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)

Arylsulfatase A and B activities were assayed in leucocytes of 43 controls, 11 cases of Metachromatic Leucodystrophy and 7 parents or siblings of patients, using a new technique implying specific inhibitors for leucocyte enzymes. Heterozygotes can be determined, with a 50% value compared to the control, in variant B. Electrophoresis of leucocytes after enzymatic staining for arylsulfatase, is a complementary technique which allowed the detection of a new form of metachromatic leucodystrophy.
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PMID:Arylsulfatases isoenzymes in metachromatic leucodystrophy/detection of a new variant by electrophoresis improvement of quantitative assay. 0 67

Metachromatic leukodystrophy and Maroteaux-Lamy syndrome can be diagnosed by assay of leukocyte or fibroblast arylsulfatase A and B activity with the fluorogenic substrate 4-methylumbelliferyl sulfate. The arylsulfatases are extracted into a 27000 x g supernatant by sonication in 0.9% sodium chloride and then separated with CM-32 on columns or in test tubes. In 0.05 M sodium acetate pH 6.0, arylsulfatase A is not absorbed while arylsulfatase B is retained by the resin. The arylsulfatase B is then eluted from the resin with 0.3 M sodium chloride. The arylsulfatase A activity obtained from normal leukocytes and fibroblasts is linear for the initial 10 minutes of the reaction, is stimulated 3-fold by 6 mM lead acetate and inhibited 80% by 0.24 mM silver nitrate. After separation with CM-32, the arylsulfatase B activity is stimulated 3-fold by Triton X-100 (0.1%). Arylsulfatase A but not arylsulfatase B is destroyed by heat (60 degrees). Both leukocyte and fibroblast arylsulfatase A activity was reduced to 11% of control values in metachromatic leukodystrophy. Essentially no arylsulfatase B activity was detected in cells from patients with Maroteaux-Lamy syndrome. Metachromatic leukodystrophy heterozygotes but not Maroteaux-Lamy syndrome heterozygotes can also be distinguished by this method. A heat inactivation technique utilizing the differential thermal stabilities of the two enzymes for diagnosis of patients with Marotezux-Lamy syndrome is also described. The advantages of these 4-methylumbelliferyl sulfate assay procedures over the p-nitrocatechol sulfate method of assay are greater sensitivity, selectivity for the desired enzyme and potential for use in large scale testing.
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PMID:Arylsulfatases A and B in metachromatic leukodystrophy and Maroteaux-Lamy syndrome: studies with 4-methylumelliferyl sulfate. 0 5

A correlation between increased arylsulfatase activities and decreased sulfated proteoglycan content in human osteoarthritic articular cartilage suggested a possible interrelationship between these parameters. Since we had previously shown that ascorbate caused a decrease in levels of arylsulfatase A and B activities in normal chondrocyte cultures, the validity of the above relationship was examined by measuring the effect of vitamin C on the biosynthesis and distribution of 35S-labeled proteoglycans and arylsulfatase A and B activities in cell extracts of chondrocytes derived from normal and osteoarthritic tissue. Arylsulfatase A and B activities were found to be reduced in the presence of ascorbic acid in all normal and osteoarthritic cell lines examined when measured 3, 6, 10, and 13 days after the introduction of the vitamin in the culture medium. Acid phosphatase activity, on the other hand, was found to be elevated in the presence of ascorbate. The inhibitory effect by ascorbic acid on arylsulfatase activities could be reversed by withdrawing the vitamin from the nutrient medium. Addition of EDTA to the cell extracts before assay also reversed the inhibiton. Sulfated proteoglycan biosynthesis as reflected in 35S-sulfate uptake per milligram of DNA was significantly increased in the presence of ascorbic acid. The distribution of the newly synthesized molecules between the cell layer and medium fractions was altered. In the presence of ascorbate, more deposition into the cell layer of newly synthesized macromolecules occurred. These data suggest an inverse relationship between arylsulfatase activities and the stability of the newly synthesized sulfated proteoglycans in the extracellular matrix.
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PMID:Effect of ascorbic acid on arylsulfatase activities and sulfated proteoglycan metabolism in chondrocyte cultures. 1 19

Arylsulfatase A and B in urine have been estimated in 18 normal subjects and 50 bilharziasis patients. The bilharziasis patients were divided into two groups according to the type of infeciton. Those with bilharziasis haematobian type of infection and those with the bilharziasis mansoni type. Each group was further subdivided into subgroups according to the severity and progress of the disease. The activities of arylsulfatase A and B were significantly elevated in all the groups of patients studied and it is evident that there is a progressive increase with the progress of the disease in both types of bilharziasis infections (the haematobian and mansoni types). Liver dysfunction consequent of bilharzial infestation appears to take part in the mechanism of induction of the bilharzial bladder cancer.
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PMID:Arylsulfatases in bilharziasis. 2 42

We measured the protein, arylsulfatase A and sphingomyelinase activities in the total normal rat sciatic nerve and in the proximal and distal stumps. The protein level of the whole sciatic nerve (about 8 % of fresh weight) is similar to the levels of the stumps. Arylsulfatase A activity, in the total sciatic nerve as well as in the stumps is more important by gram of fresh weight than the sphingomyelinase activity. Both enzymes activities, by gram of fresh weight, are more important in the proximal stumps than in the distal ones.
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PMID:[Arylsulfatase A and sphingomyelinase activities in the normal sciatic nerve of the rat, and in proximal and distal fragments]. 3 67

