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)

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

Two brothers, aged 40 and 38 years, suffered from dysplastic features, coarse facies, bone and skeletal abnormalities, deformities of spine, and joint impairments. Body heights were 168 and 164 cm, respectively. Enlargement of liver and spleen, cardiac insufficiency, marked corneal clouding, and hernias were absent. Both patients had signs of cervical and lumbar radiculopathy and cervical myelopathy (tetraspastic syndrome). Vacuoles, acid phosphatase-positive granules, and metachromatic inclusions were found in peripheral lymphocytes; granulocytes and monocytes contained azurophilic hypergranulation. By electron microscopy, clear membrane-bound vacuoles were noted in lymphocytes (but not in neurtrophils), fibroblasts, Schwann cells, mural cells of the vasculature, and epidermal cells. Leukocytes, urine, and cultured skin fibroblasts revealed a deficiency of arylsulfatase B (N-acetylgalactosamine 4-sulfate sulfatase). The 6-year-old daughter of one of the patients has an intermediate level of this enzyme. Fibroblasts exhibited a constant intracellular accumulation of 35S-labeled mucopolysaccharides. The urine of one of the brothers showed an abnormal mucopolysacchariduria; in both, the presence of urinary dermatan sulfate could be demonstrated. These findings conform to the mild B variant of Maroteaux-Lamy syndrome with high longevity.
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PMID:Deficiency of arylsulfatase B in 2 brothers aged 40 and 38 years (Maroteaux-Lamy syndrome, type B). 12 48

A 6-sulfatase specific for sugasr of the galactose configuration was purified 81-fold from the crude extract of Actinobacillus sp. IFO-13310. This preparation contained activity towards both N-acetylgalactosamine 6-sulfate and galactose 6-sulfate (relative activity, 2.4 : 1). The enzyme also release inorganic sulfate from the non-reducing galactose 6-sulfate end group of a trisaccharide disulfate prepared from keratan sulfate by sequential degradation with endo-beta-galactosidase, N-acetylglucosamine-6-sulfatase and exo-beta-N-acetylglucosaminidase. In addition, a tetrasaccharide trisulfate bearing the non-reducing N-acetylglucosamine 6-sulfate end group, also enzymatically prepared from keratan sulfate, was degraded to give rise to inorganic sulfate, N-acetylglucosamine and galactose by the sequential action of this enzyme, N-acetylglucosamine-6-sulfatase, exo-beta-N-acetylglucosaminidase and exo-beta-galactosidase (Charonia lampas).
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PMID:Galactose-6-sulfatase from Actinobacillus sp. IFO-13310 and its action on sulfated oligosaccharides from keratan sulfate. 15 51

Chondroitin sulfates, dermatan sulfate, heparan sulfate, heparin, keratan sulfate, and oligosaccharides derived from these sulfated glycosaminoglycans have been used for the measurement of sulfatase activity of rat skin extracts. Chromatographic fractionation of the extracts followed by specificity studies demonstrated the existence of five different sulfatases, specific for 1) the nonreducing N-acetylglucosamine 6-sulfate end groups of heparin sulfate and keratan sulfate, 2) the nonreducing N-acetylgalactosamine (or galactose) 6-sulfate end groups of chondroitin sulfate (or keratan sulfate), 3) the nonreducing N-acetylgalactosamine 4-sulfate end groups of chondroitin sulfate and dermatan sulfate, 4) certain suitably located glucosamine N-sulfate groups of heparin and heparan sulfate, or 5) certain suitably located iduronate sulfate groups of heparan sulfate and dermatan sulfate. Two arylsulfatases, one of which was identical in its chromatographic behaviors with the third enzyme described above, were also demonstrated in the extracts. These results taken together with those previously obtained from studies on human fibroblast cultures suggest that normal skin fibroblasts contain at least five specific sulfatases and diminished activity of any one may result in a specific storage disease.
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PMID:Separation and properties of five glycosaminoglycan sulfatases from rat skin. 46 69

