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:3.2.1.31 (beta-glucuronidase)
7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Arachidonate metabolites appear to be involved in lung injury caused by cobra venom factor (CVF)-induced complement and polymorphonuclear leukocyte (PMN) activation. These studies were designed to assess the effects of a dietary-induced deficiency of arachidonic acid on CVF-induced lung injury. Rats raised on an essential fatty acid-deficient (EFAD) diet exhibited the expected changes in fatty acid composition including decreased plasma levels of arachidonic acid and increased levels of 5,8,11-eicosatrienoic acid. In intact rats raised on the EFAD diet, CVF-induced lung injury was attenuated. When blood and excised lungs from rats raised on the normal diet were used, CVF caused pulmonary vascular constriction and acute lung injury, as evidenced by increased 125I-labeled bovine serum albumin accumulation in lung parenchyma and alveolar lavage fluid. The CVF-induced pulmonary artery pressor response and lung injury were reduced when blood perfusate or blood perfusate and excised lungs were obtained from rats raised on the EFAD diet. The pulmonary vascular constriction and lung injury were not attenuated when the blood perfusate was obtained from rats raised on the normal diet, irrespective of whether the excised lungs were obtained from rats raised on the normal or EFAD diet. PMNs obtained from rats raised on the EFAD diet demonstrated decreased superoxide production as well as impaired random migration and chemotaxis in vitro. In contrast, beta-glucuronidase release was quantitatively similar to PMNs from control rats. These data indicate that the EFAD diet-induced attenuation of CVF-induced pulmonary hypertension and acute lung injury is due to defective effector cells in blood rather than modified pulmonary target tissue.
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PMID:Lung injury caused by cobra venom factor is reduced in rats raised on an essential fatty acid-deficient diet. 280 79

In the present studies the in vivo and in vitro effects of erythromycin A and azithromycin, a new type of macrolide (Fig. 2.), were investigated upon extracellular release of lysosomal enzymes, beta-glucuronidase (beta-Gluc) and beta-N-acetylglucosaminidase (beta-Glm) by using two experimental model systems: in vivo-adjuvant-induced arthritis in rats and in vitro- human polymorphonuclear leucocytes (PMNL) exposed to bovine serum albumin/anti-bovine serum albumin (BSA/anti-BSA), immune complex. Administrations of erythromycin A or azithromycin at doses of 5, 10 and 15 mg/kg into rats one day prior and 2, 4, 6, 8 and 10 days after a single subplantar injection of Freund's complete adjuvant significantly (p less than 0.01) inhibited extracellular release of lysosomal enzymes tested in the synovial fluid of injected left hind paw. These effects were dose-dependent. Further, erythromycin A and azithromycin at concentrations of 10(-7) M, 10(-6) M and 10(-5) M significantly (p less than 0.01) reduced excocytosis of both lysosomal enzymes, beta-Gluc and beta-Glm from human PMNL initiated by BSA/anti-BSA in a dose-related fashion. However, azithromycin was by far more effective (p less than 0.01) in decreasing extracellular release of beta-Gluc and beta-Glm either in the in vivo or in vitro experiments in comparison with erythromycin A. Appropriate control experiments excluded the possibilities that erythromycin A or azithromycin interfered with activities of lysosomal enzymes or with test reagents. Also, in no instances was there enhanced release of a cytoplasmic enzyme LDH.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Comparative studies on the effects of erythromycin A and azithromycin upon extracellular release of lysosomal enzymes in inflammatory processes. 284 7

The extracellular release of beta-glucuronidase and beta-N-acetylglucosaminidase from normal human polymorphonuclear leucocytes initiated with bovine serum albumin/anti-bovine serum albumin immune complex (15 micrograms/ml) was significantly inhibited (p less than 0.01) by pretreatment with increasing concentrations (10(-8) M, 10(-7) M, 10(-6) M and 10(-5) M) of sodium thiomalate in a time- and dose-related fashion. Also, beta-glucuronidase and beta-N-acetylglucosaminidase exhibited similar responses to the effects of bovine serum albumin/anti-bovine serum albumin or sodium thiomalate. In contrast, neither bovine serum albumin/anti-bovine serum albumin nor sodium thiomalate provoked appreciable leakage of the cytoplasmic enzyme, lactate dehydrogenase. This indicates that cell integrity remains intact under the experimental conditions described.
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PMID:Effect of sodium thiomalate on immune complex-induced release of lysosomal enzymes from human polymorphonuclear leucocytes. 308 97

Naturally occurring glucuronides and glucosides dissolved in organic solvents can be split with the help of beta-glucuronidase (EC 3.2.1.31) immobilized on controlled pore glass. To protect the enzyme against denaturation by the organic solvents and to promote hydrolytic cleavage of substrates, two methods were used: (a) Immobilization via crosslinking with aged glutaraldehyde in presence of bovine serum albumin; and (b) Adsorption of wet enzyme to the carrier in the presence of organic solvents.
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PMID:Studies on the immobilization of glucuronidase (Part 2). Cleavage of hardly soluble substrates in organic solvents. 324 3

