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)

Activity of beta-glucuronidase and cathepsin-D were studied in brain, spinal cord and sciatic nerves of rats at 24 h or 10 days after daily i.p. administration of 50 mg/kg acrylamide. The activities of beta-glucuronidase and cathepsin-D in brain, spinal cord and sciatic nerves remained unaffected on single exposure but increased significantly in these tissues on administration of the neurotoxin for 9 consecutive days. The increase in the activity of beta-glucuronidase and cathepsin-D was more marked in sciatic nerves, than brain or spinal cord. These results suggest that cathepsin-D and beta-glucuronidase may be involved in the acrylamide-induced degeneration of nervous tissues and can serve as useful markers for the detection of chemical-induced neuropathies.
 ...
PMID:Acid hydrolases in brain, spinal cord and sciatic nerves of acrylamide-intoxicated rats. 647 10

Changes in activities of a new proteinase cathepsin T as well as some other lysosomal acid proteinases and hydrolases were examined in liver homogenate from rats treated with a single hepatotoxic dose of carbon tetrachloride. The most striking changes were several-fold increases of liver cathepsin T and D activities over their levels in untreated rats 3 days after administration of the agent to rats. Increase of cathepsin T was greater than that of cathepsin D at all doses of the hepatotoxin examined. The activities of N alpha-benzoyl-DL-arginine 2-naphthylamide hydrolase, acid phosphatase, beta-galactosidase and beta-glucuronidase in poisoned rat liver were unchanged or only slightly increased. Cathepsin T and D activities were less enhanced in mitochondrial lysosomal fractions than in the homogenate, and were greatly elevated in the supernatant fractions of liver from the treated rats. As judged from the molecular weights, the elevated activities of cathepsins T and D in the treated rat liver could be attributable to the two cathepsins themselves and not to other proteinases. Administration to rats of other hepatotoxic agents, thioacetamide and dimethylnitrosamine, also induced the elevation of the two cathepsin activities in liver, but on partial hepatectomy the activities of liver cathepsins T and D did not show such marked increases. Nonparenchymal liver cell fractions were responsible for almost all the increased activities of liver cathepsins T and D. It is possible that cathepsins T and D play a role in the heterolytic breakdown of hepatocyte molecules following CCl4 poisoning.
 ...
PMID:Increased activities of liver cathepsins T and D in carbon tetrachloride-treated rats. 649 24

This study investigated lysosomal disruption during hypothermic perfusion preservation of kidneys and its possible relationship to viability. The percentage of free and bound enzyme activity was analyzed for three lysosomal enzymes in homogenates made from perfused canine kidney cortex tissue, including beta-glucuronidase, cathepsin-D, and aryl sulfatase. All three enzymes displayed characteristic increases in free enzyme activity (47-68%) throughout 5 days of perfusion preservation. The increased activity obtained at 5 days of preservation was found to indicate "severe" tissue damage, as shown by a similar increase obtained in renal cortex tissue exposed to warm ischemia (37 degrees C) for 4 hr or longer. Aryl sulfatase was found to be the most sensitive indicator of severe damage. Pretreatment of kidney donors with methylprednisolone, a lysosomal stabilizer, was also studied in kidneys exposed to 5 days of perfusion. Pretreatment was found to reduce the percentage of free lysosomal enzyme activity following 5 days (nonviable) of perfusion to those levels normally obtained following 3-day (viable) perfusion. This indicates that methylprednisolone may be useful in modulating the severe disruption of lysosomes induced by long-term preservation. It is concluded that extensive disruption of lysosomes occurs during hypothermic perfusion preservation and may represent one cause for loss of organ viability.
 ...
PMID:Lysosomal enzyme release in hypothermically perfused dog kidneys. 649 98

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.
 ...
PMID:Effect of cyanidanol-3 on lysosomal enzyme activity of serum and granulocytes in chronic liver disease and active hepatitis. 671 21

Lysosomal acid phosphatase, beta-glucuronidase, and cathepsin-D were studied in liver cell fractions of rats regularly exercised by swimming. On the 21st day of the training, enzyme activities in the extralysosomal fraction and in the lysosomal fraction were higher and lower, respectively, than in the untrained controls. On the 40th day an increased enzyme activity was found in both fractions. By the end of the training period (54th and 80th days), a slightly decreased activity was recorded in both fractions. Lysosomal membrane permeability for enzymes was higher during the first period of the training, in particular when estimated under hypotonic conditions. Regular swimming training or 12-day treatment by ACTH stabilized the membrane of the liver lysosomes. This stabilization was believed to be mediated by corticosteroids mobilized by exercise or by the administration of ACTH.
 ...
PMID:Studies on the lysosomal enzyme system of the liver in rats undergoing swimming training. 674 78

Muscular dystrophy and cardiomyopathy were produced in weanling rats by feeding a vitamin E-deficient diet for 12 mth. Deficient and control rats were killed, and skeletal muscle and myocardium were used for subcellular studies and biochemical assay of selected lysosomal enzymes. Ultrastructurally, the skeletal muscle showed various degrees of pathological changes. In the severely damaged muscle fibres, prominent increase of secondary lysosomes, autophagic vacuoles, residual bodies, disappearance of myofilaments, rupture of sarcolemma and shrinkage of muscle fibres were noted. The damaged muscle fibres finally became dense residual bodies and dispersed in the interstitial spaces, where the macrophages and fibroblasts were found. In the myocardium, some muscle fibres were intact with mild fatty infiltration and marked proliferation of mitochondria. However, in the severely damaged myocardial fibres, the whole fibre was always filled with amorphous dense bodies, and the sarcolemma was ruptured. This resulted in dispersion of many cellular organelles in the surrounding interstitial space. A significant increase of cathepsin and beta-glucuronidase activity in the cytosol of both organs suggests that lysosomal enzymes may play a major role in the destruction of muscle and cardiac fibres in the long-term vitamin E-deficient animals.
 ...
PMID:Ultrastructural and lysosomal enzyme studies of skeletal muscle and myocardium in rats with long-term vitamin E deficiency. 715 34

