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 localization and concentration of lysosomal enzymes acid phosphatase and beta-glucuronidase in kidney cells of Syrian hamsters after DES administration were studied. A positive cytoplasmic reaction was demonstrated for both enzymes. Increased activity of these enzymes were observed in renal tumour in contrast to normal homologous cells. These results can be explained on the basis that lysosomal enzymes were synthesized in tumour cells at a higher rate or it may be due to the invasion of tumour tissue by hydrolase rich microphages.
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PMID:Studies of estrogen induced renal tumours in male Syrian hamsters. I. Cytochemical studies of lysosomal enzymes acid phosphatase and beta-glucuronidase. 9 53

The activities of several lysosomal hydrolases including beta-glucuronidase, acid phosphatase and hexosaminidase were compared in serum from 19 well-nourished subjects and 13 children (age 5--24 months) who were suffering from marasmus. The marasmic children exhibited growth retardation and muscle wastage but had normal serum protein values and absence of psychomotor retardation or oedema. Significant changes were observed in serum beta-glucuronidase and acid phosphatase activities. Compared to the control group, serum beta-glucuronidase (determined at pH 4.5 using the fluorogenic substrate, 4-methylumbelliferyl-beta-D-glucuronide) was 2.3-fold higher (p less than 0.001) in the marasmic children. In contrast, serum acid phosphatase values were approximately 50% lower (p less than 0.01) in the marasmic population. Serum hexosaminidase values in the two groups under study were not significantly different. Determination of the beta-glucuronidase to acid phosphatase ratio permitted effective discrimination (p less than 0.001) of serum from normal and protein-calorie malnourished children. The finding that the elevated value of the beta-glucuronidase : acid phosphatase ratio (0.64--1.37) decreased to within the normal range of values (0.10--0.43) after nutritional rehabilitation of several marasmic cases indicates that the determination of serum lysosomal hydrolases using fluorogenic substrates might provide a rapid and sensitive quantitative method for objectively evaluating the status of protein-calorie malnourished children and their responsiveness to nutritional therapy.
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PMID:Changes in serum lysosomal hydrolases in marasmus. 10 62

Auranofin, an oral chrysotherapeutic agent effective in the treatment of rheumatoid arthritis (RA), was found to be a potent, noncytotoxic inhibitor of IgG-RF immune complex-induced lysosomal enzyme release (LER) from human leukocytes. At a concentration of 1 microg Au/ml (5 microM), auranofin produced a marked reduction in beta-glucuronidase (100%), acid phosphatase (88%), and lysozyme (72%) release. In contrast, gold sodium thiosulfate (GST, an injectable gold compound) had no inhibitory activity on LER at equivalent gold concentrations (i.e., 1 microg Au/ml) and only modest activity (less than 36% inhibition) at concentrations as high as 40 microg Au/ml. The 50% inhibitory dose (LD50) of auranofin on LER was calculated to be 3-4 microM (0.6-0.8 microg Au/ml). Blood gold levels in auranofin-treated RA patients were found to be within the range required for in vitro inhibition of LER, and correlated with decreases in IgG, RF titers, and IgG-RF immune-complex formation in vitro. These results suggest that the therapeutic action of auranofin may be caused, at least in part, by inhibition of LER and/or decreases in immune-complex formation.
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PMID:Effect of auranofin, a new antiarthritic agent, on immune complex-induced release of lysosomal enzymes from human leukocytes. 10 28

The growth of some obligate intracellular parasites is contingent upon avoidance of lysosomal activation during growth in their host cells. This is accomplished by the various parasites by different mechanisms and with different degrees of efficiency. The possibility was tested that the lysosomal stabilizer cortisone acetate might protect and thus enhance the growth of Rickettsia typhi in mouse L cells irradiated 6 days earlier. Beginning 2 days before infection of the L cells with a multiplicity of 10 rickettsiae, 20 microgram of cortisone per ml was added in medium 199 containing 5% fetal calf serum. This concentration of cortisone was below the cytotoxic level, as determined by viability staining, but was sufficient to significantly alter the ratios of cellular and released acid phosphatase and beta-glucuronidase in uninfected and infected cells, as shown by spectrophotometric analysis. Rickettsial replication, measured by hemolytic activity at 96 h and confirmed by microscopic observations at earlier stages of infection, was increased by the cortisone. Cortisone concentrations of 10 or 40 microgram/ml were less effective, and cortisone was ineffective when the rickettsial multiplicity per L cell was 2 or lower. These results indicate that amounts of cortisone that increase lysosomal stabilization in L cells favor rickettsial multiplication when the multiplicity of infection is relatively high.
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PMID:Growth of Rickettsia typhi in irradiated L cells enhanced by lysosomal stabilization. 10 7

The influences of paraffin and GMA-embedding on acid phosphatase, esterase and beta-glucuronidase activity of differently fixed or freeze substituted rat livers were studied. 1. Embedding generally causes a reduction of the enzyme activities but improves considerably the quality of the microscopical pictures when compared with appropriate cryostat sections. Embedding therefore may serve as a very useful tool for detail studies on the cytological level. 2. The embedding media act differently on the reactive sites: a. Paraffin causes a heavy denaturation of the enzyme activity in lysosomes but preserves the activities of the ergastoplasmic (= "microsomal") enzymes. The degree of denaturation increases with increasing embedding temperature. b. GMA-embedding delivered opposite effects by preserving lysosomal activities and quenching endoplasmic enzymes. UV-polymerization of GMA causes a general inactivation of enzymes. 3. The histochemical reactivity of substrates such as glycogen was not influenced by the embedding. However, its most natural localization is achieved by freeze drying or isopropanol freeze substitution followed by GMA-embedding.
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PMID:The influence of glycol methacrylate (GMA) and paraffin embedding on freeze substituted and fixed tissues for enzyme histochemistry. 10 5

