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)

Electron cytochemical localizations of acid phosphatase, aryl sulfatase, deoxyribonuclease, adenylate cyclase, and c-AMP phosphodiesterase activity sites in thin sections of cells of the two growth phases of the zoopathogenic Histoplasma capsulatum are described and illustrated by transmission electron micrographs. Various activity sites of these enzymes included the cytomembranes of the nucleus, mitochondria, and endoplasmic reticulum. At the same time, electron opaque reaction products were sequestered within membrane-bound, vacuolar regions of the cytosol. These vacuoles may be ontogenically related to membranous or vesicular inclusions commonly seen in thin sections of glutaraldehyde osmium tetroxide-fixed cells. These enzymatically-active vacuoles are believed consistent with previous descriptions of fungal lysosomal-like structures found in certain other fungi. Lysosomal-like vacuoles of H. capsulatum may provide a means of compartmentalization of various hydrolytic enzymes involved in catabolism and mobilization of storage reserves, and perhaps to function as well in other aspects of the life cycle of this important pathogenic dimorphic fungus.
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PMID:Electron cytochemical evidence for lysosomal-like equivalents in Histoplasma capsulatum. 626 Nov 31

This report describes a third mucopolysaccharidosis in animals: canine mucopolysaccharidosis VII. The affected dog was the offspring of a father-daughter mating. Weakness in the rear legs was evident at 8 weeks of age and became progressively worse. He had a large head, a shortened maxilla, and corneal granularities. Most joints were extremely lax, easily subluxated, with joint capsules that were swollen and fluctuant. The dog was alert and had apparently normal pain perception. At 13 months of age, there was radiographic evidence of extensive skeletal disease including bilateral femoral head luxation, abnormalities in the shape and density of the carpal and tarsal bones, radiolucent lesions of the epiphyseal regions of most long bones, and cervical vertebral dysplasia and platyspondylia. The electrophoretic pattern of precipitated glycosaminoglycans indicated a predominance of chondroitin sulfate. The animal died suddenly from gastric dilatation. There was generalized hepatomegaly, thickening of the atrioventricular heart valves, and generalized polyarthropathy. Vacuolated cytoplasm was observed in hepatocytes, keratocytes, fibroblasts, chondrocytes and cells of the synovial membrane, retinal pigment epithelium, and cardiac valves. Neurons had cytoplasmic vacuoles. Electron microscopy demonstrated membrane-bound cytoplasmic inclusions in polymorphonuclear leukocytes, hepatocytes, synovium, heart valves and spleen. The activities of 12 lysosomal hydrolases were determined in liver from the affected and control dogs: beta-glucuronidase (EC 3.2.1.31), beta-hexosaminidases A and B (EC 3.2.1.30), alpha-hexosaminidase (EC 3.2.1.-), alpha-L-iduronidase (EC 3.2.1.76), alpha-galactosidase A (EC 3.2.1.22), beta-galactosidase (EC 3.2.1.23), arylsulfatases A and B (EC 3.1.6.1), acid alpha-mannosidase (EC 3.2.1.24), acid beta-mannosidase (EC 3.2.1.25), and N-acetyl-D-galactosamine-6-sulfate sulfatase (EC 3.1.6.-).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Beta-glucuronidase deficiency in a dog: a model of human mucopolysaccharidosis VII. 643 80

The activity of the two membrane-bound sulfatases, estrone and dehydroepiandrosterone sulfatases, are reported in human breast carcinoma tissues. In 21 tested tumors (12 from post-menopausal women and 9 from nonmenopausal women), the two sulfatases were consistently present. The apparent Km values for estrone and dehydroepiandrosterone sulfatases were, respectively, 6.8 and 14.9 microM. In terms of maximal velocity, the sulfatase activities are not correlated to the estrogen or progesterone receptor status of the tumors or to the hormonal status of the donors. It may be concluded that these two activities are not hormone dependent. Estrone sulfate, the substrate of estrone sulfatase, has been measured in plasma of postmenopausal women. The mean levels (nmol/liter) of plasma estrone sulfate were compared in post-menopausal women with (n = 51) or without (n = 39) breast cancer. For the first age group (48 to 55 years old), no statistically significant difference in these levels was observed [1.91 +/- 1.06 versus 1.50 +/- 1.04 (mean +/- t0.95 (Formula: see text) S.E.)]. For the two other age groups (56 to 65 and 66 to 80 years of age), the differences were statistically significant [1.46 +/- 0.43 versus 0.77 +/- 0.21 (p less than 0.02) and 1.77 +/- 0.53 versus 0.81 +/- 0.22 (p less than 0.01)]. The usefulness of plasma estrone 3-sulfate levels as an indicator of the real estrogen status of postmenopausal women is discussed.
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PMID:Estrone and dehydroepiandrosterone sulfatase activities and plasma estrone sulfate levels in human breast carcinoma. 658 63

