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)

A concise review of the ultrastructural features and physiological properties of eosinophils is presented with the aim of delineating those properties of eosinophils that set them apart from other granulocytes. It has become clear that eosinophols are subject to chemotaxis by attractants that do not affect other cells (e.g., histamine, ECF-A, ESP) and that they contain antiflogistic agents (arylsulfatase IIB, peroxidase) that neutralize specific substances known to elicit the inflammatory response. The mechanisms underlying eosinophilia in a variety of cutaneous disorders are analyzed in the light of this information.
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PMID:Eosinophil function related to cutaneous disorders. 35 61

The presence of acid phosphatase, beta-glucuronidase and aryl sulfatase in juxtaglomerular cell granules (JGG) as well as the uptake and concentration of certain low molecular weight dyes by these granules have repeatedly suggested that they are akin to lysosomes. In the present experiments, rats were injected with three substances of widely different molecular weight and physicochemical properties--sucrose, iron sorbitol-citric acid complex (Jectofer) and horseradish peroxidase--that are well known to selectively concentrate in renal tubular cell lysosomes. None of these substances was found to enter the JGG to any significant degree, although both sucrose and Jectofer were evident in juxtaglomerular cells. Contrary to previous reports, thorium dioxide (Thorotrast) particles were not detected in the JGG after parenteral injection. These results indicate that JGG do not possess any significant lysosomal function and raise the question of the role of hydrolytic enzymes in the physiology of these granules.
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PMID:On the lysosomal function of juxtaglomerular granules. 61 Jul 7

To study the various stages of human mononuclear phagocyte maturation, we cultivated bone marrow in an in vitro diffusion chamber with the cells growing in suspension and upon a dialysis membrane. At 2, 7, and 14 days, the cultured cells were examined by electron microscopy and cytochemical techniques for peroxidase and for more limited analysis of acid phosphatase and arylsulfatase. Peroxidase was being synthesized in promonocytes of 2- and 7-day cultures, as evidenced by reaction product in the rough-surfaced endoplasmic reticulum, Golgi complex, and storage granules. Peroxidase synthesis had ceased in monocytes and the enzyme appeared only in some granules. By 7 days, large macrophages predominated, containing numerous peroxidase-positive storage granules, and heterophagy of dying cells was evident. By 14 days, the most prevalent cell type was the large peroxidase-negative macrophage. Thus, peroxidase is present in high concentrations in immature cells but absent at later stages, presumably a result of degranulation of peroxidase-positive storage granules. Clusters of peroxidase-negative macrophages with indistinct borders (epithelioid cells), as well as obvious multinucleated giant cells, were noted. Frequently, the interdigitating plasma membranes of neighboring macrophages showed a modification resembling a septate junction--to our knowledge, representing the first documentation of this specialized cell contact between normal macrophages. We suggest that such junctions may serve as zones of adhesion between epithelioid cells.
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PMID:Differentiation of macrophages from normal human bone marrow in liquid culture. Electron microscopy and cytochemistry. 65 15

The dermal cells in grey, xanthic, and white goldfish integuments were cytochemically characterized for the following enzymatic activities: tyrosinase, DOPA-oxidase, cytochrome oxidase, monoamine oxidase, peroxidase, non-specific esterase, cholinesterase, NAD-diaphorase, NADP-diaphorase, aryl sulfatase, nucleotide phosphodiesterase, beta-glucuronidase, acid phosphatase, alkaline phosphatase, adenosine triphosphatase, thiamine pyrophosphatase, glucose-6-phosphatase, aldolase, as well as succinate, malate, isocitrate, glutamate, glucose-6-phosphate, 6-phosphogluconate, alpha-glycerophosphate, alcohol, lactate, and beta-hydroxybutyrate dehydrogenases. It was found that the epidermis was a significant barrier to the access of cytochemical reaction substrates. Removal of the epidermal barrier provided dermal cell localizations of enzymatic activities which were reproducible. Further, alterations in reaction times and temperatures from the mammalian methodology provided conditions fe various integumental cells were compared for possible interrelationships. The basic foundations for future work with the dermis of poikilothermic vertebrates on an experimental basis were established. In addition, a previously undescribed non-pigmented dermal cell, the "x"-cell, was found to have enzymatic characteristics similar to both melanophores and lipophores. The "x"-cell may be the common precursor of both types of pigment cells.
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PMID:Cytochemical characterization of goldfish (Carassius auratus L.) dermis with special reference to the pigment cells. 82 86

