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)

Cells of the mononuclear phagocyte system contain a cell surface receptor which mediates the uptake of mannose- and fucose-terminated glycoproteins. We have extended the initial studies to human alveolar and monocyte-derived macrophages in culture using two radiolabelled ligands, the synthetic glycoconjugate mannose-bovine serum albumin and the lysosomal glycosidase, beta-glucuronidase. Uptake (37 degrees C) of 125I-mannose-BSA by freshly isolated alveolar macrophages is saturable with increasing concentrations of ligand. Kuptake values in macrophages of smokers and nonsmokers are similar, and resemble earlier reported values using rabbit alveolar macrophages (Kuptake = 40 nM). Uptake of 125I-mannose-BSA in cultured smoker macrophages is identical to that found in fresh cells, and uptake is stable for 5-10 days in culture. Fucose- and mannose-BSA are the most effective inhibitors of uptake, while N-acetylglucosamine-BSA is inhibitory at slightly higher concentrations. Binding (4 degrees C) of 125I-mannose-BSA is likewise ligand concentration dependent (KD = 30 nM). Freshly isolated human monocytes from healthy subjects and patients with cystic fibrosis do not have mannose-specific uptake. However, after monocytes are in culture for 3 days, mannose-specific uptake appears and Kuptake values and specificity of uptake are identical with the results from the alveolar macrophages. No uptake of mannose-BSA could be found in the human monocyte-like cell line, U937.
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PMID:Characterization of the mannose/fucose receptor on human mononuclear phagocytes. 629 10

Mannose 6-phosphate is an important recognition site involved in transport of newly synthesized lysosomal enzymes from the endoplasmic reticulum to lysosomes. The current study is the first demonstration of functional mannose phosphate receptors in macrophages. The receptor appears to be similar in many respects to that expressed in fibroblasts. Binding at 4 degrees C of a mannose-6-P-containing ligand, alpha-mannosidase from Dictyostelium discoideum, was specific and saturable (KD = 1.6 nM). In the presence of permeabilizing agents (saponin and digitonin), macrophage mannose-6-P receptors gave a distribution of 15-20% on the surface and 80-85% inside. Uptake studies gave a Kuptake value of 4.9 nM. Mannose-6-P, Hansenula holstii phosphomannan, and fructose 1-phosphate were effective inhibitors of alpha-mannosidase uptake. Inhibitors of mannose uptake, such as beta-glucuronidase, mannose-bovine serum albumin, fucose-bovine serum albumin, or mannan had no effect on alpha-mannosidase uptake. Likewise, an inhibitor (fucoidin) of the macrophage receptor which recognizes negatively charged proteins did not inhibit alpha-mannosidase uptake. Uptake was linear over 90 min and inhibited by chloroquine, suggesting that surface receptors recycle. These data demonstrate that macrophages contain receptors which specifically recognize mannose-6-P units and are distinct from the well characterized mannose receptors. The finding that the mannose-6-P receptors play a role at the surface, together with the fact that most of the receptors are intracellular (similar to the mannose receptor) suggests that both carbohydrate receptors play a regulatory role at the surface and intracellularly in transport of lysosomal enzymes.
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PMID:Identification of mannose 6-phosphate receptors in rabbit alveolar macrophages. 632 65

The effect of in vitro capacitation (events that occur before the acrosome reaction) on the acrosomal enzymes of human spermatozoa was determined. Capacitation of human spermatozoa was assessed by their ability to penetrate denuded hamster oocytes. The activities of a number of enzymes commonly associated with the sperm acrosome, including nonzymogen acrosin, proacrosin, inhibitor-bound acrosin, hyaluronidase, acid phosphatase, beta-glucuronidase, beta-glucosidase, beta-N-acetylglucosaminidase, beta-galactosidase and beta-N-acetylgalactosaminidase were assessed. With the exception of acid phosphatase, no alteration in enzyme activity occurred after 4 h of incubating the spermatozoa under capacitation conditions although gamete fusion took place. The acid phosphatase levels decreased twofold, presumably due to the loss of seminal (prostatic acid phosphatase that loosely adheres to spermatozoa. After 8 h of capacitation, a large decrease in sperm enzyme levels took place only in the case of hyaluronidase, although small decreases were also noted in total acrosin, proacrosin and inhibited acrosin. No new electrophoretically migrating forms of acrosin were observed. Decreases in total acrosin and proacrosin, but not in inhibited acrosin, also occurred when spermatozoa were incubated under noncapacitating conditions for 8 h, indicating that capacitation may specifically cause the release of some acrosin inhibitor from human spermatozoa. It is concluded that, with the possible exception of hyaluronidase, the in vitro capacitation of human spermatozoa does not cause a major change in its acrosomal enzyme content so that these hydrolases are fully present before the acrosome reaction takes place during gamete fusion. Serum albumin appears to protect against the loss of some of these enzymes since the activity of several glycosidases was significantly reduced when the spermatozoa were incubated for 8 h in human serum albumin-free medium.
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PMID:Acrosomal enzymes of human spermatozoa before and after in vitro capacitation. 640 71

