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)

The activities of several lysosomal enzymes were assayed in control and in exercise-hypertrophied cardiac muscle of mice (Mus musculus). The repeated running program increased the activity of beta-glucuronidase (16.1%) in mouse cardiac muscle. Decreased activities of beta-N-acetylglucosaminidase (10.8%), acid ribonuclease (10.7%), and arylsulphatase (14.2%) were observed in the hypertrophied myocardium. The activities of acid deoxyribonuclease, cathepsin C, cathepsin D, and p-nitrophenylphosphatase as well as the activities of citrate synthase and cytochrome c oxidase, mitochondrial enzymes, were unaffected in cardiac muscle. We suggest that lysosomal enzyme responses are selective and highly different in physiologically and pathologically induced cardiac hypertrophies.
 ...
PMID:Changes in lysosomal enzyme activities in exercise-induced cardiac hypertrophy of mice. 622 47

GAG metabolism was investigated in rats with experimentally induced diabetes. In comparison to control animals, the uptake of 35S-sulfate was diminished in tissues of diabetic animals. Streptozotocin-induced diabetes showed a significant decrease in the content of GAG fractions except that of non-sulfated GAG in liver and kidney which was unchanged as compared to the control group. In rats rendered diabetic by alloxan, non-sulfated GAG increased appreciably in liver and kidney whereas highly sulfated GAG remained unchanged. In the skins of alloxan-diabetic rats both total and sulfated GAG decreased significantly. The activities of liver beta-glucuronidase, beta-N-acetyl glucosaminidase and cathepsin D were significantly increased in rats treated with streptozotocin and alloxan. In streptozotocin-diabetic rats, renal beta-glucuronidase and beta-N-acetyl glucosaminidase activities were reduced while cathepsin D activity was similar to that of controls. The renal beta-N-acetyl glucosaminidase and cathepsin D activities of alloxan-treated rats were not significantly different from normal but their beta-glucuronidase was significantly increased. In the spleen of streptozotocin-diabetic rats all the enzymes were increased except beta-N-acetyl glucosaminidase which remained unaltered. Increased excretion of uronic acid was observed in diabetic groups. These results collectively indicate that both streptozotocin- and alloxan-induced diabetes altered the synthesis and catabolism of GAG.
 ...
PMID:Influence of streptozotocin- and alloxan-induced diabetes on the metabolism of glycosaminoglycans. 624 Jan 83

Young rats, fed a low calcium and vitamin D deficient diet for 2 weeks, developed hypocalcemia, an increased activity of serum alkaline phosphatase and an increase in the serum concentration of immunoreactive parathyroid hormone. An increased activity of lactate dehydrogenase and cytochrome oxidase in odontoblasts was found. No shift in the general energy metabolic pathway was found as visualized in the lactate dehydrogenase iso-enzyme pattern. The dominating lactate dehydrogenase isoenzyme in odontoblasts from both the normal and the deficient rats was LDH 1 (H4, LD5), thus indicating primarily an aerobic energy-metabolism Also the activities of the lysosomal enzymes acid phosphatase, cathepsin D and hyaluronidase in the odontoblasts from the deficient animals were increased when compared to the normal animals. No significant change could be demonstrated for beta-glucuronidase and beta-N-acetylglucosaminidase. It was earlier found that this deficient diet caused an increase in odontoblast alkaline phosphatase activities and protein synthesis in vitro. In view of the present findings it might be concluded that the low calcium and vitamin D deficient diet causes a general increase in the odontoblast metabolism. It is not known whether this is due to the increase in parathyroid hormone or if it is a direct effect of the lowered serum calcium concentration.
 ...
PMID:Odontoblast metabolism in rats deficient in vitamin D and calcium. IV. Lysosomal and energy metabolic enzymes. 625 18

The modification of lysosomal enzyme activities in animals irradiated with the same sublethal dose at 4 different times of the day is reported. The results confirmed the absence of circadian fluctuations in all the lysosomal enzymes and in protein content. A difference in behaviour between acid beta-galactosidase and beta-glucuronidase on the one hand and between acid phosphatase and cathepsin D on the other was evident in irradiated animals. The results showed that acid beta-galactosidase and beta-glucuronidase increase from the early intervals after irradiation and reach the highest activity between 36 and 48 h. At these intervals autolysis phenomena, heavy cellular alterations and numerous phlogosis cells are present in the epithelium. Only beta-glucuronidase and acid beta-galactosidase indicate the level of radiation injury.
 ...
PMID:Modifications of small intestine lysosomal enzymes after irradiation at different times of the day. 628 98

The activity of collagenase and certain lysosomal hydrolases (cathepsin B1, cathepsin D, beta-glucuronidase and beta-N-acetyl glucosaminidase) was studied in serum and tissues of rats with streptozotocin- or alloxan-induced diabetes. The activity of serum lysosomal enzymes was increased in both groups (p less than 0.05). Both streptozotocin- and alloxan-diabetic animals showed significantly higher dermal collagenase activity than those of controls (p less than 0.01), but the liver and spleen showed similar activities; there was a significant decrease in the renal collagenase activity of streptozotocin-diabetic rats (p less than 0.05). Comparison of the alloxan- or streptozotocin-treated groups with control animals showed an increase in lysosomal enzymes (cathepsin B1, cathepsin D, beta-glucuronidase and beta-N-acetyl glucosaminidase in skin, liver and spleen) (p less than 0.05) but beta-N-acetyl glucosaminidase was unchanged in the spleen of streptozotocin-diabetic rats. There was no difference in renal cathepsin B1 and D in control versus alloxan-diabetic rats, but there was an increase in beta-glucuronidase and beta-N-acetyl glucosaminidase (p less than 0.05). The streptozotocin-diabetic animals showed decreased activities of renal lysosomal enzymes (p less than 0.05), but similar activity of cathepsin D to the control animals.
 ...
PMID:Influence of streptozotocin- and alloxan-induced diabetes in the rat on collagenase and certain lysosomal enzymes in relation to the degradation of connective tissue proteins. 630 89

