Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.6.12 (chondroitinase)
 2,183 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:A specific ultrastructural stain for arylsulfatase A activity in human cultured fibroblasts. 620 36

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.
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PMID:Sulfatase activity of keratinizing tissues in X-linked ichthyosis. 720 52

In the present study estrone sulfatase (steryl-sulfatase; EC 3.1.6.2) and phenylsulfatase (arylsulfatase B; EC 3.1.6.1) inhibiting as well as antioxidant effects exerted by ring B,C unsaturated sulfamates of estrone (J 1025), 17 beta-estradiol (J 1054, J 1059, J 1067), and 17 alpha-estradiol (J 1051, J 1064, J 1065) were examined as compared with their parent compounds, J 994, J 995, and J 1050, using six different in vitro models: (i) estrone sulfatase activity in human placental microsomes, (ii) phenylsulfatase activity isolated from Helix pomatia, (iii) Fenton reaction driven lipid peroxidation in rat synaptosomes, (iv) Fe(II)-chelating activities, (v) formation of superoxide anion radicals, and (vi) total antioxidative activities. Ring B,C unsaturated estrogen (so-called scavestrogen) sulfamates were found to act as potent inhibitors of the following enzyme activities and generated radicals: estrone sulfatase, phenylsulfatase, lipid peroxyl, and superoxide anion. In addition, scavestrogen sulfamates were able to influence the iron redox chemistry and total antioxidative activities. These findings indicate that relatively minor modifications in the chemical structure of classical steroid sulfamates can preserve or enhance their estrone sulfatase inhibiting properties and, simultaneously, amplify their antioxidant capacity to a great extent. Taken together, our data suggest that scavestrogen sulfamates such as J 1025, J 1051, or J 1054 (17 beta-dihydroequilenin sulfamate) may serve as a very promising basis for the development of steroid-derived estrone sulfate-sulfatase inhibitors characterized by promising estrone sulfatase inhibiting activities in combination with a "good" antioxidant potency.
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PMID:Scavestrogen sulfamates: correlation between estrone sulfatase inhibiting and antioxidant effects. 963 47

Multiple sulfatase deficiency (MSD) is an inborn error of metabolism that combines the clinical features of late infantile metachromatic leukodystrophy and mucopolysaccharidosis. The characteristic biochemical abnormality is a reduction in the activities of several sulfatases, with consequent tissue accumulation of sulfatides, sulfated glycosaminoglycans, sphingolipids, and steroid sulfates. In this study we present two unusual cases of MSD with variable enzymatic deficiency of arylsulfatases A, B, and C. Both patients had ichthyosis, broad thumbs and index fingers, an unusually slow progression of the neurologic symptoms, and lacked the hepatosplenomegaly that is typical of MSD. Olivopontocerebellar atrophy was present and one patient had a large retrocerebellar cyst. Mucopolysaccharides were not detected in the urine from either subject. Leukocyte arylsulfatase A activity in patient 1 was 0.46 nmol/mg protein/hr and in patient 2 was 0.0 nmol/mg protein/hr (normal 0.7-5.0 nmol/mg protein/hr). Leukocyte arylsulfatase B activity in patient 1 was 24 nmol/mg protein/hr and in patient 2 was 22 nmol/mg protein/hr (normal 115-226 nmol/mg protein/hr). Leukocyte arylsulfatase C in patient 1 was 0.30 pmol/mg protein/hr and in patient 2 was 0.28 pmol/mg protein/hr (normal 0.84 pmol/mg protein/hr). In conclusion, these two patients with MSD had mild clinical presentations not previously reported and variable enzymatic deficiency of arylsulfatases A, B, and C.
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PMID:Unusual clinical presentation in two cases of multiple sulfatase deficiency. 1173 81

Sulfatase enzymes have important roles in metabolism of steroid hormones and of glycosaminoglycans (GAGs). The activity of five sulfatase enzymes, including steroid sulfatase (STS; arylsulfatase C), arylsulfatase A (ASA; cerebroside sulfatase), arylsulfatase B (ASB; N-acetylgalactosamine-4-sulfatase), galactose-6-sulfatase (GALNS), and iduronate-2-sulfatase (IDS), was compared in six different mammary cell lines, including the malignant mammary cell lines MCF7, T47D, and HCC1937, the MCF10A cell line which is associated with fibrocystic disease, and in primary epithelial and myoepithelial cell lines established from reduction mammoplasty. The effects of estrogen hormones, including estrone, estradiol, estrone 3-sulfate, and estradiol sulfate on activity of these sulfatases were determined. The malignant cell lines MCF7 and T47D had markedly less activity of STS, ASB, ASA, and GAL6S, but not IDS. The primary myoepithelial cells had highest activity of STS and ASB, and the normal epithelial cells had highest activity of GALNS and ASA. Greater declines in sulfatase activity occurred in response to estrone and estradiol than sulfated estrogens. The study findings demonstrated marked variation in sulfatase activity and in effects of exogenous estrogens on sulfatase activity among the different mammary cell types.
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PMID:Steroid sulfatase, arylsulfatases A and B, galactose-6-sulfatase, and iduronate sulfatase in mammary cells and effects of sulfated and non-sulfated estrogens on sulfatase activity. 1706 91