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(2-acetamido-2-deoxy-O-(beta-D-glucuronic acid)-4-O-sulpho-D-galactose)2 + H2O
(2-acetamido-2-deoxy-O-(beta-D-glucuronic acid)-D-galactose)2 + sulfate
-
exo-sulfatase, stepwise degradation of glycosaminoglycans
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
4-methylumbelliferyl sulfate + H2O
?
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
sulfate + 4-methylumbelliferone
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
-
-
-
-
?
carbobenzoxyglucosamine 4,6-disulfate + H2O
carbobenzoxyglucosamine 6-sulfate + sulfate
-
-
-
-
?
chondroitin 4-sulfate + H2O
chondroitin + sulfate
chondroitin 4-sulfate-heptasaccharide + H2O
chondroitin 4-sulfate-heptasaccharide + sulfate
chondroitin 4-sulfate-tetrasaccharide + H2O
chondroitin 4-sulfate-tetrasaccharide + sulfate
-
only the 4-sulfated endgroup is attacked by the enzyme, sulfate is released only in presence of beta-glucuronidase, acts as exosulphatase
-
-
?
chondroitin sulfate + H2O
?
chondroitin sulfate + H2O
chondroitin + sulfate
chondroitin-4-sulfate + H2O
chondroitin + sulfate
-
arylsulfatase B removes 4-sulfate groups from the sulfated glycosaminoglycans chondroitin-4-sulfate and dermatan sulfate
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
glucosamine 4,6-disulfate + H2O
glucosamine 6-sulfate + sulfate
-
-
-
-
?
N-acetygalactosamine 4-sulfate-(1-4)-beta-glucuronic acid-(1-3)-beta-N-acetylgalactosaminitol 4-sulfate + H2O
N-acetygalactosamine-(1-4)-beta glucuronic acid-(1-3)-beta N-acetylgalactosaminitol 4-sulfate + sulfate
N-acetyl-D-galactosamine 4-sulfate + H2O
N-acetyl-D-galactosamine + sulfate
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
N-acetylgalactosamine 4,6-bisulfate-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)3 + H2O
N-acetylgalactosamine 6-sulfate-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine)3 + sulfate
-
hydrolysis only at the nonreducing residues
-
-
?
N-acetylgalactosamine 4-sulfate + H2O
N-acetylgalactosamine + sulfate
-
-
-
-
?
N-acetylgalactosamine 4-sulfate-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)2 + H2O
N-acetylgalactosamine-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)2 + sulfate
-
only the 4-sulfated endgroup is attacked by the enzyme
-
-
?
N-acetylgalactosamine 4-sulfate-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)3 + H2O
N-acetylgalactosamine-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine)3 + sulfate
-
only the 4-sulfated endgroup is attacked by the enzyme
-
-
?
N-acetylgalactosamine 4-sulfate-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)4 + H2O
N-acetylgalactosamine-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)4 + sulfate
-
only the 4-sulfated endgroup is attacked by the enzyme
-
-
?
N-acetylgalactosamine 4-sulfate-beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate + H2O
N-acetylgalactosamine-beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate + sulfate
-
-
-
-
?
N-acetylglucosamine 4-sulfate + H2O
N-acetylglucosamine + sulfate
-
-
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
sulfated glycosaminoglycan + H2O
glycosaminoglycan + sulfate
-
-
-
?
UDP-N-acetylgalactosamine 4,6-bisulfate + H2O
UDP-N-acetylgalactosamine 6-sulfate + sulfate
-
-
-
-
?
UDP-N-acetylgalactosamine-4-sulfate + H2O
UDP-N-acetylgalactosamine + sulfate
additional information
?
