Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.6.1 (sulfatase)
3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Arylsulphatases A and B (EC 3.1.6.1) of rabbit kidney cortex were purified 5250- and 7720-fold respectively by a multiple-column-chromatography method. The specific activity toward 4-nitrocatechol sulphate was 42mumol/min per mg for arylsulphatase A and 62 mumol/min per mg for arylsulphatase B. Each enzyme migrated as a single band on polyacrylamide-gel electrophoresis, and the enzyme activity corresponded to the band of protein on the gel. The rate of hydrolysis of ascorbic acid 2-sulphate by arylsulphatase A was three times that for cerebroside 3-sulphate. Arylsulphatase B hydrolysed UDP-N--acetylgalactosamine 4-sulphate and glucosamine 4,6-disulphate, but not galactosamine 6-sulphate.
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PMID:Purification and some properties of arylsulphatases A and B from rabbit kidney cortex. 1 14

Patients with the DMC syndrome have been suggested to possess a specific sulfatase abnormality and/or to be deficient in a proteinase cleaving glycoprotein-acid mucopolysaccharide (AMP) linkage. We have previously found in DMC patients an abnormal excretion of urinary AMPs of which hyaluronic acid and chondroitin sulfate (A + C) were oversulfated and keratosulfate and heparan sulfate were undersulfated. Lysosomal acid proteinase, i.e. cathepsin D (EC 3.4.23.5) and neutral proteinase : elastase (EC 3.4.21.11) and cathepsin G were found to be normal in DMC patients. However, alpha 2-macroglobulin in serum was raised. This increase may be associated with a complex formation of alpha 2-macroglobulin with a neutral proteinase released from the cells. Increased levels of chondroitin sulfate N-acetylgalactosamine-6-sulfate sulfatase and sulfamidase and decreased enzymic levels of arylsulfatase A and B (EC 3.1.6.1) were found in leucocytes of DMC patients. The sulfatase activities assayed in the present study support our theory that a specific sulfatase abnormality may exist in the DMC syndrome.
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PMID:Lysosomal (leucocyte) proteinase and sulfatase levels in Dyggve-Melchior-Clausen (DMC) syndrome. 7 86

The trisaccharide 6-sulfo-N-acetylgalactosamine-glucuronic acid-6-sulfo-N-acetyl-[1-3H]galactosaminitol was used as a substrate for the determination of N-acetylgalactosamine-6-sulfate sulfatase activity. The amount of liberated sulfate was measured indirectly by separating monosulfated reaction products from the substrate on Dowex 1 X 2 microcolumns in a simple two step procedure. Fibroblast homogenates from patients with various genotypes, except classical Morquio's disease, released 410 +/- 90 pmol sulfate/h/mg cell protein. The enzyme exhibited a pH optimum of pH 4.8 and a KM of about 1 X 10(-4) mol/1. It was strongly inhibited by phosphate, sulfate and chloride ions. In three cell lines from patients with classical Morquio's disease a residual activity between 1 and 2% of the mean normal activity was found. All cell lines tested released sulfate from 6-sulfo-N-acetylglucosamine-glucuronic acid-[1-3H]-anhydromannitol. Cell extracts from cultured amniotic fluid cells exhibited a N-acetylgalactosamine-6-sulfate sulfatase activity between 120 and 320 pmol/h/mg protein. An enzyme activity of 370 +/- 100 pmol sulfate/h/mg protein was found in peripheral leucocytes from healthy donors. The determination of N-acetyl-galactosamine-6-sulfate sulfatase activity in one family with an affected patient indicated that the enzyme deficiency is also expressed in leucocytes.
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PMID:A sensitive procedure for the diagnosis of N-acetyl-galactosamine-6-sulfate sulfatase deficiency in classical Morquio's disease. 9 44