The authors have measured the activity of acid phosphatase, beta-glucuronaidase and cathepsin-D in tthe sera of patients with different liver diseases, and the actvity of beta-glucuronidase in granulocytes and the rate of its release. Using the method for the releaseof beta-glucuronidase from the granulocytes they drew conclusions to thedegree of the membrane-damage occurring in the liver diseases. They provided that in the sera of patients with different liver diseases the increase in the activity of the acid phosphatase and the beta-glucuronidase is different. According to their in vitro studies the decrease in the beta-glucuronidase activity measured in the granulocytes, and the release of enzyme is in connection with the type of liver disease and with the different degree of lysosomal membrane alteration.
 ...
PMID:Lysosomal enzymes in sera and granulocytes of patients with chronic liver diseases. 728 55

Rat peritoneal macrophages in vitro were infected with Mycobacterium tuberculosis and the fate of M. tuberculosis inside macrophages was monitored. Alteration in the levels of nitric oxide (NO) measured in terms of nitrite formed, hydrogen peroxide (H2O2) and lysosomal enzymes such as acid phosphatase, cathepsin-D and beta-glucuronidase in macrophages following M. tuberculosis infection was also studied. Elevation in the levels of nitrite were observed from 72 h of M. tuberculosis infection. Irrespective of the time point, M. tuberculosis infected macrophages produced elevated levels of H2O2. Maximum increase in the level of acid phosphatase was observed from 72 h of M. tuberculosis infection, whereas maximum elevation in the level of beta-glucuronidase was observed 48 h after M. tuberculosis infection. However these microbicidal agents did not alter the intracellular viability of M. tuberculosis.
 ...
PMID:Fate of Mycobacterium tuberculosis inside rat peritoneal macrophages in vitro. 935 49

The present investigation was designed to characterize the biochemical and connective tissue components and to correlate the significance of morphological and biochemical perturbations in cyclophosphamide (CP)-induced lung fibrosis in rats. Lung fibrosis was induced in male Wistar rats by intraperitoneal injection of 20 mg/100 g body weight of CP, and their pneumotoxic derangements were characterized during an early destructive phase followed by a proliferative and synthetic phase. Serum angiotensin-converting enzyme (ACE) activity was higher in CP-treated rats at days 2, 3, 5, 7, and 11, but there was a significant decrease in lung ACE activity during the same time period. Elevated levels of beta-glucuronidase activity were observed in the lung lavage fluid of CP-administered rats days 2, 3, 5, and 7. Lung myeloperoxidase activity was higher in CP rats. Of significance was the presence of collagenase and collagenolytic cathepsin in the lavage fluid of CP rats, when compared with the barely detectable levels in controls. A similar increase in these enzyme activities was also noticed in the lung tissue of CP rats during the same experimental period. Lavage fluid hydroxyproline content was higher in CP rats when compared with controls. Similarly, lung protein and DNA levels were elevated significantly after treatment with CP. The pulmonary histamine and serotonin contents were significantly higher in CP rats. The incorporation of [3H]thymidine into lung total DNA, [3H]proline into lung hydroxyproline, and [35S]sulphate into lung glycosaminoglycan, measured as indicators of lung DNA, collagen, and glycosaminoglycan synthesis, respectively, was also higher in CP groups. Increased levels of hydroxyproline, elastin, hexosamine, total hexose, fucose, sialic acid, and uronic acid in the lungs of rats 14, 28, and 42 days after CP insult were characterized as biomarkers of CP-induced interstitial changes. These findings indicate that CP-induced lung fibrosis results in alterations not only in collagen synthesis and accumulation, but also in glycosaminoglycan and glycoprotein content.
 ...
PMID:Biochemical and connective tissue changes in cyclophosphamide-induced lung fibrosis in rats. 977 51

A key step in the targeting of soluble lysosomal enzymes is their recognition and phosphorylation by a 540 kDa multisubunit enzyme, UDP-N-acetylglucosamine-phosphotransferase (phosphotransferase). The molecular mechanism of recognition is still unknown, but previous experiments suggested that the phosphotransferase-binding sites on lysosomal proteins are represented by structurally conserved surface patches of amino acids. We identified four such regions on nonhomologous lysosomal enzymes, cathepsins A, B, and D, which were superimposed by rotating their structures around the Calpha atom of the glycosylated Asn residue. We proposed that these regions represent putative phosphotransferase-binding sites and tested synthetic peptides, derived from these regions on the basis of surface accessibility, for their ability to inhibit in vitro phosphorylation of purified cathepsins A, B, and D. Our results indicate that cathepsin A and cathepsin D have one closely related phosphotransferase recognition site represented by a structurally and topologically conserved beta-hairpin loop, similar to that previously identified in lysosomal beta-glucuronidase. The most potent inhibition of phosphorylation was demonstrated by homologous peptides derived from the regions located on cathepsin molecules opposite the oligosaccharide chains which are phosphorylated by the phosphotransferase. We propose that recognition and catalytic sites of the phosphotransferase are located on different subunits, therefore, providing an effective mechanism for binding and phosphorylation of lysosomal proteins of different molecular size.
 ...
PMID:Identification of UDP-N-acetylglucosamine-phosphotransferase-binding sites on the lysosomal proteases, cathepsins A, B, and D. 989 Aug 84


<< Previous 1 2 3 4 5 6 7 Next >>