-
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
-
-
-
-
?
chondroitin 4-sulfate + H2O
chondroitin + sulfate
-
-
-
-
?
chondroitin 4-sulfate + H2O
chondroitin + sulfate
-
-
-
-
?
chondroitin 4-sulfate + H2O
chondroitin + sulfate
-
-
-
?
chondroitin 4-sulfate + H2O
chondroitin + sulfate
-
-
-
-
?
chondroitin 4-sulfate + H2O
chondroitin + sulfate
-
-
-
-
?
chondroitin 4-sulfate + H2O
chondroitin + sulfate
-
-
-
-
?
chondroitin 4-sulfate + H2O
chondroitin + sulfate
-
-
-
-
?
chondroitin 4-sulfate-heptasaccharide + H2O
chondroitin 4-sulfate-heptasaccharide + sulfate
-
reduced activity in patients with Maroteaux-Lamy Syndrome
-
-
?
chondroitin 4-sulfate-heptasaccharide + H2O
chondroitin 4-sulfate-heptasaccharide + sulfate
-
-
-
-
?
chondroitin 4-sulfate-heptasaccharide + H2O
chondroitin 4-sulfate-heptasaccharide + sulfate
-
-
-
-
?
chondroitin sulfate + H2O
?
-
-
-
-
?
chondroitin sulfate + H2O
?
-
-
-
-
?
chondroitin sulfate + H2O
chondroitin + sulfate
-
-
-
-
?
chondroitin sulfate + H2O
chondroitin + sulfate
-
-
-
?
dermatan sulfate + H2O
?
-
-
-
-
?
dermatan sulfate + H2O
?
-
-
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
-
-
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
-
-
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
-
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
-
reduced activity in patients with Maroteaux-Lamy Syndrome
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
-
arylsulfatase B removes 4-sulfate groups from the sulfated glycosaminoglycans chondroitin-4-sulfate and dermatan sulfate
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
-
-
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
-
-
-
-
?
N-acetygalactosamine 4-sulfate-(1-4)-beta-glucuronic acid-(1-3)-beta-N-acetylgalactosaminitol 4-sulfate + H2O
N-acetygalactosamine-(1-4)-beta glucuronic acid-(1-3)-beta N-acetylgalactosaminitol 4-sulfate + sulfate
-
-
-
-
?
N-acetygalactosamine 4-sulfate-(1-4)-beta-glucuronic acid-(1-3)-beta-N-acetylgalactosaminitol 4-sulfate + H2O
N-acetygalactosamine-(1-4)-beta glucuronic acid-(1-3)-beta N-acetylgalactosaminitol 4-sulfate + sulfate
-
oligosaccharides
-
-
?
N-acetyl-D-galactosamine 4-sulfate + H2O
N-acetyl-D-galactosamine + sulfate
-
-
-
-
?
N-acetyl-D-galactosamine 4-sulfate + H2O
N-acetyl-D-galactosamine + sulfate
-
-
-
-
?
N-acetyl-D-galactosamine 4-sulfate + H2O
N-acetyl-D-galactosamine + sulfate
-
-
-
-
?
N-acetyl-D-galactosamine 4-sulfate + H2O
N-acetyl-D-galactosamine + sulfate
-
-
-
-
?
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
acts also on N-acetylglucosamine 4-sulfate
-
-
?
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
weak iduronate sulfatase activity
-
-
?
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
no activity on galactosamine 6-sulfate
-
-
?
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
acts also on N-acetylglucosamine 4-sulfate
-
-
?
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
acts also on N-acetylglucosamine 4-sulfate
-
-
?
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
acts also on N-acetylglucosamine 4-sulfate
135542, 135544, 135545, 135548, 135551, 135554, 135557, 135560, 135562, 135563, 135564 -
-
?
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
acts also on N-acetylglucosamine 4-sulfate
-
-
?
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
acts also on N-acetylglucosamine 4-sulfate
-
-
?
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
acts also on N-acetylglucosamine 4-sulfate
-
-
?
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
acts also on N-acetylglucosamine 4-sulfate
-
-
?
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
acts also on N-acetylglucosamine 4-sulfate
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
-
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
enzymes catalyze in addition to reaction of EC 3.1.6.12 also arylsulfatase reaction , see also EC 3.1.6.1
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
enzymes catalyze in addition to reaction of EC 3.1.6.12 also arylsulfatase reaction , see also EC 3.1.6.1
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
enzymes catalyze in addition to reaction of EC 3.1.6.12 also arylsulfatase reaction , see also EC 3.1.6.1
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
-
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
enzymes catalyze in addition to reaction of EC 3.1.6.12 also arylsulfatase reaction , see also EC 3.1.6.1
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
-
-
-
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
-
-
-
-
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
-
-
-
-
?