A sensitive and specific RIA has been developed to measure thyronine (To) in urine. The RIA used an anti-To antibody obtained from a rabbit immunized with a L-To-human serum albumin conjugate and [3H]To as the radioligand. The acetic acid analog of To (ToAc), that is the diphenyl structure with an acetic acid side-chain, cross-reacted strongly with the antibody. Relative to To, it cross-reacted 160% in phosphate-buffered saline, pH 7.4, and 100% in 0.075 mol/L barbital buffer, pH 8.6, containing sodium salicylate (final concentration, 8 mg/mL). The latter conditions were employed for the RIA, and the results reported thus reflect the presence of To and/or ToAc. 3-Monoiodothyronine, 3'-monoiodothyronine, 3',5'-diiodothyronine, and 3,5-diiodothyronine cross-reacted with the anti-To antibody 1.9%, 1.7%, 0.3%, and 0.2%, respectively; the cross-reactivity of other To derivatives and tyrosine and its derivatives was less than 0.05%. Urinary To and/or ToAc excretion in 12 normal subjects averaged 16 +/- 2 (+/- SE) micrograms/day (59 +/- 9 nmol/day) or 14 +/- 2 micrograms/g creatinine (5.9 +/- 0.6 nmol/mmol creatinine). Treatment of urine from normal subjects with beta-glucuronidase or sulfatase did not significantly alter the To content. Column and thin layer chromatographic studies revealed that 83% and 61%, respectively (range, 37-100%), of urinary To immunoreactivity was attributable to ToAc. The mean daily excretion of To in 20 patients with nonthyroidal illness [NTI; 22 +/- 4 micrograms/day (82 +/- 17 nmol/day)] was similar to that in normal subjects, but was elevated when expressed as nanomoles per mmol creatinine (20 +/- 2; P less than 0.001), because creatinine excretion was reduced in the NTI patients. The mean daily urinary To excretion in 13 patients with hyperthyroidism due to Graves' disease was slightly elevated [29 +/- 6 micrograms/day (108 +/- 21 nmol/day); P less than 0.1], but was clearly elevated when expressed as nanomoles per mmol creatinine (37 +/- 8; P less than 0.001), again because creatinine excretion was reduced in these patients. The mean urinary To excretion was subnormal in 13 patients with hypothyroidism and was significantly (P less than 0.005) less than that in the NTI patients regardless of the manner in which the results were expressed. Analysis of pronase hydrolysates of thyroid glands obtained at autopsy from euthyroid patients suggested that the To content of the thyroid approximates only 1.2% that of T4, supporting the thesis that prior iodination of tyrosine is critical for the coupling process in the thyroid.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:A radioimmunoassay for measurement of thyronine and its acetic acid analog in urine. 341 Sep 34

A receptor which recognizes glycoproteins bearing terminal mannose residues has been isolated from human placental membranes. Washed membranes were solubilized with buffer containing 1% Triton X-100 and applied to a mannose-Sepharose affinity column. The column was eluted with buffer containing 200 mM mannose and 1% cholate. The major protein eluted exhibited a molecular weight of 175 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The protein binds 125I-labeled mannosylated bovine serum albumin in a saturable fashion with a dissociation constant of 4 nM. Ligand binding is pH-dependent with maximal binding above pH 6.5. This binding can be inhibited with EDTA, mannose, fucose, mannan, beta-glucuronidase, and bovine serum albumin conjugated to fucose. Polyclonal antibodies generated against the mannose binding protein immunoprecipitate a single 175-kDa protein species from both surface-iodinated and biosynthetically labeled human monocyte-derived macrophages.
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PMID:Isolation and characterization of a mannose-specific endocytosis receptor from human placenta. 361 Oct 70

Rabbit alveolar macrophages express a plasma-membrane receptor that recognizes glycoprotein ligands bearing terminal mannose, fucose or N-acetylglucosamine residues. Macrophage membranes were washed extensively with buffers containing high salt and mannose or EDTA to remove endogenously bound ligand, before Triton X-100 extraction. The extracts were chromatographed on mannose-Sepharose. Elution with mannose, followed by dialysis and a second mannose-Sepharose step with EDTA elution, produced a preparation that migrated as single protein band of Mr 175,000 on SDS/polyacrylamide-gel electrophoresis. The purified protein binds mannose-BSA (bovine serum albumin) with a dissociation constant of 1.9 X 10(-8) M. Ligand binding is Ca2+ and pH-dependent, with maximal binding at neutral pH and low binding below pH 6.0. The binding of 125I-mannose-BSA is inhibited by ligands bearing high-mannose oligosaccharides, such as mannan or beta-glucuronidase, as well as the monosaccharides mannose, fucose and N-acetylglucosamine. Galactose, galactosylated BSA, glucose and mannose 6-phosphate are non-inhibitory. Amino acid compositional analyses indicate that the receptor contains high concentrations of aspartate/asparagine and glutamate/glutamine, and low amounts of methionine. The carbohydrate composition was studied by lectin overlays of electrophoretically transferred receptor, and the results indicate the presence of N-linked complex and O-linked sialylated oligosaccharides. A protein of Mr 175,000 was immunoprecipitated from radio-iodinated macrophage membranes with an antibody generated against purified rabbit lung mannose receptor.
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PMID:Isolation and characterization of a mannose-specific endocytosis receptor from rabbit alveolar macrophages. 366 87

