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 contractile effects of partially purified slow-reacting substance of anaphylaxis (SRS-A) and histamine were compared on isolated guinea pig tracheal spirals and parenchymal strips. Histamine was equally active on both isolated tissues in a concentration-related fashion. SRS-A (0.1--10.0 U/ml) produced a concentration-related effect on parenchymal strips, whereas the tracheal spiral was 100 times less sensitive to this mediator. The contractile activity of SRS-A on parenchymal strips was diminished by incubation with limpet arylsulfatase and antagonized by FPL 55712, a known SRS-A antagonist. SRS-A, further purified by high pressure liquid chromatography, also demonstrated this preferential activity on guinea pig parenchymal strips. These data are consistent with the hypothesis, based on previous in vivo observations, that SRS-A is a selective peripheral airway constrictor.
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PMID:Differential effects of a partially purified preparation of slow-reacting substance of anaphylaxis on guinea pig tracheal spirals and parenchymal strips. 76 39

Arylsulfatase activity has been studied in the developing molar of the Swiss albino mouse from the lamina stage to the appositional stage. Timed-pregnant Swiss albino mice were utilized in this study. Females were sacrificed by ether anesthesia and fetuses extirpated or newborns anesthetized and decapitated. Frozen sections were fixed and incubated for arylsulfatase activity according to a modification of the method of PEARSE (1972). The tissue was dehydrated, cleared and covered. Phase light microscopy was utilized in evaluating arylsulfatase activity in the developing molar. Arylsulfatase activity was evaluated for each stage of development and the results presented in tabular form. The present investigation represents the first known effort to describe arylsulfatase activity in odontogenic tissues from the initiation of the dental lamina through the appositional stage. Arylsulfatase activity appeared to be related to the degree of vascularization of the developing enamel organ and adnexa and the beginning of hard tissue elaboration.
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PMID:Aryl sulfatase activity in mouse molar odontogenesis. 82 69

The participation of tyramine oxidase in the regulation of arylsulfatase synthesis in Klebsiella aerogenes was studied. Arylsulfatase was synthesized when this organism was grown with methionine or taurine as the sulfur source (nonrepressing conditions) and was repressed by inorganic sulfate or cysteine; this repression was relieved by tyramine and related compounds (derepressing conditions). Under nonrepressing conditions, arylsulfatase synthesis was not regulated by tyramine oxidase synthesis. However, derepression of arylsulfatase and induction of tyramine oxidase synthesis by tyramine were both antagonized by glucose and other carbohydrate compounds. The derepressed synthesis of arylsulfatase, like that of tyramine oxidase, was released from catabolite repression by use of tyramine as the sole source of nitrogen. A mutant strain that exhibits constitutive synthesis of glutamine synthetase and high levels of histidase when grown in glucose-ammonium medium was subject to the catabolite repression of both tyramine oxidase and arylsulfatase syntheses. Mutants in which repression of arylsulfatase could not be relieved by tyramine could not utilize tyramine as the sole source of nitrogen and were defective in the gene for tyramine oxidase.
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PMID:Tyramine oxidase and regulation of arylsulfatase synthesis in Klebsiella aerogenes. 83 Jun 48

It was shown that at least four genes are specifically responsible for arylsulfatase synthesis in Klebsiella aerogenes. Mutations at chromosome site atsA result in enzymatically inactive arylsulfatase. Mutants showing constitutive synthesis of arylsulfatase (atsR) were isolated by using inorganic sulfate or cysteine as the sulfur source. Another mutation in which repression of arylsulfatase by inorganic sulfate or cysteine could not be relieved by tyramine was determined by genetic analysis to be on the tyramine oxidase gene (tyn). This site was distinguished from the atsC mutation site, which is probably concerned with the action or synthesis of corepressors of arylsulfatase synthesis. Genetic analysis with transducing phage PW52 showed that the order of mutation sites was atsC-atsR-atsA-tynA-tynB. On the basis of these results and previous physiological findings, we propose a new model for regulation of arylsulfatase synthesis.
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PMID:Genetic control of arylsulfatase synthesis in Klebsiella aerogenes. 85 36

A serine auxotroph of Neurospora requires exogenous serine to repress the arylsulfatase, suggesting that this enzyme is repressed by cysteine and not by methionine.
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PMID:Control of arylsulfatase in a serine auxotroph of Neurospora. 86 61