Four hydrolases, beta-galactosidase, beta-glucuronidase, beta-N-acetylglucosaminidase and acid phosphatase were examined in red blood cells (RBC) of normal donors and patients with homozygous beta-thalassaemia. Highly sensitive fluorimetric substrates were used to determine the specific activities of these enzymes. In order to avoid contamination by lysosomal activities derived from white blood cells (WBC), the mature RBV were separated from other blood elements by cellulose chromatography. The hydrolase activities in normal RBC were detected only in their plasma membranes and were found to be considerably lower than in WBC or platelets. In thalassaemic RBC, hydrolase activities were present in both plasma membranes and in the soluble fraction. The normoblast fraction contributed most of the hydrolase activity found in these preparations, suggesting the presence of lysosomal particles in thalassaemic RBC. No differences in the enzymatic activities were found when purified membranes of mature RBC from thalassemic and normal preparations were compared. The origin and roles of these hydrolytic enzymes in normal and thalassaemic RBC membranes are not known.
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PMID:"Lysosomal" enzyme activities in red blood cells of normal individuals and patients with homozygous beta-thalassaemia. 11 37

The effects of the nonsteroidal title compound (DBF) on the biochemical composition of the Fallopian tube and uterus were studied in the rhesus monkey. Monkeys received 2 mg/kg daily by mouth, which is the antifertility dose. The weight of the pituitary was significantly decreased (p less than .05) due to treatment, but the weights of the Fallopian tube, uterus, ovary and adrenal were unaltered. In both the Fallopian tube and uterus, DBF induced a significant increase (p less than .01) in the concentration of glycogen, protein and nonprotein nitrogen, and a significant decrease (p less than .01) in the concentration of lactic acid. The total phospholipid level in the uterus showed an increase (p less than .01) in the activities of adenasine triphosphatase (ATPase), malic dehydrogenase, acid and alkaline phosphatases, and glucose-6-phosphate dehydrogenase (G-6-PD) was seen. Lactic dehydrogenase activity fell (p less than .01) and the activity of beta-glucuronidase was unchanged. In the uterus, ATPase, malic dehydrogenase, alkaline phosphatase and lactic dehydrogenase activities increased significantly (p less than .01), beta-glucuronidase and acid phosphatase activities fell (p less than .01) and G-6-PD activity was unaltered. The antifertility effect of DBF may be due to its ability to elicit many biochemical effects similar to those induced by a typical estrogen.
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PMID:Effect of 2-phenyl-3-p-(beta-pyrrolidinoethoxy) phenyl-beta-methoxy benzofuran hydrochloride (DBF) on the biochemistry of the fallopian tube and uterus of rhesus monkey (Macaca mulatta). 12 89

Local irradiation of the carotid artery of the hypercholesterolemic rabbit with 2000 rd of X-rays gives rise to infiltration of lipid droplets in the intima and media, becoming visible 3 days after the irradiation. At the same time, acid phosphatase and beta-glucuronidase become activated. These enhanced activities are localized in different cells of the arterial wall. Acid phosphatase activity is localized in the intima, while the beta-glucuronidase activation is found preferentially in the media. A functional heterogeneity of the lysosomal content of the different cells is suggested. A model for the development of the radiation-induced atheromatosis is presented.
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PMID:Initial events in radiation-induced atheromatosis I. Activation of lysosomal enzymes. 12 8

Two types of rosette-forming cells were identified: rosette-forming cells with membrane-bound receptors for sheep erythrocytes (E-RFC) and rosette-forming cells with Fc receptors (EA-RFC). In both types of lymphocytes the activity of acid phosphatase, beta-glucuronidase, non-specific esterase and the content of glycogen were studied. A significant difference was established between E-RFC and EA-RFC lymphocytes as concerns acid phosphatase activity; corresponding mean values being 72.4 +/- 7.5 respectively 44.4 +/- 4.5 (p less than 0.01). As oppose to the acid phosphatase activity the glycogen was significantly higher in EA-RFC lymphocytes (mean 67.2 +/- 6.9), as compared with E-RFC (mean 41.6 +/- 9.2). It seems to us that estimations of acid phosphatase activity may be of value in differentiating 2 populations of lymphocytes.
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PMID:Cytochemical studies of rosette-forming cells. 12 52

The structure and the activity of acid phosphatase, beta-glucuronidase, alkaline phosphatase and ATP-ase in the liver and small intestine of rats receiving for 20 days a one-time, fixed at a certain time (2 o'clock) feeding was studied morphologically in dynamics in 2, 6, 24 and 48 hours after the last feeding. Furthermore, parallel with this the activity of acid phosphatase, beta-glucuronidase, alpha-glucosidase and beta-acetylglucosaminidase was determined in homogenates by biochemical methods. Alongside the total activity free activity of beta-acetylglucosaminidase and the activity of this enzyme in the blood plasma was defined. It is shown that during fasting, especially by the 48th hour, there takes place a significant activation of lysosomal enzymes both in the liver and in the small intestine (in the cells of the cylindrical epithelium). A significantly increased permeability of lysosomal membranes (mounting free activity of beta-acetylglucosaminidase) in the liver and of plasmic hepatocytes membranes (higher activity of the enzyme in the blood plasma) was also ascertained. The activation of the lysosomal enzymes is considered to be an adaptive reaction of the organism in fasting.
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PMID:[Histological, histoenzymatic and biochemical study of the liver and small intestine of rats during short periods of starvation]. 12 2


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