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)

Extracts of the pathogenic ameba Naegleria fowleri, prepared by freeze-thawing and sonication, were analyzed for their content of various hydrolytic enzymes that have acid pH optima. The organism is rich in acid phosphatase activity as well as a variety of glycosidases which include beta-glucosidase, beta-galactosidase, beta-fucosidase, alpha-mannosidase, hexosaminidase, arylsulfatase A, and beta-glucuronidase. The crude extract contained only negligible levels of sphingomyelinase, neuraminidase, or arylsulfatase B. All of the hydrolases exhibited higher activity at pH 5.5 than at 7.0, indicating that they are truly "acid" hydrolases. In general, after centrifugation (100,000 g, 1 h), except for arylsulfatase B, more than half of the activity of each of the various hydrolases was recovered in the supernatant fraction. The acid phosphatase in the high-speed supernatant was purified 45-fold (32% yield) by chromatography on QAE-Sephadex and Sephadex G-200 and shown to have the following properties: pH optima, 5.5; Km (4-methylumbelliferyl phosphate), 0.60 mM; molecular weight (estimated by gel filtration chromatography), 92,000; inhibited by heteropolymolybdate complexes but not by L(+) sodium tartrate (0.5 mM) or sodium fluoride (0.5 mM). In addition, unlike the tartrate-resistant acid phosphatase of Leishmania donovani, the major acid phosphatase of N. fowleri is less than 5% as effective in inhibiting superoxide anion production by f-Met-Leu-Phe-stimulated human neutrophils. The finding of high levels of a number of acid hydrolases in Naegleria fowleri raises several questions that merit further study: Do the hydrolases perform a housekeeping function in this single cell eukaryote or do they play some role in the pathogenic process that ensues when the organism infects a suitable host?
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PMID:Demonstration of various acid hydrolases and preliminary characterization of acid phosphatase in Naegleria fowleri. 301 38

Further clinical heterogeneity of Morquio disease, mucopolysaccharidosis IV (MPS IV), is delineated by the observation of a 30-year-old man with unusually mild clinical manifestations. He is 156 cm tall, has comparatively mild skeletal abnormalities and fine corneal deposits. Keratosulfaturia is absent. N-Acetylgalactosamine-6-sulfate (GalNAc-6-S) sulfatase (E.C. 3.1.6.-) was markedly reduced in his fibroblasts. The residual enzyme activity exhibited a pH profile comparable to that of patients with the "classical" form of the disorder. From our observation and a review of the literature it is concluded that Morquio disease can be divided in several subgroups: besides the severe ("classical") type A there exist an intermediate and a mild form that are also caused by a GalNAc-6-S sulfatase deficiency. A late-onset variant of Morquio disease, which is due to a deficiency of beta-galactosidase, has been classified as type B. In addition, patients with mild manifestation of the disease and normal activities in fibroblasts of GalNAc-6-S sulfatase and beta-galactosidase have been observed (type C). The genetic nature of the broad clinical variability of Morquio disease is incompletely understood: it is partially caused by different enzyme defects. Other factors thought to influence the clinical expression include the pH profile of the residual enzyme activity and an additional neuraminidase defect.
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PMID:Heterogeneity of Morquio disease. 308 64

Assay conditions were studied for eleven lysosomal enzymes (beta-D-galactosidase, alpha-D-mannosidase, beta-hexosaminidase, beta-D-glucuronidase, alpha-D-galactosidase, alpha-D-glucosidase, arylsulfatase, beta-D-glucosidase, alpha-L-fucosidase, alpha-D-neuraminidase and alpha-L-iduronidase) in cultured amniotic fluid cells (CAFC), cultured skin fibroblasts (CSF) and cultured embryonic lung fibroblasts (CELF), and the properties of the enzymes were compared among these cultured cells. In addition, changes in these enzymes from the three cell types were investigated between 4-6 earlier passages and 24-26 later passages. With the exception of alpha-D-glucosidase, alpha-D-neuraminidase and alpha-L-fucosidase, all enzymes assayed for the 4-6 earlier passages and the 24-26 later passages had the same Km values and the same pH optima, and were also unchanged with the increasing age of cell cultures, with regard to their points. The specific activities of beta-D-glucuronidase, arylsulfatase, alpha-D-glucosidase and beta-D-glucosidase for the 4-6 earlier passages increased significantly with development, though no change was observed with development in the specific activities of other enzymes. Variations were observed between the levels of these enzymes in the three cell types with the increasing age of cell cultures, such as increases in some, decreases in others and no change in still others.
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PMID:Comparative enzymology of eleven acid hydrolases in cultured amniotic fluid cells, skin fibroblasts and embryonic lung fibroblasts, and the respective changes with the increasing age of the cell cultures. 316 Dec 15