The distribution of soluble arylsulfatase (aryl-sulfate sulfohydrolases, EC 3.1.6.1) in human tissues was investigated by DEAE-cellulose chromatography, All tissues examined contained arylsulfatase A and arylsulfatase B. In addition, brain singularly contained significant quantities (15-25% of total arylsulfatase) of a minor anionic arylsulfatase from designated arylsulfatase Bm, whereas only trace amounts of arylsulfatase Bm were found in liver, kidney, testis and placenta. Arylsulfatase B and arylsulfatase Bm had equal activity toward methyl-umbelliferyl sulfate, nitrocatechol sulfate and a physiological substrate UDP-N-acetylgalactosamine 4-sulfate, but both forms were inactive toward the arylsulfatase A substrates cerebroside sulfate and ascorbic acid 2-sulfate. Purified preparations of placental arylsulfatase B, brain arylsulfatase Bm, and urinary arylsulfatase A did not hydrolyze estrone sulfate, dehydroepiandrosterone sulfate or pregnenolone sulfate. The physico-chemical properties of arylsulfatase Band arylsulfatase Bm differed with respect to thermal lability, DEAE-cellulose chromatography, polyacrylamide gel electrophoresis and isoelectric focussing. In the latter technique, utilizing thin polyacrylamide slab gels, the isoelectric point for placental arylsulfatase B was 8.2, while brain arylsulfatase Bm resolved into 3 activity bands with pI values 6.8, 7.0 and 7.2. Although the physico-chemical properties differed, arylsulfatase B and arylsulfatase Bm appear to be functionally equivalent as well as generically related.
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PMID:Arylsulfatase of human tissue. Studies on a form of arylsulfatase B found predominantly in brain. 87 49

5-Flourouracil (5-FU) and methyl-CCNU have demonstrated separate sensitivities in carcinoma of the large bowel. This study was an attempt to see if methyl-CCNU versus methyl-CCNU plus 5-FU would demonstrate different responses in advanced colorectal carcinoma. Forty-nine patients have been evaluated, 14 receiving methyl-CCNU and 35 receiving 5-FU plus methyl-CCNU. One partial response has been seen with methyl-CCNU alone in a patient with liver metastasis. Thirteen partial responses have been noted in patients treated with the two-drug combination. There was a significant difference in the median survival of the responders versus the nonresponders for the two-drug group. Side effects were expected: nausea and vomiting, leukopenia, and thrombocytopenia. Plasma carcinoembryonic antigen and urine arylsulfatase were measured in all patients and correlated well with response.
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PMID:Methyl-CCNU versus methyl-CCNU and 5-fluorouracil in carcinoma of the large bowel. 92 50

The activities of four lysosomal acid hydrolases (LAH) in the lungs of two strains of mice changed significantly throughout the life cycle. In the CK7B1/6J animals, acid phosphatase (AP) and beta-glucuronidase (beta-G) were maximally active during early neonatal life then gradually declined the adult levels by 4-5 weeks of age. After reaching the adult level, acid phosphatase activities did not change significantly tcreased markedly with advanced age. N-Acetyl-beta-D-glucosaminidase (GAD) activities did not change significantly duringlate fetal, neonatal or young adult stages but increased significantly with advancing age. In the lungs of the CFW animals, the increase in activities of beta-G and GAD between young adult life and advanced age was highly significant, whereas there was no notable change in the activities of acid phosphatase or arylsulfatase (AS). The specific activities of the hydrolases in the lungs of the C57B1/6J strain were quite similar to those in the lungs of the CFW strain. The activities of all four hydrolases were markedly elevated in two spontaneous adenomatous tumors found in the lungs of old mice. The data indicate that LAH play a significant role in lung growth and maturation, and in changes associated with aging.
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PMID:Lysosomal acid hydrolase activities in the lungs of fetal, neonatal, adult, and senile mice. 95 22

Extracts of isolated rat peritoneal mast cells were demonstrated to contain appreciable quantities of arysulfatase activity. The enzyme was inhibited by both phosphate and sulfate ions and demonstrated a pH optimum of 5.0. The enzyme was recovered in the eluate of DE-52 columns and appeared to have a m.w. of 150,000 of Sephadex G-200 gel filtration. These findings and the anomalous kinetic behavior of the enzyme suggest that at least part of the enzymatic activity is of the arylsulfatase IIA type. While spontaneous release of the enzyme was observed, challenge of isolated rat mast cells with a goat anti-rat IgE serum resulted in a significant increase in release of the enzyme. The arylsulfatase activity extracted from isolated rat mast cells demonstrated comparable activity in inactivating slow reacting substance of anaphylaxis (SRS-A) to that described for human eosinophil and lung arylsulfatase.
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PMID:Functional characterization of rat mast cell arylsulfatase activity. 99 97

BALB/c male mice possess twofold higher kidney p-nitrocatechol-SO4 arylsulfatase B than do A/HeJ male mice; however, their liver arylsulfatase activities are comparable. Twentyfold-purified kidney arylsulfatases B from these two strains have similar Michaelis constants, electrophoretic mobilities, pH optima, and inhibitor profiles; however, the BALB/c enzyme is more heat stable than the A/HeJ enzyme. BALB/c, C3H/HeJ, DBA/2J, and SWR/J mice share an autosomal allele, As-1a, which apparently determines the heat-stable arylsulfatase B, while A/HeJ and C57BL/6J mice possess the As-1b allele, which determines the heat-sensitive enzyme. A second autosomal locus, Asr-1, determines liver arylsulfatase B activity. C57BL/6J mice carry the Asr-1a allele, which results in high liver activities, while C3H/HeJ mice are homozygous for the low-activity allele, Asr-1b. Male mice generally have 30-40% higher kidney activities than females; however, female kidney arylsulfatase activities rise and actually surpass those of males during late pregnancy and lactation.
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PMID:Genetic control of heat sensitivity and activity level of murine arylsulfatase B. 101 19


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