UDP-N-acetylgalactosamine-4-sulfate + H2O
UDP-N-acetylgalactosamine + sulfate
-
-
-
-
?
UDP-N-acetylgalactosamine-4-sulfate + H2O
UDP-N-acetylgalactosamine + sulfate
-
-
-
-
?
UDP-N-acetylgalactosamine-4-sulfate + H2O
UDP-N-acetylgalactosamine + sulfate
-
-
-
-
?
UDP-N-acetylgalactosamine-4-sulfate + H2O
UDP-N-acetylgalactosamine + sulfate
-
-
-
-
?
additional information
?
-
mucopolysaccharidosis type VI is an autosomal recessive lysosomal storage disorder caused by the deficiency of N-acetylgalactosamine-4-sulfatase. Mutations in the N-acetylgalactosamine-4-sulfatase gene are responsible for 4S deficiency, which leads to the intralysosomal storage of partially degraded glycosaminoglycan, dermatan sulfate, and chondroitin 4-sulfate
-
-
?
additional information
?
-
-
mucopolysaccharidosis type VI is an autosomal recessive lysosomal storage disorder caused by the deficiency of N-acetylgalactosamine-4-sulfatase. Mutations in the N-acetylgalactosamine-4-sulfatase gene are responsible for 4S deficiency, which leads to the intralysosomal storage of partially degraded glycosaminoglycan, dermatan sulfate, and chondroitin 4-sulfate
-
-
?
additional information
?
-
-
the enzyme is required for the degradation of the glycosaminoglycan substrates dermatan and chondroitin sulfate. A 4-sulfatase deficiency results in the accumulation of undegraded substrate and causes the severe lysosomal storage disorder mucopolysaccharidosis type VI or Maroteaux-Lamy syndrome. A wide variation in clinical severity is observed between MPS VI patients and reflects the number of different 4-sulfatase mutations that can cause the disorder.Y210C is detected in about 10% of the MPS VI patients
-
-
?
additional information
?
-
-
ARSB removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate and dermatan sulfate
-
-
?
additional information
?
-
-
ASB is a lysosomal exohydrolase, cleaving the 4-sulfate from the N-acetylgalactosamine-4-sulfate residue at the nonreducing terminal of glycosaminoglycan structures
-
-
?
additional information
?
-
-
ARSB removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate and dermatan sulfate
-
-
?
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metabolism
modification of expression of the enzyme regulates the content of chondroitin sulfate
additional information
-
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
-
ARSB mutations are involved in mucopolysaccharidosis type VI, i.e. MPS VI, Maroteaux-Lamy syndrome
malfunction
-
arylsulfatase B is associated with the lysosomal storage disease mucopolysaccharidosis VI
malfunction
-
ASB-deficient cells accumulate dermatan sulfate and chondroitin sulfate, which may be partially hydrolyzed by other lysosomal hydrolases
malfunction
-
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
-
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
-
ARSB enzymatic activity is significantly greater in normal than in malignant tissue
malfunction
-
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
-
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
-
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
-
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
-
ASB and chondroitin 4-sulafte are involved in regulation of interleukin-8 secretion
physiological function
-
arylsulfatase B removes 4-sulfate groups from the sulfated glycosaminoglycans chondroitin-4-sulfate and dermatan sulfate
physiological function
-
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
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L476P
-
mutation in MPS IV cats
C117R
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, severe phenotype
C192R
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, mild phenotype
C447S
associated with the severe phenotype of mucopolysaccharidosis type VI
C53S
-
the mutation causes ASB-deficiency, phenoytpe, overview. The enzyme is taken up into cultured ASB-deficient human fibroblasts, GM00519 cells, and translocates to the lysosomes, it is catalytically active. The enzyme enters target cells predominantly through the CI-M6P receptor. The uptake of rhASB is able to restore lysosomal function in an in vitro cell-based assay
D54N
associated with the severe phenotype of mucopolysaccharidosis type VI
D83Y
associated with the attenuated phenotype of mucopolysaccharidosis type VI
E421X
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, intermediate phenotype
G171D
associated with the attenuated phenotype of mucopolysaccharidosis type VI
G171S
