Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The influence of three lysosomal enzymes, beta-glucuronidase, acid phosphatase and hialuronidase, the representatives of lysosomal enzymes which can be released by exocytosis, was tested o reactivity of rat lymph node lymphocytes in vitro. These three enzymes do not change the spontaneous lymphocyte stimulation. However, beta-glucuronidase enhances the lymphocyte response to PHA. On the contrary, acid phosphatase and hialuronidase suppress PHA-induced stimulation of lymphocytes. In the mixed lymphocyte cultures (MLC) beta-glucuronidase enhances or suppresses DNA synthesis depending on the degree of lymphocyte stimulation in control MLC. Acid phosphatase and hialuronidase suppress lymphocyte stimulation in MLC.
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PMID:Regulatory role of lysosomal enzymes in rat lymphocyte reactivity in vitro. 645 81

Microdissection of lyophilized sections of fetal heads permits the analysis of relatively pure samples of epithelium and mesenchyme. These techniques were applied to a study of acid phosphatase and beta-glucuronidase activities in the developing palate in A/Jax mice. Acid phosphatase was found to be more concentrated in the palatal epithelium than the underlying mesenchyme. Conversely, beta-glucuronidase was more concentrated in the mesenchyme than the epithelium. A disparate developmental pattern of acid phosphatase and beta-glucuronidase activity was observed in the oral epithelium: acid phosphatase activity increased from intra-uterine Day 17 into neonatehood and beta-glucuronidase activity decreased towards term. Analysis of cortisone-induced palatal shelves showed increased activity of both acid phosphatase and beta-glucuronidase in the presumptive fusing epithelium.
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PMID:Microanalysis of epithelial and mesenchymal acid hydrolase activities in the developing palate. 664 52

The authors examined the effect in vivo and in vitro of Catergen (cyanidanol-3) on demonstrable lysosomal enzyme activity in the serum and granulocytes in liver diseases. Acid phosphatase, cathepsin-D and beta-glucuronidase were investigated. In the in vitro studies the direct effect of Catergen was observed by enzyme release. In chronic active hepatitis without treatment the lysosomal activity of the serum increases, the lysosomal activity of the granulocytes decreases and in vitro release increases. Under the effects of Catergen treatment the lysosomal activity of the serum decreases in comparison with initial values, approaching the lysosomal enzyme activity observed in healthy persons. Under in vitro conditions, lysosomal enzyme release from the granulocytes decreases in treated individuals and thus a higher lysosomal enzyme activity in the granulocytes is observed. Granulocytes separated from the blood of healthy persons were incubated with Catergen in isotonic and hypotonic media. In an isotonic medium the release did not change significantly. Under the effect of hypotension the release of lysosomal enzyme increased considerably. In vitro incubation with small doses of Catergen significantly inhibited the degree of release. On the basis of these data it may be supposed that Catergen has a stabilizing effect on the lysosomal membrane and is thus beneficial in the treatment of liver injuries (alcoholic, toxic, inflammatory) with lysosomal membrane alterations.
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PMID:Effect of cyanidanol-3 on lysosomal enzyme activity of serum and granulocytes in chronic liver disease and active hepatitis. 671 21

Lysosomal preparations were exposed to various concentrations of dimethylsulphoxide (DMSO) and aspirin singularly and in combination. Acid phosphatase and beta-glucuronidase activities were measured and utilized as an indication of lysosomal membrane stability under experimental conditions in the presence and absence of these drugs. Extremely low concentrations of each drug were employed in an attempt to mimic the levels which might be feasible in vivo. There was a significant decrease of enzyme activity (increased structure-linked latency) in the presence of DMSO. Aspirin had no significant effect on the latency of the lysosomes. There was no indication of synergism between DMSO and aspirin. It was concluded that some of the therapeutic advantages attributed to DMSO in the treatment of arthritis and other musculoskeletal diseases may come from the stabilization of lysosomes in cells that contribute to the pathological condition. Aspirin did not seem to exert a therapeutic effect through this mechanism.
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PMID:The effects of aspirin and dimethyl sulphoxide on the latency of lysosomes in a cell-free system. 672 49

The activity of acid hydrolases was studied in serum from patients with mucolipidosis (II and III) and other lysosomal disorders. In mucolipidosis II and III all hydrolases examined except alpha-glucosidase, beta-glucosidase and acid phosphatase were greatly increased. High values for beta-galactosidase were seen in mucopolysaccharidosis types I and II, Gaucher's disease, juvenile amaurotic idiocy and metachromatic leucodystrophy. N-Acetyl-beta-glucosaminidase activity was high in mucopolysaccharidosis types I, II, III and Gaucher's disease. The activity of beta-glucuronidase was increased in mucopolysaccharidosis types I, II and III, Gaucher's disease, juvenile amaurotic idiocy and metachromatic leucodystrophy. Acid phosphatase had increased activity only in Gaucher's disease. In several lysosomal storage disorders no increased values could be found. It is suggested that high values in serum from patients with lysosomal storage disorders (not including mucolipidosis II and III) may depend upon liver cell damage, which disturbs the clearing of acid hydrolases from serum.
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PMID:Acid hydrolases in serum from patients with lysosomal disorders. 676 92