Proteinases are thought to be responsible for cartilage and bone erosion noted in chronic inflammatory conditions. Suramin [8-(3-benzamindo-4-meta-1-benzamindo)naphthalene-1,3,5-trisulfonic acid], 10(-5) and 10(-4) M, inhibited the release of a mouse macrophage-derived cartilage proteoglycan-degrading enzyme. At 10(-5) M it antagonized the activity of beta-glucuronidase and cathepsin D derived from the mouse macrophage, as well as similar enzymes secreted by rat macrophages in vivo. When cultured at 10(-4) M with rabbit knee cartilage, it antagonized the autolytic release of proteoglycan, indicating an inhibitory activity against a chondrocyte-derived neutral proteinase. After in vivo treatment at 10 mg/kg/day s.c., it was ineffective in preventing the cartilage and bone erosion noted in the adjuvant arthritic rat.
 ...
PMID:Divergent effects of suramin on in vitro and in vivo assays of cartilage degradation. 634 39

The activities of four lysosomal and two nonlysosomal hydrolases were studied in skeletal muscle biopsy samples from patients with neuromuscular diseases and from controls. beta-Glucosaminidase activity was increased in polymyositis. beta-Glucuronidase and alkaline protease activities were elevated in muscular dystrophy in adults, whereas cathepsin D activity was increased in amyotrophic lateral sclerosis. There were significant correlations between the activities of lysosomal and nonlysosomal hydrolases. The activity of beta-glucuronidase, beta-glucosaminidase, alkaline protease, and dipeptidyl aminopeptidase IV showed a positive correlation with the severity of muscular atrophy. The activities of these hydrolases and the activity of dipeptidyl aminopeptidase I correlated positively with the activities of muscular galactosylhydroxylysyl glucosyltransferase and with the serum concentration of type III procollagen aminoterminal propeptide. The results suggest that in neuromuscular diseases the lysosomal and nonlysosomal pathways for muscle degradation are affected concomitantly with collagen biosynthesis.
 ...
PMID:Lysosomal and nonlysosomal hydrolases of skeletal muscle in neuromuscular diseases. 635 16

During pulse-chase experiments in cultured porcine kidney cells, an early 75-kilodalton (kDa) form of beta-glucuronidase is converted to a late 72-kDa form. The relative molecular weight difference between the two forms is maintained on removal of high-mannose carbohydrate with endoglycosidase H. Both forms have the same partial NH2-terminal sequence, and both migrate as single polypeptide chains following reduction, alkylation, and electrophoresis under denaturing conditions. On treatment with carboxypeptidase Y, the early form released [35S]Met faster than the late form. Thus, the late form of beta-glucuronidase is generated by COOH-terminal proteolytic processing of the early form. During similar experiments, the mass of the 30-kDa heavy chain of porcine cathepsin D decreased by about 1 kDa. The heavy chain of the two-chain enzyme is derived from the COOH terminus of a 44-kDa single-chain enzyme. On treatment with carboxypeptidase Y, the early single-chain enzyme released COOH-terminal [35S]Met and [3H]Lys faster than the later 29-kDa heavy chain. Like beta-glucuronidase, cathepsin D evidently undergoes COOH-terminal proteolytic processing during biosynthesis.
 ...
PMID:Carboxyl-terminal proteolytic processing during biosynthesis of the lysosomal enzymes beta-glucuronidase and cathepsin D. 636 Feb 5

The antishock effects of gabexate mesilate (FOY) were investigated in rats subjected to hemorrhagic hypotension, with particular attention focused on the stabilizing effects of hepatic lysosomes. The survival time of rats treated with FOY, infused for 2 hours intravenously at a rate of 50 mg/kg/hr, was significantly prolonged, accompanied by a tendency to decreased activity of plasma lysosomal enzymes. FOY, at a concentration of 10(-3) M, exerted a significant decrease in the extralysosomal release of acid phosphatase (15%, P less than 0.05), beta-glucuronidase (25%, P less than 0.05) and cathepsin D (25%, P less than 0.02) following hyposmotic labilization of lysosomes. Although the release of lysosomal enzymes might be counterbalanced by 50 mg/kg/hr of FOY, favorable cytochemical findings indicating stabilization of lysosomal membranes were consistently observed. The data suggest that FOY has antishock properties, and that these properties are caused, at least partially, by the stabilization of lysosomes.
 ...
PMID:Antishock effect of gabexate mesilate (FOY). 640 49

Lysosomal enzymes acid phosphatase, acid DNAase, acid RNAase cathepsin D,beta-galactosidase beta-glucuronidase were studied in mice and rat liver tissue within 3 days beginning from 4 o'clock a.m. at 4 hrs intervals. Activities of acid phosphatase, acid RNA ase in mice liver tissue and of cathepsin D in rat and mice liver tissues was higher at morning and day time than at evening and night. Alterations in enzymatic activity of non-sedimenting fraction of mice liver tissue correlated with that of total activity. In non-sedimenting fraction of rat liver tissue the enzymatic activity was altered only slightly. Within the second half of a day the enzymatic activity redistributed in the cells with an increase of the activity in non-sedimenting fraction, caused by labilization of lysosomal membranes.
 ...
PMID:[Diurnal changes in the lysosomal enzyme activity of the liver of mice and rats]. 642 29


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>