associated with the attenuated phenotype of mucopolysaccharidosis type VI
G308R
-
mutant shows very low level of activity, the expressed mutation significantly reduces the amount of mature protein, the ARSB mutation has a significant effect on enzyme activity, protein processing and mRNA stability
H430R
associated with the attenuated phenotype of mucopolysaccharidosis type VI
I296N
associated with the severe phenotype of mucopolysaccharidosis type VI
K439E
associated with the severe phenotype of mucopolysaccharidosis type VI
K470A
-
mutation leads to an decrease of enzyme activity in the medium to 13% of total activity compared to 25% of the wild-type enzyme, no effect on phosphorylation
K470A/K497A/K507A
-
mutation leads to an decrease of enzyme activity in the medium to 17% of total activity compared to 25% of the wild-type enzyme, no effect on phosphorylation
K470A/K507A
-
mutation leads to an decrease of enzyme activity in the medium to 16% of total activity compared to 25% of the wild-type enzyme, no effect on phosphorylation
K497A
-
mutation leads to an decrease of enzyme activity in the medium to 19% of total activity compared to 25% of the wild-type enzyme, no effect on phosphorylation
K497A/K507A
-
mutation leads to an decrease of enzyme activity in the medium to 18% of total activity compared to 25% of the wild-type enzyme, no effect on phosphorylation
K507A
-
mutation leads to an decrease of enzyme activity in the medium to 23% of total activity compared to 25% of the wild-type enzyme, no effect on phosphorylation
L236P
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, second mutation C405Y, mild phenotype
L321P
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, intermediate phenotype
L72Q
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, heterozygote of L72Q and 219delC/221-230delCGCTGGCGGC on same allele and 743delC on other allele, severe phenotype
L72R
associated with the severe phenotype of mucopolysaccharidosis type VI
L82R
-
mutant shows very low level of activity, the expressed mutation significantly reduces the amount of mature protein, the ARSB mutation has a significant effect on enzyme activity, protein processing and mRNA stability
M142I
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, intermediate phenotype
P313A
-
mutant shows very low level of activity, the expressed mutation significantly reduces the amount of mature protein, the ARSB mutation has a significant effect on enzyme activity, protein processing and mRNA stability
Q456X
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, intermediate phenotype
Q503X
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, intermediate phenotype
R102H
associated with the attenuated phenotype of mucopolysaccharidosis type VI
R160Q
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, intermediate phenotype
R160X
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, intermediate phenotype
R315Q
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, intermediate phenotype
R434I
associated with the attenuated phenotype of mucopolysaccharidosis type VI
R513X
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, heterozygote of the R315X and Y513W alleles, severe phenotype
S240F
-
mutant shows very low level of activity, the expressed mutation significantly reduces the amount of mature protein, the ARSB mutation has a significant effect on enzyme activity, protein processing and mRNA stability
S320R
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, intermediate phenotype
T442M
associated with the attenuated phenotype of mucopolysaccharidosis type VI
T442R
associated with the attenuated phenotype of mucopolysaccharidosis type VI
W146X
second mutation Y210C, mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, intermediate phenotype
W353R
associated with the severe phenotype of mucopolysaccharidosis type VI
Y138C
-
mutant shows very low level of activity, the expressed mutation significantly reduces the amount of mature protein, the ARSB mutation has a significant effect on enzyme activity, protein processing and mRNA stability
C405Y
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, second mutation L236P, mild phenotype
C405Y
associated with the attenuated phenotype of mucopolysaccharidosis type VI
C447F
associated with the severe phenotype of mucopolysaccharidosis type VI
C447F
-
mutant shows very low level of activity, the expressed mutation significantly reduces the amount of mature protein, the ARSB mutation has a significant effect on enzyme activity, protein processing and mRNA stability
