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)

3-Hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase is the key regulatory enzyme for cholesterol biosynthesis. The human gene (HMGCR) has been assigned to the q13.3-q14 region of chromosome 5 (HSA5). We have now mapped the mouse gene Hmgcr to mouse chromosome 13 by Southern analysis of somatic cell hybrids. We also report the mapping to mouse chromosome 13 of the murine homolog of the gene for an intronless beta 2-adrenergic-like receptor, which is also located on human chromosome 5 region q11.2-q13 and has recently been identified as the serotonin 1a receptor. Our results confirm the existence of an evolutionarily conserved syntenic group of genes on the proximal long arm of HSA5 and on MMU13 that also includes the loci for arylsulfatase B, hexosaminidase B and dihydrofolate reductase.
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PMID:Genes for HMG-CoA reductase and serotonin 1a receptor are on mouse chromosome 13. 278 17

Although the arylsulfatase B has been reported to inactivate slow reacting substance of anaphylaxis (SRS-A) in vitro there has not been studied about the relation between this enzyme and nasal allergy in vivo. The present study was done to examine the serum level of arylsulfatase B in 73 nasal allergy patients and 13 normal controls. Serum arylsulfatase activity was quantified by measurement of the hydrolysis product (p-nitrocatechol) generated by the interaction of this enzyme and a substrate (p-nitrocatechol sulfate, Sigma). The results are summarised as follows; 1. Arylsulfatase B activity is significantly elevated in sera of nasal allergy patients than in that of normal subjects. 2. There are no correlation between the enzyme activity and the number of peripheral blood eosinophiles. 3. There is tendency the severe the nasal obstruction, the lower the level of the enzyme activity.
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PMID:[Activity of serum arylsulfatase B in nasal allergy patients]. 280 69

Since a lysosomal arylsulfatase B has been shown to be phosphorylated by a cAMP-dependent protein kinase (cAMP-PK) in transplantable human lung tumor, protein kinase isozymes were investigated in the tumor. Although the kinase of normal human lung comprised both type I and II isozymes at lower level, the tumor kinase was elevated in the activity and occupied almost exclusively by the type II which was responsible for the phosphorylation of arylsulfatase B. The isozyme deviation was also observed in the casein kinase of the tumor with predominance of type II in the tumor in contrast to the coexistence of both types I and II in normal lung.
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PMID:Alterations of protein kinase isozymes in transplantable human lung cancer with special reference to the phosphorylation of arylsulfatase B. 282 63

Primary cultures of retinal pigment epithelial (RPE) cells from cats with mucopolysaccharidosis VI (MPS VI) have been initiated from mixed populations of cells (ie, derived from the entire eyecup and represented by both pigmented and nonpigmented RPE cells). The cells were enzymatically dissociated from the eyecup and seeded at 6 X 10(4) cells/cm2. Cells from normal and affected cats formed confluent monolayers of polygonal cells between 5-10 days in culture and maintained most of their in vivo morphologic characteristics. The only abnormality observed in the MPS VI-affected cultures was the accumulation of vacuolated intracytoplasmic inclusions; when numerous, these vacuoles caused cellular hypertrophy. Hypertrophy was present only in cells devoid of pigment. Pigmented cells adjacent to or near the hypertrophied cells exhibited little or no accumulation of vacuoles. The inclusions were indistinguishable from those observed in vivo in terms of size, distribution, and appearance. The MPS VI-affected RPE exhibited deficient arylsulfatase B (ASB) activity (RPE-ASB activity: normal = 506 nmol/hr/mg protein; affected = 22 nmol/hr/mg protein), whereas the activities of two other lysosomal enzymes, arylsulfatase A and alpha-L-iduronidase, were normal. A method was developed to initiate primary cultures of RPE cells from defined regions of normal and MPS VI-affected eyes. Studies indicated that cultures initiated from superior-equatorial regions (RPE nonpigmented) contained more vacuolated cytoplasmic inclusion than those initiated from inferior-equatorial regions (RPE pigmented). These findings indicated that the spatial distribution characteristic of the disease in vivo was maintained in culture and that disease expression was inversely correlated with pigmentation.
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PMID:Disease expression in cultured pigment epithelium. Feline mucopolysaccharidosis VI. 285 90

Fibroblasts from patients with multiple sulfatase deficiency were analyzed for activities of arylsulfatase A and B, iduronate 2-sulfatase and sulfamatase. A group of patients (group I) severely deficient in all sulfatases (residual activities less than or equal to 10% of control) were differentiated from patients (group II) with residual sulfatase activities of up to 90% of control. The synthesis and stability of arylsulfatase A and B were determined in pulse-chase labelling experiments. The apparent rate of synthesis of arylsulfatase A and B varied from 30% to normal in both fibroblasts from group I and II multiple sulfatase deficiency. In group I the molecular activity of the arylsulfatase A and B was more than 10-fold lower than in control fibroblasts. In group II the molecular activity of the arylsulfatase A was twofold to threefold lower and that of arylsulfatase B half of normal. In fibroblasts of both groups the stability of arylsulfatase A polypeptides was significantly diminished. For arylsulfatase B the instability was restricted to the mature 47000-Mr polypeptide and was variable within both groups. These results demonstrate that multiple sulfatase deficiency is a heterogeneous disorder, in which the primary defects can impair both the catalytic properties and the stability of sulfatases.
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PMID:Synthesis and stability of arylsulfatase A and B in fibroblasts from multiple sulfatase deficiency. 286 38

