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

---

Query: EC:3.1.6.12 (chondroitinase)
2,183 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
...
PMID:Arylsulfatases of human-lung tumors transplanted into athymic mice. Cancer-associated modification of arylsulfatase B variant. 611 60

To culture retinal pigment epithelial (RPE) cells from normal cats, the cells were enzymatically dissociated from the eyecup and grown in either Ham's F-10 Nutrient Mixture or Eagle's Minimum Essential Media supplemented with 20% fetal calf serum. Cultures reached confluency between 6 and 10 days and contained monolayers of polygonally shaped cells. Light and electron microscopy demonstrated that most of the normal morphological characteristics of cat RPE cells in vivo were maintained in vitro; these included apical microvilli, apicolateral junctional specializations, basal infoldings and intracellular organelles. Pigment granules appeared to be diluted by cell division. No evidence of a basal membrane formation was seen; however, a fine granular or fibrillar extracellular matrix was observed in some cultures and was located between the culture plate surface and the basal surface of the RPE. Primary cultures were viable for up to 145 days. The activities of two lysosomal hydrolases (arylsulfatase A and arylsulfatase B) involved in the metabolism of sulfatide and dermatan sulfate were measured in confluent cultures. Mean arylsulfatase A activity was 1297 nmol nitrocatechol/mg protein/hr and arylsulfatase B activity was 553 nmol nitrocatechol/mg protein/hr. These activities were approximately 5 to 10-fold higher than present in cat peripheral leukocytes and skin fibroblasts in vitro. This in vitro system will facilitate studies on normal function and in conditions where the RPE has been compromised by inherited diseases (i.e. gyrate atrophy, mucopolysaccharidosis I and VI).
...
PMID:Tissue culture of cat retinal pigment epithelium. 613 Sep 61

The effect of ascorbic acid on adrenal and cartilage lysosomal enzyme activity was evaluated in guinea pigs maintained on either 2.4 mg, or 150 mg of ascorbate per day. When compared to adrenal enzyme activities in animals on high dietary levels of ascorbate, the adrenals of animals on 2.4 mg of ascorbate per day expressed 50% increase in the activities of acid phosphatase, arylsulfatase A, and arylsulfatase B (p less than 0.02). In cartilage, the activity of acid phosphatase was significantly elevated in animals on low dietary levels of ascorbate (p less than 0.01), but arylsulfatase A and arylsulfatase B activities were not affected by varying the dietary intake of ascorbate. These data indicate an inverse relationship between tissue vitamin C concentrations and lysosomal enzyme activities.
...
PMID:Effect of ascorbate on lysosomal enzyme activities in guinea pig cartilage and adrenals. 613 Oct 46

Rat liver and Morris hepatoma 7777 arylsulfatase A were isolated from the soluble lysosomal extract by a procedure involving blue-Sepharose affinity chromatography, DEAE-cellulose chromatography, hydrophobic chromatography on phenyl-Sepharose and preparative polyacrylamide gel electrophoresis. The preparation obtained by this method was apparently homogenous in disc electrophoresis and in immunoelectrophoresis. The comparative studies revealed that the properties of arylsulfatase A from rat liver and Morris hepatoma 7777 are very similar, considering molecular weight of the native monomer and its subunits, the ability to form tetramers, isoelectric point, Michaelis constant and the anomalous kinetics of the reaction. The twofold elevation of arylsulfatase B activity found in Morris hepatoma 7777 suggests that the enzyme may have certain functions in tumor growth.
...
PMID:Isolation and comparison of arylsulfatase A from rat liver and Morris hepatoma 7777. 613 61

A staining reaction was developed to specifically detect arylsulfatase A activity in the presence of arylsulfatases B and C. Nitrocatechol, generated by all arylsulfatases from the substrate p-nitrocatechol sulfate, can be coupled to produce Hatchett 's brown which reacts with 3,3'-diaminobenzidine to yield an osmiophilic polymer visible under the electron microscope. The reaction was made specific for arylsulfatase A by inhibiting arylsulfatase C activity with low pH and arylsulfatase B activity with pyrophosphate. The specificity was confirmed both by electrophoretic analysis and by patient fibroblasts deficient only in arylsulfatase A activity. Under optimal conditions for preserving structural integrity and enzyme activity, enzyme reaction deposits were found mainly around vesicles. Some of these vesicles were large and heterogeneous (48-330 nm in diameter), distributed randomly within the cytoplasm, but most of the positive-reacting vesicles were uniform in size (86 +/- 18 nm in diameter) and distributed in a peripheral zone about 0.1-0.5 micron wide. These periplasmic vesicles might be partly fused with each other or with the plasma membrane. In conclusion, a specific stain for arylsulfatase A activity suitable for light and electron microscopy and the optimal conditions for structural and enzymatic preservations were developed. Although this enzyme has been considered to be lysosomal in origin, most of the activity was detected in periplasmic vesicles near the cell surface.
...
PMID:A specific ultrastructural stain for arylsulfatase A activity in human cultured fibroblasts. 620 36