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

The Dyggve-Melchior-Clausen (DMC) syndrome includes short stature, dwarfism, mental retardation, and skeletal abnormalities especially in the spine and the extremities resembling the findings in the mucopolysaccharidoses. A particular abnormality is the "lace border" found on radiological examination of the iliac crest. The three original cases have been followed for 15--20 years and the course is characterized by increasing mental retardation and motor disability whereas the "lace border" is less pronounced than before. A survey of 17 other cases is given and similarities and differencies to the mucopolysaccharidoses are pointed out. Patients with the DMC syndrome have been suggested to be deficient in an enzyme cleaving glycoprotein-acid mucopolysaccharide (AMP) linkage. We have previously found in DMC patients, an abnormal excretion of urinary AMP's of which some were undersulfated and some were oversulfated. Lysosomal acid proteinase, i.e., cathepsin D and neutral proteinases: elastase and cathepsin G were found to be normal in DMC patients. However, alfa2-macroglobulin in serum was raised. This increase may cause an inhibition of the neutral proteinases. An increased level of chondroitin sulfate N-acetylgalactosamine-6-sulfate-sulfatase and decreased enzymic levels of aryl sulphatase A and B (assayed with p-nitrocatecholsulfate as a substrate) were found in leucocytes of DMC patients. Metabolic studies have revealed an unbalanced incorporation of glycoprotein AMP-precursors in DMC lymphocytes. All in all the data suggests the DMC syndrome to be an inborn error of glycoprotein-AMP-metabolism.
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PMID:The Dyggve-Melchior-Clausen (DMC) syndrome. A 15 year follow-up and a survey of the present clinical and chemical findings. 57 40

Sulphatases B1alpha and B1beta (EC 3.1.6.1) have been prepared as apparently homogeneous proteins by chromatography on ConA-Sepharose. Both have a mol. wt. of 56 000, and E1%280nm of 17 and a turnover number of 8600 min-1 with nitrocatechol sulphate as substrate. Their amino acid compositions are identical: like sulphatase A, the sulphatases B are rich in proline and yield glucosamine on hydrolysis. They are not altered by treatment with neuraminidase. Both fractions show strong UDP-N-acetylgalactosamine 4-sulphatase activity, weak iduronate sulphatase activity, but no significant heparan N-sulphatase activity. It is suggested that the physiological activity of sulphatase B is that of the N-acetylgalactosamine 4-sulphatase which is lacking in the Maroteaux-Lamy Syndrome.
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PMID:The sulphatase of ox liver. XX. The preparation of sulphatases B1alpha and B1beta. 100 20

Lectin cytochemistry was performed to clarify the process of glycosylation and the localization of glycocalyx in osteoclasts. Microslicer sections of decalcified rat tibiae were incubated in the presence of HRP-conjugated lectins (Con A, PNA, MPA, WGA, UEA-1). Lectin reactions in cell organelles revealed that glucose (Glc) and mannose (Man) are transferred to carbohydrate chains in nuclear envelopes, rough endoplasmic reticuli, and the cis and medial sides of the Golgi apparatus. N-acetylgalactosamine (GalNAc), N-acetylglucosamine (GlcNAc), and/or N-acetylneuraminic acic (NANA) residues are transferred, in turn, in the Golgi apparatus. Lectin reactions detected in lysosomal structures suggest that some sugar residues are incorporated into carbohydrate chains of hydrolytic enzymes, such as acid phosphatase and arylsulfatase. Others would be transported to plasma membranes as glycocalyx. PNA and MPA reactions were most evident on ruffled borders of osteoclasts. On the other hand, cement-line-like structures on bone surfaces displayed Con A, MPA, and WGA positive reactions. The following factors suggest that osteoclasts actively metabolize sugar: characteristic localization of glycocalyx in osteoclasts reflect the polarity of osteoclasts, and carbohydrate complexes in cement-line-like structures seem to play an important role in the coupling phenomenon in bone tissue.
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PMID:Characteristic localization of carbohydrates in osteoclasts by lectin cytochemistry. 147 18

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

N-Acetylgalactosamine-6-sulfate sulfatase from human placenta was purified 33,600-fold using beta-N-acetyl-D-galactosamine 6-sulfate-(1----4)-beta-D-glucuronic acid-(1----3)-N-acetyl-D-[3H]galactosaminitol 6-sulfate as the substrate. This enzyme is an oligomer with a molecular mass of 120 kDa and consists of polypeptides of 40 and 15 kDa. The 15 kDa polypeptide is a glycoprotein. This purified protein has activities of N-acetylgalactosamine-6-sulfate sulfatase and galactose-6-sulfate sulfatase. Rabbit antiserum was raised against the purified protein. The antibody titrated N-acetylgalactosamine-6-sulfate sulfatase and galactose-6-sulfate sulfatase. The size of the precursor of the enzyme is 60 kDa, as determined by cell-free translation. The optimal pH values of the N-acetylgalactosamine-6-sulfate sulfatase and galactose-6-sulfate sulfatase activities are pH 3.8-4.0, and the Kms are 8 and 13 microM, respectively. Sulfate and phosphate ions are potent competitive inhibitors for the enzyme and their inhibition constants are 35 and 200 microM, respectively. Cross-reactive materials of 40 and 15 kDa were detected by immunoblot analysis, in the placenta, liver, and normal fibroblasts, but not in fibroblasts from a patient with Morquio disease.
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PMID:N-acetylgalactosamine-6-sulfate sulfatase in human placenta: purification and characteristics. 179 86


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