Human placental steroid-sulfatase was extracted nearly quantitatively from microsomes as well as from acetone dry powder of placenta homogenates using CHAPS as detergent. The solubilized enzyme was enriched 10-fold by ammonium sulfate precipitation and gel chromatography. The sulfatase extracted from both microsomes and acetone dry powder eluted as a single fraction on Sepharose 6B, but with different apparent molecular masses (390 and 270 kDa, respectively). Kinetic experiments with the sulfate esters of dehydroepiandrosterone, 16 alpha-hydroxydehydroepiandrosterone, estrone, and estriol as substrates or inhibitors indicated that the solubilized sulfatase was fully active. Both the particulate and the extracted enzyme showed higher affinities for the 16-unsubstituted than for the 16 alpha-hydroxylated substrates. Whereas a competitive inhibition was observed in mixed substrate incubations with dehydroepiandrosterone sulfate/16 alpha-hydroxydehydroepiandrosterone sulfate and estrone sulfate/estriol sulfate, diverse patterns of inhibition were obtained with dehydroepiandrosterone sulfate/estrone sulfate, depending on the sulfatase preparation used. However, evidence for the distinct nature of the steroid-sulfatase and the estrogen-sulfatase was not obtained. The membrane-bound, but not the solubilized enzyme was to a certain degree sensitive to lipase and acetone. The solubilized sulfatase strongly bound to ConA-Sepharose. This observation together with the elution by alpha-methyl mannoside were indicative of the presence of carbohydrates on the sulfatase. Since its enzymatic activity was markedly decreased by the effects of alpha-mannosidase and N-acetylglucosaminidase, a possible involvement of the carbohydrate moiety in the catalytic activity of the sulfatase might be considered.
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PMID:Human placental steroid-sulfatase solubilized with a cholic-acid derivative: molecular mass, kinetic properties and susceptibility to glycosidases. 205 96

The epithelium of caput and cauda epididymidis of the rat was studied with transmission electron microscopy (TEM) and freeze-fracture techniques. In thin sections of both zones, the tissue consisted mainly of tall columnar cells (principal cells) with long sterocilia. Clusters of small membrane-bound vesicles were located in the lumen between or immediately over the stereocilia. Freeze-fracture replicas also displayed groups of smooth-surface vesicles in the same location. Membrane-bound vesicles isolated from the lumen of the rat epididymis were studied by TEM. In thin sections, some of them contained an electron dense material and others looked empty. In addition, the hydrolases: beta-galactosidase, N-acetyl-glycosaminidase, alpha-mannosidase, aryl-sulfatase and beta-glucuronidase were detectable in pellets of vesicles treated with Triton X-100. The results presented here indicate the presence of membrane-bound vesicles observed by two different methodologies in the rat epididymal fluid and demonstrate five glycosidases in their content.
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PMID:Morphological and enzymatic study of membrane-bound vesicles from the lumen of the rat epididymis. 775 84

Accumulation of sulfolipids associated with markedly elevated levels of glycolipid sulfotransferase activities was previously demonstrated in human renal cell carcinoma cells. To explore the regulation mechanisms of sulfoglycolipid synthesis in renal cancer, effects of various growth factors on the metabolic enzymes of sulfoglycolipids were investigated by using a human renal cell carcinoma cell line, SMKT-R3. Among the growth factors tested, transforming growth factor alpha (TGF-alpha) and epidermal growth factor (EGF) were found to increase the sulfotransferase activity markedly (about 300%), but did not change that of arylsulfatase A, which hydrolyzes sulfoglycolipids. The augmented effects of TGF-alpha was abolished by cycloheximide. Since TGF-alpha is known to bind to the same receptor as EGF, SMKT-R3 cells were investigated for the EGF receptor by affinity cross-linking with 125I-EGF. A radiolabeled protein with a molecular mass of 175 kDa corresponding to the ligand-receptor complex was immunoprecipitated with a monoclonal anti-EGF receptor antibody. When production of the growth factors was examined immunochemically, the cells were found to secrete TGF-alpha at a low level and retain it in a membrane-bound form, whereas EGF was not detected. These observations suggest that the sulfotransferase activities are regulated through the autocrine, paracrine, and/or juxtacrine modes of intercellular stimulation by TGF-alpha in human renal cancer cells.
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PMID:Regulation of activity levels of glycolipid sulfotransferases by transforming growth factor alpha in renal cell carcinoma cells. 790 7