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.
...
PMID:Anionic forms of brain arylsulfatase B: evidence for a phosphorylated form in man and monkey. 668 Jun 91

Arylsulfatases A and B were measured in the liver of mice infected with Schistosoma mansoni. The increase of total arylsulfatases paralleled enlargement of the granulomas. It began at 7 weeks after infection and reached a maximum at 10 to 14 weeks when the enzyme activity became about 2.5 times that of normal liver. The elevated enzyme activity was due to granulomatous tissue, because when granulomas were separated from hepatic cells, the former contained the increased activity but the latter did not. Arylsulfatase A, arylsulfatase B, and arylsulfatase Bv, in both normal liver and granulomas, were separated by anion-exchange column chromatography and differences in net charges of these enzymes were demonstrated by polyacrylamide gel electrophoresis. Biochemical properties were indistinguishable between arylsulfatase B and arylsulfatase Bv while they differed from arylsulfatase A. Granulomas at 8 weeks after infection showed 3.0-, 3.5-, and 5.0-fold increases in activity for arylsulfatase A, B, and Bv, respectively. As the granulomas enlarged, by 12 weeks, arylsulfatases B and Bv activities further increased but the arylsulfatase A value remained the same as that of 8 weeks. The finding suggests that arylsulfatases are involved in granuloma development and arylsulfatases B and Bv activities may reflect functions of macrophages and other cells including fibroblasts.
...
PMID:Biochemical characterization of arylsulfatases detected in granulomatous inflammation. 669 6

Arylsulfatases A and B were measured in the stratum corneum of four normal controls and two individuals with sex-linked ichthyosis. For arylsulfatase A, the mean delta optical density/hr/mg protein value was 1.6 for controls and 2.0 for patients, whereas for arylsulfatase B values of 1.5 for controls and 1.4 for patients were observed. Assay of arylsulfatase C in the callus of four normal controls showed a mean delta optical density/hr/100 mg callus of 0.63, whereas no or trace activity was detected in callus from four patients with x-linked ichthyosis. The assay of steroid sulfatase is best for studying microsomal sulfatase activity. Table 1 shows the activity of this enzyme in nails, callus, and hair bulbs from controls and patients with x-linked ichthyosis. No steroid sulfatase could be demonstrated in patients with x-linked ichthyosis. The values in normal controls and obligate heterozygotes are compared in Table 2. The mean value of the two groups is statistically different with P less than or equal to 0.05 using the Student t test.
...
PMID:Sulfatase activity of keratinizing tissues in X-linked ichthyosis. 720 52

Various sulfatase activities were assayed in cultured skin fibroblasts from patients with multiple sulfatase deficiency (MSD). MSD cell lines displayed deficiencies of arylsulfatase A and iduronate sulfatase, but activities of arylsulfatase B, N-acetylgalactosamine 6-sulfate sulfatase and N-acetylglucosamine 6-sulfate sulfatase were within normal ranges, but not consistently. Arylsulfatase A, minor anionic arylsulfatase and N-acetylgalactosamine 6-sulfate sulfatase in MSD cell lines had similar Km, pH optima, inhibitory or activator sensitivity to that of normal skin fibroblasts. Arylsulfatase B in MSD cell lines also had properties similar to that of normal skin fibroblasts, except an abnormal heat stability. From our results, we conclude that properties of arylsulfatase A, minor anionic arylsulfatase and N-acetylgalactosamine 6-sulfate sulfatase in MSD fibroblasts were intact. On the other hand, arylsulfatase B in MSD might be a functionally abnormal enzyme.
...
PMID:Properties of sulfatases in cultured skin fibroblasts of multiple sulfatase deficient patients. 733 23

The activities of arylsulfatases A and B were determined in human primary and secondary tumor tissues (total, 53 cases) of various histological types. Significantly higher activities of these sulfatases were found in almost all the primary lung carcinomas as compared to their corresponding uninvolved tissues. No significant correlation was demonstrated between the enzyme activities and histological figures (stroma amounts, etc.). Lung adenocarcinoma and squamous cell carcinoma showed the presence of an additional arylsulfatase component (B1) which was not detected in normal human lung. The tumor arylsulfatase B1 had an isoelectric point (pI) of 6.7 and was clearly distinguished from arylsulfatase A (pI 4.9) and arylsulfatase B (pI 9.1 to 9.2) in normal lung and lung tumor. The tumor B1 enzyme was demonstrated to be most probably an isoenzyme of arylsulfatase B, since this unusual enzyme was indistinguishable from arylsulfatase B in terms of Ag+ inhibition; its kinetic parameters of Km for p-nitrocatechol sulfate, which was 2.9 mM with B1; optimum pH of 6.3 for B1; heat stability; and substrate specificity for three synthetic and two physiological substrates.
...
PMID:Elevated activities and properties of arylsulfatases A and B and B-variant in human lung tumors. 743 63


<< Previous 1 2 3 4 5 6 Next >>

---