C521Y
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, severe phenotype. Second mutation R152W, intermediate phenotype
C521Y
causes large structural changes, associated with the severe phenotype of mucopolysaccharidosis type VI
C91S
catalytically inactive enzyme can be converted into an active enzyme form by vanadate and light
C91S
present at significantly higher levels in conditioned media when compared with the wild type
G137V
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, intermediate phenotype
G137V
causes small structural changes, associated with the attenuated phenotype of mucopolysaccharidosis type VI
G144R
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, severe phenotype
G144R
causes large structural changes, associated with the severe phenotype of mucopolysaccharidosis type VI
G302R
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, severe phenotype
G302R
associated with the severe phenotype of mucopolysaccharidosis type VI
H393P
-
mutation in MPS IV patient
H393P
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, second mutation R95Q, severe phenotype. Second mutation Y210C, intermediate phenotype
H393P
causes large structural changes, associated with the severe phenotype of mucopolysaccharidosis type VI
L360P
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, second mutation R152W and S384N, mild phenotype
L360P
associated with the attenuated phenotype of mucopolysaccharidosis type VI
L472P
associated with the attenuated phenotype of mucopolysaccharidosis type VI
L472P
-
mutant shows very low level of activity, the expressed mutation significantly reduces the amount of mature protein, the ARSB mutation has a significant effect on enzyme activity, protein processing and mRNA stability
L498P
-
mutation in MPS IV patient
L498P
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, second mutation T92M, mild phenotype
L98P
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, second mutation 245delT, intermediate phenotype
L98P
associated with the attenuated phenotype of mucopolysaccharidosis type VI
P116H
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, severe phenotype
P116H
associated with the severe phenotype of mucopolysaccharidosis type VI
P531R
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, mild phenotype
P531R
associated with the attenuated phenotype of mucopolysaccharidosis type VI
R152W
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, second mutation 237-243delGGTGCTC or C521Y, intermediate phenotype. Second mutation L360P or S384N, mild phenotype
R152W
associated with the attenuated phenotype of mucopolysaccharidosis type VI
R315X
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, heterozygote of the R315X and Y513W alleles, severe phenotype
R315X
-
a narturally occuring mutationiin exon 5 of the ARSB gene causing reduced enzyme activity
R95Q
-
mutation in MPS IV patient
R95Q
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, second mutation H393P, severe phenotype
R95Q
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, second mutazion Y210C alleles, mild phenotype
R95Q
causes large structural changes, associated with the severe phenotype of mucopolysaccharidosis type VI
S384N
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, severe phenotype
S384N
associated with the severe phenotype of mucopolysaccharidosis type VI
S65F
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, intermediate phenotype
S65F
associated with the attenuated phenotype of mucopolysaccharidosis type VI
T92M
-
mutation in MPS IV patient
T92M
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, second mutation L489P, mild phenotype
W146L
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, svere phenotype
W146L
associated with the severe phenotype of mucopolysaccharidosis type VI
W146R
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, homozygous, severe phenotype
W146R
associated with the severe phenotype of mucopolysaccharidosis type VI
W146S
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, mild phenotype
W146S
associated with the severe phenotype of mucopolysaccharidosis type VI
Y210C
-
mutation in MPS IV patient
Y210C
mutation in the arylsulfatase B gene responsible for mucopolysaccharidosis, second mutation H393P, intermediate phenotype. Second mutation R95Q, mild phenotype
Y210C
-