The clearance of circulating IgA immune complexes following acute bile duct obstruction was investigated in this study. IgA immune complexes were formed in vitro from MOPC-315, an IgA M-component with anti-dinitrophenyl (DNP) specificity, and 125I-DNP10 bovine serum albumin (BSA). Eighteen hours after laparotomy during which the common bile duct was either identified only or identified and ligated, the IgA immune complexes were injected intravenously. Groups of bile duct-ligated and bile duct-patent rats were also injected intravenously with IgG anti-DNP-125I-DNP10BSA immune complexes and 125I-bovine liver beta-glucuronidase to assess the hepatic clearance of materials not dependent on an intact biliary system. Clearance of IgA immune complexes was delayed after bile duct ligation. Although the clearance of IgA immune complexes was delayed, only 10% of these complexes remained in the circulation at 3 hr. The clearance of IgG immune complexes and beta-glucuronidase was not affected by ligation. These experiments demonstrate the physiologic importance of a patent bile duct in the normal clearance of IgA immune complexes in the rat. The observation that clearance is delayed, but not completely inhibited by bile duct ligation suggests that alternate mechanisms exist for removing IgA immune complexes from the circulation.
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PMID:The effect of bile duct obstruction on the clearance of circulating IgA immune complexes. 669 69

125I-Labeled L-fucose-albumin complex and rat preputial beta-glucuronidase are rapidly cleared from plasma after intravenous infusion. L-Fucose-albumin retards the plasma clearance of beta-glucuronidase whereas D-fucose-albumin is inactive. In vitro, 125I-labeled L-fucose-albumin is taken up into rat or rabbit alveolar macrophages by receptor-mediated pinocytosis. Uptake (37 degrees C) is time-dependent, is saturable with increasing ligand concentration (Kuptake = 4.4 X 10(-8) M), and requires Ca2+. 125I-labeled D-fucose-albumin is poorly taken up. Binding (4 degrees C) is saturable and Ca2+ dependent. Binding and uptake are fully inhibited by yeast mannan. A series of neoglycoproteins, including L-fucose-albumin, were tested as inhibitors of uptake of 125I-labeled beta-glucuronidase into macrophages. The following order of potency was observed: L-Fuc = D-Man greater than GlcNAc approximately D-Glc greater than D-Xyl much greater than than D-Gal = L-Ara = D-Fuc. L-Fucose-terminated oligosaccharides coupled to bovine serum albumin also block 125I-labeled beta-glucuronidase uptake into macrophages.
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PMID:L-Fucose-terminated glycoconjugates are recognized by pinocytosis receptors on macrophages. 694 Jan 20

Synovitis was induced in rabbits sensitized to bovine serum albumin (BSA) by a modification of the method of Dumonde and Glynn. Agents were administered starting on the day of initial BSA joint challenge and every weekday (14-17 doses) for 17 to 21 day periods. Synovial tissues were then excised and evaluated either (1) histologically for inflammatory cell infiltration, or (2) both histologically and for total IgG, anti-BSA, and beta-glucuronidase levels in homogenates of portions of the same tissues. By the intraperitoneal and oral routes, methylprednisolone (1 mg/kg/day), azathioprine (25-40 mg/kg/day) and cyclophosphamide (10 mg/kg/day) produced significantly decreases of 40-100% in some or all of the parameters measured. Non-steroidal anti-inflammatory drugs, including phenylbutazone, ibuprofen and acetylsalicylic acid at oral doses of 75 or 100 mg/kg/day, were ineffective as were colchicine at 1 mg/kg/day and indomethacin at 5 mg/kg/day. Thus, as we have measured it, this model of rheumatoid arthritis is not affected by those agents considered to be of limited effectiveness in this chronic disease, but is ameliorated by corticoids and some slow acting agents.
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PMID:Chronic immune synovitis in rabbits. II. Modulation by anti-inflammatory and anti-rheumatic agents. 697 4