The activities and properties of arylsulfatase A and B from human lung carcinoma transplanted into athymic mice were demonstrated. The activities of arylsulfatase A and B from transplanted carcinomas with four histological types were more than twofold higher as compared to those from surgical tumors, except for arylsulfatase A activity in blastoma. Arylsulfatase B in transplanted tumors was almost completely replaced, except for blastoma, by an anionic B variant (B1) which was a minor component of arylsulfatase B in surgical lung tumor and absent in normal human lung. The properties of arylsulfatases A and B from transplanted tumors were essentially identical, respectively, with those from normal lung or surgical tumors in respect of molecular weight, heat stability, pH optimum, isoelectric point (pI), Km, time course profile and substrate specificity. Arylsulfatase B1 showed the properties similar to B enzyme except for net charge. The cause of the negative charge of tumor B1 enzyme was investigated. By the action of phosphatase, which was added exogenously or had been persistently included in the partially purified enzyme preparation, B1 enzyme (pI 7.5) shifted to about pI 8.2. Treatment of B1 enzyme with neuraminidase, concomitant with the endogenous phosphatase, resulted in marked increase (pI 9.5) of the isoelectric point, identical to that of arylsulfatase B. Thus, it is most probable that tumor B1 enzyme is modified by additional sialic acid and phosphate bound to arylsulfate B.
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PMID:Arylsulfatases of human-lung tumors transplanted into athymic mice. Cancer-associated modification of arylsulfatase B variant. 611 60

Murine brain possesses an anionic form of arylsulfatase B which accounts for approximately 12-16% of non-microsomal arylsulfatase activity. This isozyme is antigenically similar to cationic arylsulfatase B, displays a similar developmental profile, and can be converted to a form resembling the cationic species by prior treatment with neuraminidase.
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PMID:Comparative studies of murine anionic and cationic arylsulfatase B (1). 612 93

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

Electron-dense material in clear synaptic vesicles in rat cerebral cortex and neuromuscular junctions of frog cutaneous pectoris muscle was demonstrated by using ferrocenyl cationics. Electron-dense spots were usually attached to the inner surface of the vesicular membrane. Control experiments (treatment with Triton X-100 or cetylpyridinium chloride; enzyme digestion with trypsin, hyaluronidase, neuraminidase, sulfatase and beta-glucuronidase) suggested that the electron-dense material is a glycoprotein.
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PMID:Demonstration of electron-dense material in clear synaptic vesicles using cationic ferrocenyl compounds. 633 45

Much of the total genomic variation in eukaryotic organisms may be due to genes other than those coding the primary translation product. Allelic variation, especially as detectable by electrophoresis, in the post-translational processing of enzymes has been briefly reviewed with considerable attention given to a mouse gene (Neu-1) and its pleiotropic effects on several lysosomal hydrolases. Liver acid phosphatase, alpha-mannosidase, arylsulfatase B, and alpha-glucosidase are differentially sialylated as the result of allelic variation for a gene controlling liver neuraminidase activity. Strain SM/J has only 15-20% of the total neuraminidase activity of control strains and is almost totally deficient in the more heat labile of two components of liver activity. The locus controlling this variation (Neu-1) maps very near the D end of H-2 on chromosome 17, apparently within the S region of H-2. A homologous gene has been mapped near the MHC of the rat. The exact nature of the mouse mutant and its relationship to several human diseases characterized by neuraminidase deficiency has not been determined.
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PMID:Post-translational modification of enzymes: processing genes. 635 Feb 18

A deficiency of glycoprotein neuraminidase (sialidase, acylneuraminyl hydrolase, EC 3.2.1.18) activity was found in fibroblasts from a patient with the clinical symptoms of Morquio disease type A (mucopolysaccharidosis IV A). Residual neuraminidase activity was about 5% of the mean normal activity. N-Acetylgalactosamine-6-sulfate (GalNAc-6-S) sulfatase activity was reduced to less than 1% of normal with a pH-optimum of 3.0 as expected for the severe form of Morquio disease. In peripheral leucocytes of the patient, however, neuraminidase activity but not Ga1NAc-6-S sulfatase activity was in the normal range. Mixing experiments excluded the presence of excessive amounts of inhibitors of neuraminidase activity.
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PMID:Partial deficiency of glycoprotein neuraminidase in some patients with Morquio disease type A. 642 47

Arylsulfatase A, B and an anionic form of B were separated by DEAE-cellulose column chromatography from the brains of man, monkey, rabbit, rat and chicken. The relative proportion of brain arylsulfatases differed from one species to the other. The anionic form of arylsulfatase B was a minor component as compared to arylsulfatase A or B in human and monkey brains while it was a major component in rat and chicken brains. Anionic arylsulfatase B was found in fetal human brains and in newborn monkey brain. In the rat brain, the activities of arylsulfatases A and anionic B showed an increasing trend during development, reaching a peak around 20 days after birth, without any change in their proportions. Treatment with Escherichia coli alkaline phosphatase resulted in the conversion of a major portion (about 70%) of the anionic arylsulfatase B of human and monkey brains into a less charged form which remained unbound to DEAE-cellulose. This conversion by phosphatase was inhibited by inorganic phosphate. Rat and chicken brain anionic arylsulfatase B was not susceptible to alkaline phosphatase. Vibrio cholerae neuraminidase treatment did not significantly affect the charge on anionic arylsulfatase B from any of the species. The results suggested a phosphorylated form of anionic arylsulfatase B exclusively in the primate brain.
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PMID:Anionic forms of brain arylsulfatase B: evidence for a phosphorylated form in man and monkey. 668 Jun 91


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