the enzyme is synthesized at a comparable molecular size and amount to wild-type enzyme. 33% of the intracellular Y210C mutant enzyme remains as a precursor form, for at least 8 h post labeling and is not processed to the mature lysosomal form. A significant amount of the mutant enzyme escapes the endoplasmic reticulum and is either secreted from the expression cells or underwent delayed intracellular traffic. The mutant enzyme is inactivated and degraded at an enhanced rate in the lysosomal compartment
Y210C
causes small structural changes, associated with the attenuated phenotype of mucopolysaccharidosis type VI
additional information
the vast majority of mucopolysaccharidosis type VI mutant alleles are either unique to a patient or are present in a small number of patients
additional information
-
the vast majority of mucopolysaccharidosis type VI mutant alleles are either unique to a patient or are present in a small number of patients
additional information
-
a large deletion, c.899-1142del, e.iminates the whole exon5, the large deletion mutation g.99367-102002del involves exon 5 and parts of introns 4 and 5 of the arylsulfatase B gene leading to a frameshift and causing apparent homozygosity in a mucopolysaccharidosis type VI patient
additional information
-
ASB silencing and overexpression are associated with alterations in syndecan-1 and decorin expression in MCF-7 cells and in IL-8 secretion in human bronchial epithelial cells. Silencing or overexpression of ASB in normal rat kidney epithelial cells in tissue culture modified the content of total sulfated glycosaminoglycans, chondroitin 4-sulfate, kininogen, and bradykinin in spent media and cell lysates. When ASB is overexpressed, the cellular kininogen that associated with C4S declines
additional information
-
ASB silencing in IB3-1 and C38 bronchial epithelial cell lines and in primary bronchial epithelial cells, leading to reduced ASB activity, chondroitin 4-sulfate content, and increased interleukin-8 content associated to the cell membranes instead of secreted. Neutrophil attraction to the cell lysate is increased in ABS silencing, overview
additional information
a homozygous deletion of exon 4 is observed in a 5-year-old girl who presented with an exaggerated, convex curvature of the back at the age of one year. The mutation leads to abnormal excretion of dermatan sulfate in the urine and extremely low leukocyte ARSB activity. The deletion leads to a truncated protein that lacks most of the catalytic domain. The patient received recombinant human ARSB as enzyme replacement therapy at an early stage (2 years), and responded positively in terms of skeletal development and other developmental milestones
additional information
-
a homozygous deletion of exon 4 is observed in a 5-year-old girl who presented with an exaggerated, convex curvature of the back at the age of one year. The mutation leads to abnormal excretion of dermatan sulfate in the urine and extremely low leukocyte ARSB activity. The deletion leads to a truncated protein that lacks most of the catalytic domain. The patient received recombinant human ARSB as enzyme replacement therapy at an early stage (2 years), and responded positively in terms of skeletal development and other developmental milestones
additional information
-
ASB silencing or overexpression, silencing leads to reduced ASB activity, which than leads to increased chondroitin-4-sulfation, increased binding of kininogen, and reduced bradykinin release
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Oncotarget
8
242-260
2017
Homo sapiens (P15848), Homo sapiens
brenda
Bhattacharyya, S.; Feferman, L.; Tobacman, J.
Inhibition of phosphatase activity follows decline in sulfatase activity and leads to transcriptional effects through sustained phosphorylation of transcription factor MITF
PLoS ONE
11
e0153463
2016
Homo sapiens (P15848), Mus musculus (P50429)
brenda
Bhattacharyya, S.; Feferman, L.; Tobacman, J.
Dihydrotestosterone inhibits arylsulfatase B and Dickkopf Wnt signaling pathway inhibitor (DKK)-3 leading to enhanced Wnt signaling in prostate epithelium in response to stromal Wnt3A
Prostate
79
689-700
2019
Homo sapiens (P15848)
brenda
Bhattacharyya, S.; Feferman, L.; Tobacman, J.K.
Effect of CFTR modifiers on arylsulfatase B activity in cystic fibrosis and normal human bronchial epithelial cells
Pulm. Pharmacol. Ther.
36
22-30
2016
Homo sapiens (P15848)
brenda
Lin, W.D.; Ke, Y.Y.; Chou, I.C.; Wang, C.H.; Tsai, F.J.
Deletion of exon 4 in the N-acetylgalactosamine-4-sulfatase gene in a Taiwanese patient with mucopolysaccharidosis type VI
Tohoku J. Exp. Med.
235
267-273
2015
Homo sapiens (P15848), Homo sapiens
brenda