The human colon adenocarcinoma cell lines SW 948, SW 1116, and SW 1222 were tested for their ability to sort and internalize lysosomal enzymes. The biosynthesis of the lysosomal enzymes cathepsin B, arylsulfatase A, and beta-hexosaminidase in these cell lines exhibits no significant differences to that in human fibroblasts. The intracellular targeting of newly synthesized hydrolases to the lysosomes relies in colon carcinoma cells on the mannose 6-phosphate receptor system. Both the cation-independent mannose 6-phosphate receptor (CI-MPR) and the cation-dependent mannose 6-phosphate receptor are expressed in all colon carcinoma cell lines investigated. Endocytosis of lysosomal enzymes via mannose 6-phosphate receptors is reduced in colon carcinoma cells as compared with human fibroblasts. SW 1116 cells were shown to be deficient in receptor-mediated endocytosis of mannose 6-phosphate containing ligands. Ligands of other endocytic receptors as well as the fluid-phase marker horseradish peroxidase were internalized at normal rates. While antibodies against CI-MPR bind to the surface of SW 1116 cells, these antibodies cannot be internalized. These data suggest that the cycling of CI-MPR is specifically impaired in SW 1116 cells.
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PMID:Biosynthesis and endocytosis of lysosomal enzymes in human colon carcinoma SW 1116 cells: impaired internalization of plasma membrane-associated cation-independent mannose 6-phosphate receptor. 132 52

To investigate the potential role of lysosomes in cirrhosis, we analyzed the activity of lysosomal enzymes in rats exposed long-term to phenobarbital and carbon tetrachloride. The activity of lysosomal enzymes was markedly increased in the homogenate of cirrhotic livers (e.g., arylsulfatase 9 +/- S.D.2 vs. 16 +/- 6 nmoles.min-1.mg-1 in control rats and cirrhotic rats, respectively; p less than 0.001). The corresponding plasma levels were also increased (7 +/- 1 vs. 12 +/- 3 nmoles.min-1.mg-1; p less than 0.01), whereas biliary excretion was diminished (16 +/- 7 vs. 7 +/- 2 pmol.min-1.gm liver-1; p less than 0.05) in cirrhotic rats. Stereological quantification of lysosomes visualized cytochemically revealed an increase of pericanalicular lysosomes averaging 1.5 +/- 0.4 around a canaliculus in controls and 3.7 +/- 1.0 in cirrhotic rats (p less than 0.01). Because this suggested a defect in the transcellular vesicular pathway, we investigated the biliary excretion of horseradish peroxidase and epidermal growth factor in perfused livers. Bile flow and total horseradish peroxidase excretion were similar in control rats and cirrhotic rats. However, the early peak of biliary horseradish peroxidase excretion--usually taken as evidence of paracellular transport--was increased in cirrhotic rats (13 +/- 7 vs. 57 +/- 22%; p less than 0.01), whereas the second peak--reflecting the transcellular vesicular pathway(s)--was markedly reduced (87 +/- 7 vs. 43 +/- 22%; p less than 0.001). A similar reduction in the biliary excretion of intact epidermal growth factor and of its degradation products was found. These results demonstrate an increased number of lysosomes in hepatocytes of cirrhotic livers; this appears to be the result of accumulation rather than proliferation, in view of the reduced transcellular vesicular movement of different markers into bile.
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PMID:Hepatic accumulation of lysosomes and defective transcytotic vesicular pathways in cirrhotic rat liver. 139 8

Enhanced chemiluminescent assays for hydrolase enzymes have been developed using proenhancer and pro-anti-enhancer substrates. Alkaline phosphatase is measured using disodium para-iodophenyl phosphate (proenhancer) which is converted to para-iodophenol and this in turn enhances the light emission from the horseradish peroxidase catalysed chemiluminescent oxidation of luminol by peroxide. An alternative strategy uses para-nitrophenyl phosphate which is converted by alkaline phosphatase to para-nitrophenol which inhibits the enhanced chemiluminescent reaction. The detection limit for the enzyme using the proenhancer and pro-anti-enhancer assays was 100 attomoles and 1 picomole, respectively. The proenhancer strategy was effective in assays for beta-D-galactosidase, beta-D-glucosidase and aryl sulfatase. A limited comparison of the proenhancer and a conventional colorimetric assay for an alkaline phosphatase label in an enzyme immunoassay for alpha-fetoprotein showed good agreement.
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PMID:Chemiluminescent assay of enzymes using proenhancers and pro-anti-enhancers. 172 39