The activity of N-acetyl galactosamine-6-sulfate sulfatase was studied for the first time in the liver and brain of a patient with a clinically typical case of Morquio syndrome with keratosulfaturia. As has been demonstrated in the fibroblasts of patients with this syndrome, this enzymatic activity was markedly decreased in both organs. Neuropathological examination revealed moderately swollen neurons containing PAS-positive, coarse globular inclusions in the cerebral cortex, Ammon's horn, basal ganglia, and thalamic nuclei. Ultrastructurally, the inclusions consisted of stacked, straight or loose, wavy membranes of various lengths, often associated with pale or moderately electron dense homogeneous "lipid droplets." These ultrastructural features of the inclusions were closely similar to the granulomembranous bodies of Hurler syndrome and the inclusions described in type B of the Sanfilippo syndrome. Unlike those mucopolysaccharidoses, however, no abnormalities were found in the gangliosides in the brain of the patient with Morquio syndrome.
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PMID:The Morquio syndrome: neuropathology and biochemistry. 10 45

Cultured fibroblasts from two individuals with multiple sulfatase deficiency (MSD) were found to have decreased activities of arylsulfatases (aryl-sulfate sulfohydrolase, EC 3.1.6.1) A, B, and C as well as iduronate-sulfate sulfatase, sulfamidase, and N-acetylglucosamine-6-sulfate sulfatase. The activity of N-acetylgalactosamine-6-sulfate sulfatase was decreased in one line but not in the other. Mixtures of MSD cell extracts with extracts from normal cells did not result in inhibition of normal sulfatase activities. Mixtures of MSD cell extracts with extracts of fibroblasts from patients with Hunter or Sanfilippo A syndrome did not activate iduronate-sulfate sulfatase or sulfamidase activity. Heterokaryons formed by fusion of MSD cells with Sanfilippo A fibroblasts demonstrated a partial correction of the enzyme deficiency. In similar manner, MSD-Hunter heterokaryons showed a significant increase in iduronate-sulfate-sulfatase activity. Genetic complementation in heterokaryons of MSD fibroblasts and cells of either Sanfilippo A or Hunter syndrome implies a genetic defect in MSD different from that causing specific sulfatase deficiencies.
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PMID:Genetic complementation studies of multiple sulfatase deficiency. 11 67

A 14-year-old white girl with mild dysostosis multiplex, odontoid hypoplasia, short stature, cloudy corneas, keratansulfaturia, but without detectable central nervous system abnormalities was referred with the diagnosis of Morquio syndrome. Clinical and roentgenographic findings were minimal compared to those of typical patients with the Morquio syndrome, MPS IV. Beta-Galactosidase activity in extracts of the patient's cultured fibroblasts was deficient, while that of galactosamine-6-sulfate sulfatase was normal. Conjunctival biopsy revealed intracytoplasmic vacuoles typical of lysosomal storage diseases. It is postulated that in this patient the deficiency of a beta-galactosidase is responsible for inadequate degradation of keratan sulfate and the appearance of a mild form of the Morquio syndrome (MPS IVB).
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PMID:Morquio-like syndrome with beta galactosidase deficiency and normal hexosamine sulfatase activity: mucopolysacchariodosis IVB. 41 14

Fibroblasts of four patients affected with mucosulfatidosis (multiple sulfatase deficiency, Austin variant of metachromatic leukodystrophy) were assayed for activities of the five sulfatases known to degrade mucopolysaccharides. These were iduronide 2-sulfate sulfatase, sulfamidase, N-acetyl-galactosamine 6-sulfate sulfatase, arylsulfatase B (N-acetylgalactosamine 4-sulfate sulfatase), and N-acetylglucosamine 6-sulfate sulfatase. The activities of these five sulfatases were severely depressed, thus confirming the known deficiency of arylsulfatase B and the absence of the Hunter and Sanfilippo III A corrective factors that have iduronide 2-sulfate sulfatase and sulfamidase activity, respectively. Together with earlier reports of the deficiencies of arylsulfatases A and C, cholesteryl sulfatase, and dehydroepiandrosterone sulfatae, mucosulfatidosis is now characterized by the deficiency of nine different sulfatases.
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PMID:Multiple deficiency of mucopolysaccharide sulfatases in mucosulfatidosis. 52 91

