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)

The biosynthesis of arylsulfatase A in human skin fibroblasts was studied by labeling cells and isolating arylsulfatase A using immune precipitation and polyacrylamide gel electrophoresis under denaturing and reducing conditions. Arylsulfatase A was synthesized as precursor polypeptides of 62 kDa or 59.5 kDa. Cell lines synthesizing either or both polypeptides were found. The results of a family study were consistent with the assumption that the two arylsulfatase A polypeptides are of allelic nature. In various heterozygous cell lines, the two polypeptides were formed at equal or different rates. The relative rate of biosynthesis was constant for an individual cell line, suggesting that both allelic products were under separate genetic control. In a group of 21 unrelated individuals, the gene frequency of alleles for the 62- and 59.5-kDa precursor forms was 3:1. The two allelic forms of the arylsulfatase A polypeptides were converted into a 57-kDa form by endo-beta-N-acetylglucosaminidase H, an enzyme specifically removing asparagine-linked oligosaccharides of the high-mannose (and hybrid) type. The apparent difference in the number of asparagine-linked oligosaccharides suggests that the two allelic genes differ in a region coding the sequence Asn-X-Thr(Ser), which is required for attachment of asparagine-linked oligosaccharides.
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PMID:Two allelic forms of human arylsulfatase A with different numbers of asparagine-linked oligosaccharides. 613 51

The biosynthesis of arylsulfatase A was studied in cultured fibroblasts by pulse-chase labeling with [2-3H]mannose; the enzyme was isolated by immunoprecipitation and denaturing polyacrylamide gel electrophoresis. In normal fibroblasts, and in fibroblasts from a patient with multiple sulfatase deficiency, the enzyme was synthesized as a glycoprotein of apparent molecular weight of 59,000; half of it was processed over a period of 4 days to Mr = 57,000. The precursor chain of Mr = 59,000 was secreted in the presence of 10 mM NH4Cl. An immunoprecipitable glycoprotein of normal size was synthesized by fibroblasts from two unrelated patients with metachromatic leukodystrophy, but this material disappeared within twenty hours. In fibroblasts from an individual with pseudo-deficiency of arylsulfatase A, the immunoprecipitable precursor glycoprotein was smaller (Mr = 56,000). The synthesis of cross-reactive proteins with altered properties supports the concept of allelic mutations as the genetic basis of metachromatic leukodystrophy and of arylsulfatase A pseudo-deficiency.
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PMID:Synthesis and maturation of cross-reactive glycoprotein in fibroblasts deficient in arylsulfatase A activity. 613 6

Lysosomal arylsulfatases A and B of peripheral leukocytes from patients with chronic myelogenous leukemia and from healthy subjects were studied. Two enzyme activities of leukemia cells were significantly higher than those of cells from healthy subjects, irrespective of total and differential counts of leukemic cells. Upon anion-exchange chromatography, the arylsulfatases of chronic myelogenous leukemia cells and normal leukocytes were separated into the basic B enzyme and its anionic variant (B1) and A enzyme. However, the amount of B1 enzyme relative to B enzyme or the activity ratio of B1 enzyme to total arylsulfatase B (B + B1) was higher in chronic myelogenous leukemia cells than in normal cells. The anionic property of the enzyme was found to be due to phosphate groups bound to the carbohydrate moiety of the arylsulfatase, based on the following results. When B1 enzyme was treated with alkaline phosphatase followed by isoelectric focusing, it was changed to a less anionic enzyme with heterogeneous components which are ascribed to phosphodiester groups linked to the heterogeneous carbohydrate moiety of the enzyme; no effect was observed by sialidase treatment. Upon treatment of B1 enzyme with endo-beta-N-acetylglucosaminidase H, which cleaves sugar chains of a high mannose type in glycoproteins, the anionic heterogeneous components were converted to the basic component similar to B enzyme. From our present and previous observations, it can be concluded that the increase of phosphorylated forms of the lysosomal hydrolase represents one characteristic of rapidly proliferating neoplastic cells.
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PMID:Lysosomal arylsulfatases of human leukocytes: increment of phosphorylated B variants in chronic myelogenous leukemia. 613 78

Cerebroside sulfatase also known as arylsulfatase A from human liver displays six microheteromer bands upon narrow pH range isoelectric focusing. Sialic acid residues only partially account for this enzyme multiplicity since neuraminidase treatment reduces the number of bands to three. Uptake studies with cultured fibroblasts strongly suggest arylsulfatase A has covalently bound mannose 6-phosphate residues. However, treatment with alkaline phosphatase and a battery of glycohydrolases failed to reduce the number of enzyme charge forms below three. These results imply that the neuraminidase-resistant charge microheterogeneity is not due to structures associated with the carbohydrate moiety of arylsulfatase A.
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PMID:Microheterogeneity of arylsulfatase a: Treatment with hydrolytic enzymes. 614 17

Metachromatic leukodystrophy is a recessively inherited disease of children and adults. The basic disorder is a failure of the catabolism of sulfatide, the sulfate ester of galactose cerebroside. This lipid is a component of the myelin membrane and is probably a component of neuronal membranes as well. The various forms of clinical presentation, the aids to diagnosis, the genetic variations of arylsulfatase A, the enzyme involved in sulfatide catabolism, and possible approaches to therapy are presented.
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PMID:Metachromatic leukodystrophy: clinical and enzymatic parameters. 615 12