The effect of platelet-activating factor (PAF) on inositol (1,4,5)trisphosphate (Ins[1,4,5]P3) mass, calcium mobilization, and the release of granule enzymes was studied on guinea pig peritoneal eosinophils (EOSs). PAF evoked a concentration-dependent accumulation of Ins(1,4,5)P3 with a drug concentration that elicits 50% of the maximum attainable response (EC50) of 10 nmol/L; the production of this second messenger was maximal at 1 mumol/L of PAF. Kinetic analysis of PAF (1 mumol/L)-induced Ins(1,4,5)P3 accumulation demonstrated it to be transient with a 3.8-fold increase over resting levels observed at 5 seconds. Thereafter, the level of Ins(1,4,5)P3 declined, returning to vehicle-treated levels 60 seconds after PAF challenge. Lyso-PAF, the inactive precursor and metabolite of PAF, was inactive at all concentrations examined. PAF also induced a rapid, concentration-dependent (EC50, 12 nmol/L) rise in the cytosolic-free calcium concentration ([Ca++]i) in fura 2-AM-loaded EOSs that was transient, peaking after the maximum increase in Ins(1,4,5)P3 mass was observed. A highly significant positive correlation was found between the peak increase in Ins(1,4,5)P3 and the peak rise in [Ca++]i. Functionally, PAF evoked a concentration-dependent release of granule constituents from both the small (arylsulfatase B; EC50, 3 nmol/L) and specific (EOS peroxidase; EC50, 2.7 nmol/L) granules that lagged, temporally, behind both Ins(1,4,5)P3 accumulation and the rise in [Ca++]i. Both the biochemical and functional effects of PAF examined in this study were antagonized by WEB 2086 (300 nmol/L), a selective PAF receptor-blocking drug. It is concluded that stimulus (PAF)-response coupling in guinea pig peritoneal EOSs may involve the receptor-mediated formation of Ins(1,4,5)P3 and subsequent release of intracellularly stored Ca++. This sequence of events may link PAF receptor activation to Ca(++)-dependent cellular responses, such as degranulation.
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PMID:Platelet-activating factor stimulates a rapid accumulation of inositol (1,4,5)trisphosphate in guinea pig eosinophils: relationship to calcium mobilization and degranulation. 207 75

Eosinophils from normal nonatopic healthy volunteers (195 +/- 106 cells per microliter) were isolated by centrifugation over a discontinuous Percoll gradient, under isotonic conditions, with a recovery of 46.5 +/- 26.2% from whole blood (n = 21; mean +/- SD). More than 90% of the eosinophils (purity greater than 93%) with a density between 1.095 to 1.105 gm/ml were defined normodense. Less than 10% of the eosinophils had a density less than 1.095 gm/ml and were defined hypodense. Isolation of eosinophils of patients with atopic asthma revealed a cell population with 65% to 70% hypodense cells that was independent of the total eosinophilic cell count. In vitro activation of normodense eosinophils, measured by an increase in superoxide production, induced quantities of hypodense eosinophils in the range found in patients with asthma. The amount of hypodense eosinophils induced by different stimuli was in the same order as the increase in superoxide production (antibiotic calcium ionophore A23187 greater than serum-treated zymosan greater than platelet-activating factor greater than N-formyl-methionyl-leucyl phenylalanine). During the stimulation of the normodense cells, no secretion of eosinophilic peroxidase or arylsulfatase B could be measured, even though hypodense eosinophils were produced. Enzymatic activity of arylsulfatase B within the eosinophils remained the same, before and after stimulation. The enzymatic activity of eosinophilic peroxidase in normodense eosinophils (16.6 +/- 9.7 micrograms/10(6) cells) did not change in the normodense fraction but was increased in the induced hypodense cells (34.0 +/- 8.4 micrograms/10(6) cells; n = 7; mean +/- SD; p less than 0.01) after stimulation.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Hypodense eosinophilic granulocytes in normal individuals and patients with asthma: generation of hypodense cell populations in vitro. 253 51

Although endosomes and lysosomes are associated with different subcellular functions, we present evidence that a lysosomal enzyme, arylsulfatase-A, is present in prelysosomal vesicles which constitute part of the endosomal compartment. When human cultured fibroblasts were subfractionated with Percoll gradients, arylsulfatase-A activity was enriched in three subcellular fractions: dense lysosomes, light lysosomes, and light membranous vesicles. Pulsing the cells for 1 to 10 min with the fluid-phase endocytic marker, horseradish peroxidase, showed that endosomes enriched with the marker were distributed partly in the light lysosome fraction but mainly in the light membranous fraction. By pulsing the fibroblasts for 10 min with horseradish peroxidase conjugated to colloidal gold and then staining the light membranous and light lysosomal fractions for arylsulfatase-A activity with a specific cytochemical technique, the endocytic marker was detected under the electron microscope in the same vesicles as the lysosomal enzyme. The origin of the lysosomal enzyme in this endosomal compartment was shown not to be acquired through mannose 6-phosphate receptor-mediated endocytosis of enzymes previously secreted from the cell. Together with our recent finding that the light membranous fraction contains prelysosomes distinct from bona fide lysosomes and was highly enriched with newly synthesized arylsulfatase-A molecules, these results demonstrate that prelysosomes also constitute part of the endosomal compartment to which intracellular lysosomal enzymes are targeted.
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PMID:Presence of a lysosomal enzyme, arylsulfatase-A, in the prelysosome-endosome compartments of human cultured fibroblasts. 256 59


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