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

Several pharmacologic agents were tested for inhibition of phagocyte-induced release of lysosomal enzymes from guinea-pig alveolar mononuclear cells and peritoneal leukocytes. The activities of the lysosomal enzyme beta-glucuronidase and the cytoplasmic enzyme lactate dehydrogenase were determined in the cells and media following a 2-hour incubation period of cells and zymosan particles. Adrenergic and cholinergic agents, the 3,'5'-adenosine and guanosine cyclic nucleotides, and theophylline had no effect on phagocytosis or release of beta-glucuronidase or lactate dehydrogenase from alveolar cells. Cytochalasin B stimulated lysosomal but not cytoplasmic enzyme release from these cells in the absence of zymosan. Colchicine and hydrocortisone inhibited phagocytosis and beta-glucuronidase extrusion, and phenylbutazone inhibited only beta-glucuronidase release. Colchicine and phenylbutazone also inhibited enzyme release stimulated by cytochalasin B indicating that they were affecting postphagocytic events. The cyclic nucleotides and theophylline were without effect on the peritoneal leukocytes; dexamethasone and phenylbutazone inhibited enzyme release with only the former antagonizing phagocytosis.
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PMID:Effects of pharmacologic agents on release of lysosomal enzymes from alveolar mononuclear cells. 16 51

Monocytes derived from the peripheral blood of patients with familial Mediterranean fever (FMF) demonstrated a consistently lower phagocytic capacity (38-44%) for 125I-labelled Shigella flexneri when compared to monocytes from healthy subjects. Phagocytosis of both viable and killed Staphylococcus albus was similar in patients and controls. However, FMF monocytes had a two- to eight-fold depressed bactericidal capacity against S. albus in comparison to normal monocytes. Acid phosphatase and beta-glucuronidase monocyte activities were similar in patients and controls. It is suggested that the defects in monocyte function may be of importance in the pathogenesis of FMF. Colchicine had no effect on any of the indices studied.
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PMID:Monocyte function in familial Mediterranean fever. 34 7

Mouse peritoneal macrophages were cultured for 3 days with or without zymosan and at the same time exposed to various inhibitors of cellular metabolism. The cells were assayed for selective release of a lysosomal enzyme, and for cytotoxic activity against a tumor cell line, L-929-cells. Selective release of beta-glucuronidase was demonstrated in the supernatants from zymosan-stimulated macrophages. The stimulated macrophages were cytotoxic for the tumors cells, evaluated by measuring release of radioactivity during subsequent 4 days' co-culture of macrophages and 14C-thymidine-labelled tumor cells, and by counting cells per culture. Colchicine caused a slight, variable reduction in enzyme release and no change in cytotoxic effect from stimulated macrophages. Monensin decreased extracellular enzyme secretion and reduced the cytotoxicity in stimulated macrophages to control levels. Chloroquine caused a similar reduction in lysosomal enzyme release and cytotoxic activity in zymosan-stimulated cells. This inhibitor increased the enzyme release from control cells and induced a small, variable cytotoxic effect from these cells. The data indicate co-variation between macrophage-mediated cytotoxicity and a secretory process which can be blocked by monensin. The need for intact lysosomal function was also demonstrated.
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PMID:Cytotoxic activity of stimulated mouse macrophages exposed to various inhibitors. 371 7

The features and function of IgM-FcR of rat peritoneal macrophages were studied. Macrophages specifically bind and phagocytose ox red blood cells coated with rat IgM (EA-IgM) through a specific receptor. This receptor is trypsin sensitive and its activity requires Ca++ ions. Both sodium azide and low temperature (4 degrees) inhibit the bindings as well as ingestion of EA-IgM by macrophages, suggesting the metabolically dependent character of the interaction between EA-IgM and macrophages. Colchicine inhibits the binding of EA-IgM by macrophages. Similarly, the ingestion of EA-IgM was also inhibited when peritoneal exudate cells (PEC) were pre-treated with colchicine or vinblastine or cytochalasin B. It is suggested that cytoskeletal elements of macrophages play an important role both in the binding of EA-IgM to their receptors and in the subsequent internalization of the receptor-ligand complexes. Ingestion of soluble IgM antibodies containing immune complexes (IC) resulted in a release of beta-glucuronidase from macrophages.
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PMID:IgM-Fc receptor-mediated phagocytosis of rat macrophages. 720 29

Polymorphonuclear cells derived from the peripheral blood of patients with Familial Mediterranean Fever release more lysozyme in response to high temperature (42 degrees, 46 degrees C) than do control cells. No differences between the FMF and control cells were observed in the release of acid phosphatase, beta-glucuronidase, or lactoferrin. Colchicine treatment had no effect on the measurable release of the enzyme from PMNs derived from FMF patients. The increased release of lysozyme in response to high temperatures appears to be specific to FMF neutrophils, and was not found in PMNs from non-FMF patients with febrile or inflammatory diseases, nor was it seen in monocytes derived from the FMF patients. It is suggested that the increased release of lysozyme from the neutrophils may be of importance in the pathogenesis of FMF.
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PMID:A neutrophil lysozyme leak in patients with familial Mediterranean fever. 733 47

Organophosphate compounds are known to cause a selective increase of beta-glucuronidase activity in rat serum. Previous data suggested that increase of serum beta-glucuronidase activity was well correlated with decrease of that activity in rat liver microsomal fraction, thereby, suggesting a role of the microsomal enzyme in mediating the organophosphate effect. To investigate further the intracellular sorting pathway of beta-glucuronidase in dibutyl phosphate-treated rats, liver subcellular fractions were prepared at 12 or 48 h after in vivo administration of [3H]leucine and it was established that microsomal beta-glucuronidase was the origin of the increased serum enzyme. To characterize the intracellular secretory pathway of beta-glucuronidase in dibutyl phosphate-treated rats, Golgi subfractions were isolated and a time course study was carried out. At 30 min after administration of dibutyl phosphate, specific activity of beta-glucuronidase in GF-2 (Golgi intermediate fraction) and GF-3 (Golgi heavy fraction) was significantly increased to the maximum. Furthermore, colchicine pretreatment of rats caused a delay of the peak of specific activity for 30 min in GF-2 and GF-3, and accumulation of enzyme activity in Golgi subfractions was observed. Colchicine pretreatment also had an inhibitory effect on release of beta-glucuronidase into serum until 30 min after dibutyl phosphate injection. The electrophoretic pattern of microsomal beta-glucuronidase on polyacrylamide gel was found to show two major bands of microsomal enzyme type and lysosomal enzyme type in dibutyl phosphate-treated rats. Taken together, these findings indicate that microsomal beta-glucuronidase follows the intracellular secretory pathway and is secreted into serum via Golgi complex in response to dibutyl phosphate.
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PMID:Intracellular sorting of lysosomal beta-glucuronidase is altered due to administration of dibutyl phosphate. 853 25