Multiple sulfatase deficiency can be classified into group I with severe and group II with moderate deficiencies in sulfatases. In fibroblasts in both groups the stability of arylsulfatase A and of the 47000-Mr form of arylsulfatase B is decreased [F. Steckel, A. Hasilik & K. von Figura (1985) Eur. J. Biochem. 151, 141-145]. After endocytosis in control fibroblasts or those from multiple sulfatase deficiency, arylsulfatase A and B derived from the latter were subjected to enhanced degradation in both types of recipient cells. The degradation was closely linked in time to endocytosis. Whereas instability of arylsulfatase A derived from different cell lines from multiple sulfatase deficiency was comparable, a marked heterogeneity was observed for the instability of the 47000-Mr polypeptide of arylsulfatase B. Each of the cell lines from multiple sulfatase deficiency synthesized arylsulfatase A and B polypeptides with normal and with decreased stability. Treatment with benzyloxycarbonyl-Phe-Ala-CHN2, an inhibitor of cysteine proteinases, stabilized arylsulfatase A polypeptides and partially restored arylsulfatase A activity in group II fibroblasts. The inhibitor had no protective effect on the 47000-Mr polypeptide or the activity of arylsulfatase B. The bearing of these findings on the yet unknown primary defect in multiple sulfatase deficiency is discussed.
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PMID:Multiple sulfatase deficiency: degradation of arylsulfatase A and B after endocytosis in fibroblasts. 286 39

Approximately 25 and 40%, respectively, of murine (Mus musculus) and rat (Rattus norvegicus) hepatic arylsulfatase (EC 3.1.6.1) activity eluted from DEAE-ion exchange resins under high salt conditions. This high salt fraction contained arylsulfatase A and an enzyme which was immunologically similar to arylsulfatase B. The latter enzyme was thermostable, resistant to inhibition by silver, completely inhibited by phosphate, displayed linear kinetics, and had a higher pH optimum than arylsulfatase A. Anionic arylsulfatase B also hydrolyzed chondroitin-4-SO4 heptasaccharide. Sephacryl S-300 gel filtration resolved anionic arylsulfatase B into 55 and 115 kd fractions. Rodent arylsulfatase A activity was grossly underestimated when 4-methyl-umbelliferyl sulfate was employed as substrate.
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PMID:Comparative studies of rodent anionic arylsulfatases. 286 44

Rodent and bovine arylsulfatase B hydrolyze 4-methylumbelliferyl sulfate (4MUS) 10- to 30-fold more efficiently than arylsulfatase A. Therefore, 4MUS grossly underestimates arylsulfatase A activity in the presence of excess arylsulfatase B.
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PMID:Mammalian arylsulfatases A and B: relative rates of hydrolysis of artificial substrates. 286 13

Lysosomal arylsulfatases A and B (aryl-sulfate sulfohydrolases, EC 3.1.6.1) from horse leukocytes were purified about 680-fold and 70-fold, respectively, starting from a crude extract of the azurophil and specific granules of leukocytes, by affinity, ion exchange, and gel filtration chromatography. Purified arylsulfatase A displayed anomalous kinetics, a pH optimum at 5.2, an isoelectric point at 4.3, and a Km value for p-nitrocatechol sulfate (pNCS) of 0.37 mM. This enzyme was found to exist in two association states depending on pH: a high molecular weight form at pH 5.0 and a low molecular weight form at pH 7.5. Arylsulfatase B displayed normal kinetics, a pH optimum at 5.8, two isoelectric points at pH 8.6 and 8.9, and a Km value for pNCS of 3.38 mM. The thermostability of the two enzymes was different: arylsulfatase B was found to be more stable than arylsulfatase A. Arylsulfatase A was inhibited by sulfate, sulfite, silver, magnesium, manganese and calcium ions and arylsulfatase B by chloride, sulfate, sulfite and silver ions.
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PMID:Lysosomal arylsulfatases A and B from horse blood leukocytes: purification and physico-chemical properties. 287 81

Ascorbic acid-2-sulfatase was isolated from rat liver by a multistep procedure. DEAE Sephacel ion-exchange chromatography resolved crude ascorbic acid-2-sulfatase into cationic and anionic fractions. These fractions were purified 75- and 230-fold, respectively. The comparative biochemical properties suggest that arylsulfatase B is responsible for the cationic ascorbic acid-2-sulfatase activity, while arylsulfatase A appears to be responsible for the anionic ascorbic acid-2-sulfatase activity. Partially purified arylsulfatase A hydrolyzed ascorbic acid-2-sulfate at 4% the rate of p-nitrocatechol sulfate hydrolysis, while arylsulfatase B hydrolyzed ascorbic acid-2-sulfate at 0.6% the p-nitrocatechol sulfate rate.
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PMID:Isolation and characterization of rat hepatic ascorbic acid-2-sulfatases. 288 99


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