Lysosomal hydrolases as indicators of plaque-induced bone resorption in tissue culture were studied. Fetal rat bones cultured in a synthetic medium containing sonicated and filtrated human dental plaque were used as bones to be resorbed. Acid phosphatase and beta-glucuronidase were found to be the most suitable enzymes for studying the degradation rate of bone cell lysosomes. When dental plaque is used as a resorbing agent, special attention has to be paid to the fact that plaque extract contains similar lysosomal hydrolase activity. Plaque hydrolases in the present study were quite stable in culture medium. No significant adsorption of enzymes by fetal rat bones occurred while remarkable adsorption by synthetic hydroxyapatite was found. The present results indicate that dental plaque is able to release lysosomal hydrolases from bone explants. This release corresponds to the degree of resorption measured by 45Ca release from bones.
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PMID:Release of lysosomal hydrolases from bone explants affected by dental plaque. 694 Apr 14

Implantation of embryos was studied in mice which had bee ovariectomized on the afternoon of day 4 of pregnancy and injected intraperitoneally with a non-steroidal antioestrogen or control injection. Normal implantations were obtained in the latter mice as indicated from the positive blue-dye sites when animals were killed late in the evening of day 4. Exposure to CI-628, however, led to a significant inhibition in the number of implantations and only a small percentage of the mice exposed to the steroid antagonist showed normal implantation sites. Study of a few lysosomal enzymes in uterine tissues at the time of early embryo attachment revealed a striking change in the activity of leucyl naphthylamidase. The enzyme showed a reduction in its activity only in uterine which contained attached blastocysts. Acid phosphatase, beta-glucuronidase and non-specific esterase did not show any such implantation-specific changes in their activity patterns. A possible role of leucyl naphthylamidase in the attachment of the embryo to the wall of the uterus has been explored.
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PMID:Involvement of lysosomal enzymes in mouse embryo implantation: effect of the anti-oestrogen, CI-628 citrate. 702 43

Chondrocytes from adult and immature articular cartilage were separated on the basis of size by rate-zonal centrifugation in a Ficoll density gradient. Lysozomal enzyme activity (acid phosphatase and beta-glucuronidase) was determined in gradient fractions containing chondrocytes of different sizes. Acid phosphatase and beta-glucuronidase activity in mature articular cartilage was greatly increased in small sized cells, located in the superficial tangential zone. In cells from immature calf articular cartilage, there were two peaks of increased activity, on in the superficial tangential zone, the other in the deep radial zone, close to the cartilage bone junction. It is speculated that the small surface cells, with thier high degradative enzyme levels, may explain why the osteoarthritis process starts at the surface.
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PMID:Degradative enzyme activity in isolated chondrocyte populations. 706

Autolysosomes were isolated from rat livers treated with leupeptin by a combination of differential and Percoll density gradient centrifugation techniques. The purified autolysosome fraction was verified by morphological analysis to be highly purified and to contain contaminants which were scarcely detectable. The enrichment of the lysosomal enzyme activities in the purified autolysosomes over the homogenate was 12-, 14-, 22-, and 24-fold for beta-glucuronidase, acid phosphatase, beta-N-acetylglucosaminidase, and cathepsin D, respectively. Measurement of the activity of the marker enzymes for various subcellular organelles also proved that the purified autolysosome fraction was essentially free from contamination by other organelles. When the autolysosomes isolated from rat livers treated with leupeptin for 1 h were disrupted by osmolysis, acid hydrolases were easily solubilized. Acid phosphatase, however, became membrane bound in the autolysosomes prepared at longer periods of time after the leupeptin treatment. The autolysosomes exhibited enhanced permeability of the membranes after a short duration of time after the leupeptin treatment (30 and 60 min) and became stabilized later. These changes in the properties of the autolysosomes with time after the leupeptin treatment may be interpreted as meaning that progressive rearrangement of the lysosomal constituents occurred within the autolysosomes with time after the genesis.
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PMID:Isolation and characterization of autolysosomes which appeared in rat liver after leupeptin treatment. 711 55

The activity of the lysosomal enzymes acid phosphatase, beta-glucuronidase, alpha-mannosidase and hexosaminidase were determined in CSF obtained from patients with proven bacterial meningitis and from patients with various other diagnoses. The mean value for CSF beta-glucuronidase from bacterial meningitis was elevated 73-fold when compared to the aggregate mean of all control groups. Acid phosphatase and alpha-mannosidase means were 26-fold and 33-fold elevated respectively while hexosaminidase was threefold elevated. Measurement of CSF acid phosphatase and beta-glucuronidase should prove a rapid useful test in establishing the diagnosis of bacterial meningitis. Chromatography of CSF samples on DEAE Sephadex allowed the resolution of hexosaminidase and beta-glucuronidase into individual isozymes. The ratio of hexosaminidase A to hexosaminidase B was generally higher in CSF from patients with bacterial meningitis but was very variable. The isozyme distribution for beta-glucuronidase was identical to that found in serum and no differences in pattern were found between patients and control subjects.
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PMID:CSF lysosomal hydrolase activity as an aid in the diagnosis of bacterial meningitis. 721 93


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