Localization of steroid sulfatase, a membrane-bound microsomal enzyme, in human fallopian tubes was immunohistochemically investigated, and expression of RNA was confirmed by competitive RT-PCR. Human fallopian tubes were obtained from 10 patients in follicular and early luteal phases during gynecological laparotomy. An anti-human rabbit polyclonal antibody was prepared against sulfatase protein purified from human placenta. Total RNA was isolated from epithelium of fallopian tubes. A heterologous RNA competitor was designed, and competitive RT-PCR was carried out. Steroid sulfatase was localized to the cytoplasm of epithelial cells. With respect to the positive staining of cells, the number of positive secretory cells was higher than that of ciliated cells. A significantly higher number of positive cells was found in tissue obtained from the early luteal phase than that found in tissue from the follicular phase. An abundant expression of sulfatase mRNA in early luteal phase was also observed. This study demonstrates, for the first time, that steroid sulfatase is localized to human epithelial cells and that steroid sulfatase staining and mRNA expression changes with the menstrual cycle. These results suggest that sulfatase in the fallopian tube may be involved in controlling the local steroid environment, which appears to regulate aspects of the physiological reproductive function of the fallopian tube.
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PMID:Localization and expression of steroid sulfatase in human fallopian tubes. 1114 87

Saposin B (also known as cerebroside sulfate activator or CSAct) is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulfates (sulfatides) in lysosomes. Saposin B contains three intramolecular disulfide bridges, exists as a dimer and is remarkably heat, protease, and pH stable. We have expressed the protein in a thioredoxin reductase deficient strain of Escherichia coli and purified the protein by heat treatment, followed by ion-exchange, gel filtration, and hydrophobic interaction chromatographies. The protein is properly folded as judged by the observed disulfide bond topology, the hydrogen-deuterium exchange rate, and the level of stimulation of sulfatide hydrolysis by arylsulfatase A. Crystals of human saposin B were grown by vapor diffusion and diffract to a resolution of 2.2A. Despite obtaining only merohedrally twinned P3(1) native crystals, an untwined seleomethionine-substituted crystal belonging to space group P3(1)21 was also grown. The three-dimensional structure of saposin B protein will provide insights into how this 79 amino acid protein is able to solubilize relatively large membrane-bound lipid ligands.
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PMID:Expression, purification, crystallization, and preliminary X-ray analysis of recombinant human saposin B. 1251 3

Steroid sulfatase (STS) is a membrane-bound microsomal enzyme that hydrolyzes various alkyl and aryl steroid sulfates, leading to the in situ formation of biologically active hormones. The entire human STS gene spans over approximately 200kbp of which the first 100kbp include the regulatory region, while the STS-coding region is located downstream. Previous studies indicated that STS expression, in different human tissues, could be regulated by at least six different promoters associated with alternative first exons. Here, we describe two new splicing patterns: the first, found in the prostatic cell line PC3, is based upon a partially coding new first exon (0d) that is spliced to a new second exon (1e). The second variant was found in the ovary and it is characterized by the novel splicing of the untranslated exon 0b to exon 0c, which is then spliced to the common exon 1b. We also report the results of a multiplex ligation-dependent probe amplification (RT-MLPA) analysis for the simultaneous detection, in qualitative and/or semi-quantitative terms, of the transcription patterns of STS in different tissues.
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PMID:Transcriptional control of human steroid sulfatase. 1942 62

Sea urchin petalloid coelomocytes effectuate the clotting pathway by undergoing a rapid and dynamic cellular transformation that leads to cellular adhesion and wounds closure. We have identified high levels of activity of arylsulfatase (Ars) associated with coelomocytes of the sea urchin Lytechinus variegatus (Lamarck, 1816). Ars activity was extracted from clotted coelomocytes with EDTA and showed high levels of activity up to a 1:100 dilution. Clot formation from isolated coelomic fluid was significantly inhibited by the ARS inhibitor, p-nitrophenyl phosphate. Ars activity was collected by 80% ethanol precipitation, a diagnostic test previously used in Ars isolation. Cellular extraction studies in the presence and absence of the non-ionic detergent Triton X-100 indicated that some Ars activity was present intracellularly, possibly in intracellular membrane-bound compartments, however the majority of Ars activity was extracted from the extracellular coelomocyte membrane. Polyclonal anti-sea urchin embryo Ars antibodies recognized a single protein band with an approximate molecular weight of 75 kDa on western blots. Immunofluorescence using the anti-sea urchin Ars antibody revealed an intracellular and extracellular staining of Ars in both petalloid and filopodial coelomocytes. Taken together, these data indicate that coelomocyte Ars might be involved in cell-to-cell crosslinking of surface sulfated polysaccharides vital for clot formation.
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PMID:Sea urchin coelomocyte arylsulfatase: a modulator of the echinoderm clotting pathway. 2240 49


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