An enzyme preparation from cultured chick embryo vertebral chondrocytes attacks chondroitin SO4 oligosaccharides from the nonreducing terminal in a recycling pathway involving the sequential action of a beta-glucuronidase, a 4- or a 6-sulfatase, and a beta-N-acetylgalactosaminidase. The sequence is blocked by saccharo-1,4-lactone, an inhibitor of the beta-glucuronidase, or by 2-acetamido-2-deoxy-D-galactonolactone, an inhibitor of the beta-N-acetylgalactosaminidase. The level of 4-sulfatase activity is low relative to the other activities and limits the rate of catabolism of hybrid oligosaccharide structures containing both 6-sulfated galactosamine residues and 4-sulfated galactosamine residues. This results in the accumulation of shortened oligosaccharides, most of which have galactosamine-4-SO4 residues at their nonreducing terminals. In the presence of the lactone inhibitors, polymeric chondroitin SO4 is broken down by the enzyme preparation to oligosaccharides which are 10 to 15 monosaccharides long, indicating that degradation of chondroitin SO4 chains is initiated by an endoglycosidase which generates oligosaccharide substrates for the recycling exoglycosidase system.
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PMID:Chondroitin SO4 catabolism in chick embryo chondrocytes. 57 Sep 72

Human N-acetylgalactosamine-6-sulfate sulfatase (6-sulfatase) activity is measured by using as a substrate a sulfated tetrasaccharide obtained by digesting purified chondroitin-6-sulfate (C-6-S) with testicular hyaluronidase. The amount of inorganic sulfate released is measured turbidimetrically. The enzyme from human kidney has a pH optimum of 4.8; its activity is augmented by low levels of NaCl and inhibited by phosphate and high levels of NaCl. Free glucuronate, acetylgalactosamine, inorganic sulfate, polymeric C-6-S, or tetrasaccharide obtained from chondroitin-4-sulfate do not affect the enzyme activity. The method may be used for the diagnosis of Morquio disease since extracts of Morquio fibroblasts are devoid of 6-sulfatase activity.
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PMID:N-acetylgalactosamine-6-sulfate sulfatase in man. Absence of the enzyme in Morquio disease. 82 Jul 16

Mucopolysaccharidosis type IVA (MPS IVA) results from a genetic deficiency of N-acetylgalactosamine-6-sulfate (Gal-NAc6S) sulfatase. We have identified two different exonic mutations causing GalNAc6S sulfatase deficiency in two unrelated Japanese families, in one patient with classical Morquio disease, and in two brothers with a mild form of MPS IVA. The nucleotide sequence of the full-length cDNA derived from a patient with classical Morquio disease revealed a two-base deletion at nucleotide position 1343-1344 (1344-1345 or 1345-1346) that altered the reading frame (designated 1342delCA). This mutation, inherited from the proband's consanguineous parents, was revealed by TaqI restriction analysis of a cDNA fragment amplified by the polymerase chain reaction. In the proband with the mild form of the disease, a C to G transversion at nucleotide 667 predicted the substitution of Lys for Asn204 (N204K). Since a new AluI site was created by the N204K mutation, restriction analysis indicated that the affected brothers were homozygous for this mutation, as confirmed by the finding that both their parents had this lesion. Transient expression in GalNAc6S sulfatase deficient fibroblasts of these two mutant alleles showed completely deficient or markedly decreased enzyme activities, thereby indicating that these two mutations were responsible for the enzyme deficiency.
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PMID:Mucopolysaccharidosis type IVA. N-acetylgalactosamine-6-sulfate sulfatase exonic point mutations in classical Morquio and mild cases. 152 13


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