Human lung cancer transplanted into athymic mice contains predominantly an acidic variant (designated B1) of lysosomal arylsulfatase B. B1 enzyme was suggested to be phosphorylated and sialylated (Gasa, S., Makita, A., Kameya, T., Kodama, T., Koide, T., Tsumuraya, M., and Komai, T. (1981) Eur. J. Biochem. 116, 497-503). In order to determine the localization of phosphate in B1 enzyme, we labeled in vivo the transplanted tumor with [32P]H3PO4 or [3H]glucosamine and purified B1 enzyme by immunoprecipitation. Bio-Gel chromatography of the labeled B1 enzyme treated with endoglycosidase H demonstrated that both the excluded and included materials were labeled with 32P and 3H. From acid hydrolysate of the excluded materials, phosphorylated serine and threonine were detected. Protein phosphorylation of arylsulfatase was confirmed by in vitro labeling experiments with [gamma-32P]ATP. By incubation of the tumor homogenate with ATP followed by isolation of the enzymes, B1 enzyme had a significant amount of radioactivity, whereas the B enzyme had little; by exogenous protein kinase, partially purified B enzyme was phosphorylated 35 times more than B1 enzyme. Acid hydrolysate of the included materials in the Bio-Gel column demonstrated mannose 6-phosphate and an unknown phosphorylated compound which migrates more than Man-6-P on electrophoresis and chromatography.
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PMID:Phosphorylation on protein and carbohydrate moieties of a lysosomal arylsulfatase B variant in human lung cancer transplanted into athymic mice. 640 42

To elucidate precise chemical nature of urinary keratan sulfate (KS) of Morquio's disease, crude glycosaminoglycans (GAG) were separated from 24-hr urines of 3 patients with Morquio's disease and from pooled urine of a healthy boy, using cetylpyridinium chloride. KS fractions were then separated from the crude GAG after removal of other GAG and acidic glycopeptide by successive digestion with testicular hyaluronidase and chondroitinase ABC, and by nitrous acid treatment, followed by Dowex 1 column chromatography. The distribution of KS in several fractions (1.5 M Fr-5.0 M Fr) obtained by Dowex 1 column chromatography suggested polydispersity of urinary KS. The relative amounts (micrograms/24-hr urine/kg body weight) of the KS fractions excreted into Morquio's urine were 52-63 times as much as that excreted into normal urine. The KS fractions contained galactose, glucosamine and sulfate as the major constituents, together with fairly amounts of galactosamine and sialic acid, and small amounts of mannose, L-fucose and glucose. The KS fractions resembled sulfated glycopeptide with respect to the sugar composition. The contents of sulfate and sialic acid in each KS fraction from Morquio's urine were higher than those in the corresponding one from normal urine, whereas opposite was the case for the ratio of glucosamine to galactosamine. The sulfate contents in the KS fractions from Morquio's urine indicated that the patient excreted over-sulfated KS into urine. The chemical compositions of the KS fractions from Morquio's urine suggest that the sulfatase specific for 6-sulfate linked to sugars with the galactose configuration may act in a early step of the catabolism of oversulfated KS in the normal tissues.
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PMID:Urinary keratan sulfate of Morquio's disease. 645 53

Arylsulfatases B1 and B2 isolated from human brain were introduced into neonatal type MSD fibroblast culture. Arylsulfatase B2 was linearly taken up into MSD fibroblasts with respect to time and the dose of enzyme, whereas arylsulfatase B1 enzyme was practically not taken up into cells. Uptake of arylsulfatase B2 was inhibited in the presence of mannose 6-phosphate. These data suggest that the biological functional difference between arylsulfatases B1 and B2 is due to the presence of a phosphorylated residue acting as a recognition marker on one of the enzymes.
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PMID:A comparative study of brain arylsulfatases B1 and B2: the difference between the two forms in rates of uptake by multiple sulfatase deficient (MSD) disorder fibroblasts. 665 67

We have prepared a new substrate (o-beta-D-sulfo-galactosyl-(1-4)-beta-D-6-sulfo-2-acetamido-2-deoxyglucosyl- (1-4)-D-[1-3H]galactitol), from shark cartilage keratan sulfate, for the assay of galactose 6-sulfate sulfatase activity. Using this substrate, we found there was a striking deficiency of galactose 6-sulfate sulfatase activity, in addition to the known deficiency of N-acetylgalactosamine 6-sulfate sulfatase, in the cultured skin fibroblasts of patients with Morquio syndrome. Our results could be explained by the hypothesis that accumulation of keratan sulfate and chondroitin 6-sulfate in Morquio syndrome is due to a deficiency of galactose 6-sulfate sulfatase and N-acetylgalactosamine 6-sulfate sulfatase activity, which are necessary for the degradation of these two mucopolysaccharides.
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PMID:Galactose 6-sulfate sulfatase activity in Morquio syndrome. 680 61

We have isolated from monkey (Macaca radiata) brain lysosomal fraction by phosphomannan-Sepharose chromatography a protein that binds four different lysosomal enzymes, beta-hexosaminidase, beta-glucuronidase, alpha-L-fucosidase and arylsulfatase. The isolated protein which appeared in an aggregated homogeneous form on gel electrophoresis under non-denaturing conditions at both pH 8.3 and pH 5.0 was found to be heterogeneous on SDS-gel electrophoresis with molecular weights less than 67,000. Binding was partly abolished by periodate treatment or by alkaline phosphatase treatment of the lysosomal enzymes. Binding was completely abolished by pronase digestion of the binding protein. Of the different sugars tested for inhibition of binding, mannose-6-phosphate was most effective followed by mannose and N-acetyl glucosamine while glucose and fucose were ineffective.
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PMID:A binding protein for lysosomal enzymes isolated from brain by phosphomannan-sepharose chromatography. 684 56


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