The purified amphipathic proteins, alpha s 1-casein, beta-casein, and alkali-denatured serum albumin were studied for chemotactic and enzyme-releasing effects on human neutrophil leucocytes. Evidence for chemotaxis both in fluid-phase gradients and on solid-phase gradients was obtained using visual assays. In fluid-phase gradients, neutrophils showed good orientation to gradient sources of these proteins at concentrations of 10(-4) to 10(-5) M. Solid-phase gradients of casein and of denatured albumin were prepared on glass coverslips, and the locomotion of neutrophils attached to these coverslips was filmed by time-lapse cinematography. Displacement of neutrophils towards the highest concentration of substratum-bound protein was observed, suggesting that neutrophils can show true chemotaxis on a solid-phase gradient. All three proteins induced enzyme release from neutrophils in the absence of cytochalasin B. Lysozyme release was equivalent to that released by stimulation with formyl methionyl peptide in the presence of cytochalasin B, but the proteins stimulated a smaller release of beta-glucuronidase than the peptide. The proteins stimulated release of neutrophil proteases which were able to digest both casein and denatured albumin extracellularly. It is suggested that this proteolytic activity may assist locomotion of neutrophils, especially on solid-phase protein gradients, by cleaving membrane-attached protein, thus both freeing cell-surface receptors and allowing the cell to detach itself from the substratum and continue movement.
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PMID:Chemotactic and enzyme-releasing activity of amphipathic proteins for neutrophils. A possible role for protease in chemotaxis on substratum-bound protein gradients. 701 48

Proximal tubular segments (S1, S2 and S3) of the rabbit kidney were incubated in oxygenated Ringer's solution (30 min, pH 7.4, 37 degrees C) containing bovine serum albumin (10 g/l) and [3H]morphine (0.7 microM). The uptake, expressed as tissue water/medium ratio at equilibrium, for S1 was 42.2 +/- 3.95 (mean +/- S.E.), n = 16 tubules from six animals; for S2, 41.6 +/- 4.17, n = 18 tubules from six animals; and for S3, 29.0 +/- 3.83, n = 15 tubules from six animals, a value significantly lower (P less than .05) than in the S1 and S2 segment. High-performance liquid chromatography analysis of the accumulated tritium revealed metabolism of [3H]morphine. Unchanged morphine represented 35.5 +/- 3.4% of the total radioactivity recovered in the extract from S1 segments, 51.1 +/- 7.7% from S2 and 77.3 +/- 1.8 from S3 segments. After treating the tubular extracts with beta-glucuronidase (5 hr, 25 degrees C), all the recovered radioactivity represented unchanged morphine. The main metabolite, thus, was a glucuronide. KCN (10(-2) M), mepiperphenidol (Darstine, 10(-4) M) and quinine (10(-4) M) inhibited [3H]morphine uptake by 55-70%. Surprisingly, there was no decrease in uptake in the presence of N1-methylnicotinamide (10(-3) M). We conclude that the whole proximal tubule is able to accumulate morphine by a specific transport system for organic cations, but that part of this uptake might be due to cellular metabolism and intracellular binding of the drug.
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PMID:Transport and metabolism of [3H]morphine in isolated, nonperfused proximal tubular segments of the rabbit kidney. 714 42

The urinary aldosterone (ALD) was measured by aldosterone RIA kit and the following results were obtained. (1) We have known that ten percent solution of bovine serum albumin (BSA) instead of free serum LAD is used as the diluent of the urine in aldosterone RIA kit. (2) The upper limits of free ALD, HCl-ALD and beta-glucuronidase ALD in the urine diluted with 10% BSA were 1.6, 9.0 and 9.5 micrograms/dl respectively. (3) The values of urinary conjugated HCl-ALD and beta-glucuronidase ALD were approximately 3.5 times and 4 times as much as that of free ALD respectively. (4) A good correlation was obtained among the results of three methods (HCl-ALD, beta-glucuronidase ALD and free ALD). (5) No difference was found in the values of the urinary ALD in the healthy subjects and the patients with essential hypertension, kidney diseases and acute liver diseases.
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PMID:[Estimation of the urinary aldosterone (author's transl)]. 732 22

Immunoglobulin and beta-glucuronidase levels in joint exudates and homogenates of synovial tissues were measured during the course of bovine serum albumin (BSA) antigen-induced synovitis in rabbits. After intra-articular BSA challenge, the anti BSA hemagglutinating antibody in tissue homogenates increased with time up to 14 days. Results obtained indicated relatively greater increases in specific anti-BSA activity compared with total IgG and are compatible with in vivo antibody synthesis by inflamed synovial tissue. beta-Glucuronidase was measured as a reflection of phagocytic cell activity. Tissue enzyme levels increased to a maximum at 1 day and this level persisted up to at least 7 days, despite the fact that exudate enzyme levels reached a maximum at 1 day and then declined significantly over the next 2-3 weeks. These observations reinforce the view that inflamed synovial tissue possesses a substantial potential for perpetuating joint destruction by producing increased levels of inflammatory mediators.
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PMID:Chronic immune synovitis in rabbits. I. Immunoglobulin and beta-glucuronidase analyses of synovial tissues and joint exudates. 734 Apr 64


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