The selective release of beta-glucuronidase (beta-Gluc) and beta-N-acetylglucosaminidase (beta-Glm) from human polymorphonuclear leucocytes (PMN), initiated with bovine serum albumin/anti-bovine serum albumin (BSA/anti-BSA) immune complex (15 micrograms/ml-1) was significantly reduced by increasing concentrations (10(-7) M, 10(-6) M and 10(-5) M) of D-penicillamine (D-PEN) in a dose-dependent fashion. These effects upon the exocytosis of the lysosomal enzymes studied are in accordance with the results obtained previously in rats with adjuvant arthritis. In contrast, Dichlofenac Sodium (DICHL), which has been found to exert inhibitory activity upon extracellular release of beta-Gluc and beta-Glm in adjuvant arthritic rats in previous studies, had no significant in vitro effect on the exocytosis of these enzymes at the concentrations identical to those of D-PEN. Also, Gold Sodium Thiomalate (GST), in the same concentrations ranging from 10(-7) M-10(-5) M, failed to inhibit selective release of beta-Gluc and beta-Glm in the present investigations. Additionally, BSA/anti-BSA, D-PEN, DICHL and GST did not significantly produce the extracellular release of lactate dehydrogenase (LDH) indicating that under experimental conditions described the cell remained intact. Moreover, neither D-PEN, DICHL, GST or BSA/anti-BSA significantly changed the activities of lysosomal enzyme markers used in these experiments. The possible mechanism(s) of the observed phenomena are discussed.
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PMID:Effects of D-penicillamine, dichlofenac sodium and gold sodium thiomalate upon the selective release of lysosomal enzymes from human polymorphonuclear leucocytes to immune complex. 393 42

Antibodies raised to human placental beta-glucuronidase were shown to cross-react with the beta-glucuronidase secreted by mouse 3T3 fibroblasts, but did not react with other lysosomal enzymes. The beta-glucuronidase secreted by 3T3 cells was purified 15000-fold by chromatography on an affinity column made from this antibody and resolved into a single component, of Mr 68000, by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Iodinated samples of purified enzyme were taken up into mouse peritoneal macrophages by receptor-mediated endocytosis at a rate similar to that calculated previously for unlabelled enzyme, and uptake was competitively inhibited by yeast mannan. Binding of beta-glucuronidase to macrophages was saturable, with a Kd of 7 X 10(-9)l/mol, an affinity comparable with that calculated for the binding of mannosylated bovine serum albumin (Kd 1.3 X 10(-9)l/mol), a ligand specific for mannose receptors. Four times as many molecules of mannosylated albumin (12000) as of beta-glucuronidase (3000), however, bound to each cell. This purification and iodination procedure did not therefore have any adverse effect on the uptake properties of secreted beta-glucuronidase, and provides a ligand with which to investigate binding and specific endocytosis into a range of different types of cell.
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PMID:Iodinated fibroblast beta-glucuronidase as a ligand for receptor-mediated endocytosis. 403 56

Serial renal biopsies for glomerular culture, histochemical staining for beta-glucuronidase, electron microscopy (EM) and light microscopy, were used to study macrophage involvement in experimental chronic immune complex (IC) glomerulonephritis (GN) induced in rabbits by daily intravenous injections of bovine serum albumin (BSA). In the 26 animals studied, proliferative GN of variable severity was induced, with mild disease in 5 animals, moderate proliferation in 15 and crescentic GN in 6. Macrophages first appeared in glomerular culture outgrowths during the 2nd and 3rd weeks, coincident with the onset of proteinuria and rising serum creatinine concentration. Large numbers of macrophages (in excess of 20 per glomerulus) were seen by the 5th weeks and persisted to the 9th week. The number of macrophages in outgrowths was not significantly greater in animals with crescentic disease. EM demonstrated macrophages in capillary loops, and in glomeruli with crescents, macrophages could be seen in the urinary space. Histochemical staining for beta-glucuronidase also demonstrated macrophages in the glomerular tuft and in crescents when present. These results indicate that macrophages constitute a considerable proportion of the glomerular hypercellularity seen in chronic IC glomerulonephritis.
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PMID:Involvement of the macrophage in experimental chronic immune complex glomerulonephritis. 621 16


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