Arylsulfatase A was purified to apparent homogeneity from normal human livers obtained at autopsy. According to gel electrophoresis in sodium dodecyl sulfate, purified arylsulfatase A consistently contained two subunits of slightly different sizes: approximately 69 000 and 57 000 daltons, but were not present in stoichiometrically equal amounts. Peptide maps of the entire enzyme and of the two individual subunits showed that the two polypeptides share similar if not identical sequences. These observations raise the possibility that the smaller polypeptide might be derived from the larger one. The sensitive peptide mapping procedures employed will make feasible future studies with the abnormal enzyme found in metachromatic leukodystrophy.
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PMID:Studies in metachromatic leukodystrophy. XIV. Purification and subunit structure of human liver arylsulfatase A. 4 Jul 16

Ten lysosomal enzyme activities have been compared during the growth and ageing of adult human liver cell lines. Arylsulfatase A, beta-D-galactosidase and beta-D-glucuronidase activities were significantly lower and arylsulfatase B activity was significantly higher in senescent cells than in actively growing cells. Furthermore, hexosaminidase activity was lower and acid phosphatase activity higher in old cells in every cell line tested but the differences were not significant. On the other hand, no change occurred in alpha-L-fucosidase, alpha-D-mannosidase, alpha-D-galactosidase and alpha-D-glucosidase activities. These results demonstrate that the increase in size and number of secondary lysosomes during ageing is accompanied for a few lysosomal enzymes by an increase or a decrease in activity depending on the enzyme.
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PMID:Lysosomal enzyme activities during ageing of adult human liver cell lines. 52 13

Arylsulfatase A purified from human placenta contained an unreported component with an apparent molecular mass of 7 kDa in addition to the two known components with apparent molecular masses of 58 and 50 kDa. The detailed relationship between the 58 kDa component and the 50 kDa component is as yet unknown. The present study was undertaken to define the structure of the subunits of the sulfatase. The N-terminal sequence of the 50 kDa component was identical to that of the 58 kDa component. Furthermore, the peptide maps of the 50 kDa component, which was separately digested with trypsin and Achromobacter proteinase I, were quite similar to those of the 58 kDa one. Through sequence analysis of the incompatible peaks in the peptide maps, the 50 kDa component was found to lack a sequence from Val-445 to the C-terminus. On the other hand, the N-terminal sequence of the 7 kDa component began with Ala-448, though there was a minor sequence commencing with Thr-449. These observations suggest that the 50 and 7 kDa components were produced by limited proteolysis near the C-terminus of the 58 kDa component. Through analysis using unreducing SDS-PAGE, the 58 and the 7 kDa components were found to be linked by disulphide bonds. Arylsulfatase A purified from human liver was also composed of the same subunits as the placental one. This finding suggests that human arylsulfatase A undergoes similar proteolytic processing regardless of the tissue involved.
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PMID:Proteolytic processing of human lysosomal arylsulfatase A. 135 93

Arylsulfatase A (arylsulfatase sulfohydrolase) EC 3.1.6.1 was purified from rat liver by a procedure consisting of differential centrifugation, Con A-Sepharose and Blue Sepharose chromatography, PBE 94 chromatofocusing, DEAE-cellulose and gel filtration chromatography followed by preparative electrophoresis. A molecular mass of 132,000 was estimated by gradient PAGE. Particular proteins were detected by immunoelectrophoresis. Isoelectric focusing combined with immunoelectrophoresis gave two peaks of arylsulfatase A, with isoelectric points of pH 3.9 and 4.5. Microheterogeneity of rat liver arylsulfatase A was studied by affinity immunoelectrophoresis with 9 different lectins. The presence of concanavalin A-, Lens culinaris agglutinin-, Lotus tetragonolobus agglutinin- and wheat germ agglutinin-reactive forms permitted assessment of the types of carbohydrate moieties in arylsulfatase A.
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PMID:Purification of rat liver arylsulfatase A and its microheterogeneity assayed by crossed affinity-immunoelectrophoresis. 136 53

Arylsulfatase A was radioimmunoassayed in serum specimens of 96 healthy volunteers and 368 patients with histopathologically confirmed cancer of gastrointestinal tract, breast, lung, central nervous system, kidney and woman genital tract. Sensitivity, specificity and predictive value of the test were 43%, 82% and 90%, respectively, which means that a positive test is significant for diagnosis of cancer regardless of its localization. More detailed statistical analysis of the results indicates that determination of the serum concentration of arylsulfatase A might be helpful in the diagnosis of lung (59% sensitivity, 82% specificity) and central nervous system cancer (60% sensitivity, 82% specificity). Further studies should also be continued in respect to renal and women genital tract cancers for which the results of the test, although promising, are at present not conclusive due to the small numbers of examined cases. Particularly, determination of serum arylsulfatase A in case of endometrial cancer seems to be of diagnostic value. Arylsulfatase A concentration in serum with a lower than 40% sensitivity of the test cannot be considered as a valuable tumor indicator in the case of cancer of breast and gastrointestinal tract, although 80% predictive value of the test for the latter group of tumors is quite high and perhaps merits additional consideration.
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PMID:Arylsulfatase A in serum from patients with cancer of various organs. 168 88


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