maroteaux-Lamy syndrome, is an inherited metabolic disease caused by the deficiency of N-acetylgalactosamine 4-sulfatase. In the absence of this enzyme, the stepwise degradation of the glycosaminoglycan dermatan sulfate is blocked, resulting in intracellular accumulation of the substrate into the lysosomes, leading to a progressive disorder with multiple organ and tissue involvement
malfunction
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ARSB enzymatic activity is significantly greater in normal than in malignant tissue
malfunction
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inborn deficiency of ARSB leads to the lysosomal storage disease mucopolysaccharidosis VI, characterized by accumulation of sulfated glycosaminoglycans in vital organs, disruption of normal physiological processes, severe morbidity, and premature death
malfunction
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silencing or overexpression of ASB in normal rat kidney epithelial cells in tissue culture modifies the content of total sulfated glycosaminoglycans, C4S, kininogen, and bradykinin in spent media and cell lysates. Treatment of the cultured cells with chondroitinase ABC also increases the secretion of bradykinin into the spent media and reduces the C4S-associated kininogen. When ASB is overexpressed, the cellular kininogen that associates with C4S declines, suggesting a vital role for chondroitin-4-sulfation in regulating the kininogen-C4S interaction
malfunction
deficiencies of N-acetylgalactosamine-4-sulfatase is associated with the mucopolysaccharidoses
physiological function
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arylsulfatase B regulates interaction of chondroitin-4-sulfate and kininogen in renal epithelial cells. ASB activity may provide a link between salt responsiveness and the bradykinin-associated mechanism of blood pressure regulation
physiological function
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arylsulfatase B regulates interaction of chondroitin-4-sulfate and kininogen in renal epithelial cells. ASB activity may provide a link between salt responsiveness and the bradykinin-associated mechanism of blood pressure regulation
physiological function
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ASB and chondroitin 4-sulafte are involved in regulation of interleukin-8 secretion
physiological function
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arylsulfatase B removes 4-sulfate groups from the sulfated glycosaminoglycans chondroitin-4-sulfate and dermatan sulfate
physiological function
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ASB, owing to its effect on chondroitin-4-sulfation, impacts on the kininogen-bradykinin axis and, thereby, may influence blood pressure
physiological function
astrocyte treatment with ethanol inhibits the activity of arylsulfatase B, and triggers the degradation of chondroitin-4-sulfate, increases total sulfated glycosaminoglycans, chondroitin-4-sulfate and neurocan core-protein content and inhibits neurite outgrowth in neurons cocultured with ethanol-treated astrocytes in vitro. Ethanol also inhibits arylsulfatase B activity and increases sulfated glycosaminoglycans and neurocan levels in the developing hippocampus after in vivo ethanol exposure. Arylsulfatase B silencing increases the levels of sulfated glycosaminoglycans, chondroitin-4-sulfate, and neurocan in astrocytes and inhibits neurite outgrowth in cocultured neurons
physiological function
in human prostate stromal and epithelial cells, when arylsulfatase B is silenced, chondroitin-4-sulfate, versican and versican promoter activity increase, and the galectin-3 that co-immunoprecipitates with chondroitin-4-sulfate declines. Galectin-3 silencing inhibits the arylsulfatase B-silencing-induced increases in versican and versican promoter due to effects on the AP-1-binding site in the versican promoter
physiological function
in post-natal ventral rat prostate, a distinct and reciprocal localization of arylsulfatase B and N-acetylgalactosamine-6-sulfatase is seen, with arylsulfatase B predominant in the stroma and N-acetylgalactosamine-6-sulfatase predominant in the epithelium. Control arylsulfatase B activity increases significantly between days 5 and 30, but following estrogen exposure, activity is reduced and the observed increase on day 30 is inhibited
physiological function
a decline in ARSB activity increases transmembrane glycoprotein NMB expression. Protein tyrosine phosphatase SHP2 activity declines due to increased binding with chondroitin 4-sulfate when ARSB is reduced. When SHP2 activity is inhibited, phosphorylations of p38 mitogen-associated phosphokinase and of microphthalmia-associated transcription factor increase, leading to transmembrane glycoprotein NMB promoter activation. In contrast, constitutively active SHP2 and overexpression of ARSB inhibit NMB expression
physiological function
a decline in ARSB activity increases transmembrane glycoprotein NMB expression. Protein tyrosine phosphatase SHP2 activity declines due to increased binding with chondroitin 4-sulfate when ARSB is reduced. When SHP2 activity is inhibited, phosphorylations of p38 mitogen-associated phosphokinase and of microphthalmia-associated transcription factor increase, leading to transmembrane glycoprotein NMB promoter activation. In contrast, constitutively active SHP2 and overexpression of ARSB inhibit NMB expression
physiological function
abnormal expression and distribution of ARSB are closely associated with the neuron death in the superoxide dismutase mutant G93A transgenic mice. ARSB participates in the pathogenesis of amyotrophic lateral sclerosis (ALS), the relative deficiency of ARSB expression and redistribution in the anterior horn of gray matter and the posterior horn of gray matter of spinal cord in ALS-like superoxide dismutase G93A transgenic mice is closely associated with the neuron death
physiological function
in prostate stem cells, when N-acetylgalactosamine-4-sulfatase ARSB is reduced by silencing or galactosamine-N-acetyl-6-sulfatase GALNS is increased by overexpression, activity of non-receptor tyrosine phosphatase SHP2 declines, attributable to increased binding of SHP2 with C4S. This leads to increases in phospho-ERK1/2, Myc/Max nuclear DNA binding, DNA methyltransferase (DNMT) activity and expression, and methylation of the Dickkopf Wnt signaling pathway inhibitor (DKK)3 promoter and to reduced DKK3 expression. Since DKK3 negatively regulates Wnt/beta-catenin signaling, silencing of ARSB or overexpression of GALNS increases Wnt/beta-catenin signaling
