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)

The levels of six lysosomal enzymes (acid phosphatase, beta-acetylglucosaminidase, cathepsin D, beta-galactosidase, arylsulfatase A, and beta-glucuronidase) and four neutral and alkaline hydrolases (esterase, inorganic phyrophosphatase, alkaline phosphatase, and 5'-nucleotidase) were measured in osteoarthritic, rheumatoid and control synovia. All enzyme levels in diseased synovium except esterase values in osteoarthritis were significantly elevated compared with controls. The mean values of the group of acid hydrolases and the group of neutral and alkaline hydrolases in osteoarthritic synovia were 1.9- and 2.0-fold greater than those of control specimens. In rheumatoid synovia, the values were 4.2- and 4.5 fold greater than control for the same enzymes. Levels in rheumatoid synovia were significantly higher than those in osteoarthritic synovia with the exception of 5'-nucleotidase. Only a limited correlation between the extents of inflammation present in the synovia and the levels of a lysosomal marker enzyme (cathepsin D) was observed. These results demonstrate that whatever the mechanism, increased levels of acid hydrolases as well as certain neutral and alkaline hydrolases are present in osteoarthritic and rheumatoid synovia, and these enzymes are probably contained in the synovial lining cells.
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PMID:Acid, neutral, and alkaline hydrolases in arthritic synovium. 0 9

Optimal assay conditions are described for 8 hydrolases of Euglena gracilis var. bacillaris, SM-L1 (streptomycin-bleached) strain, 7 of which have an acid pH-optimum. Acid-phosphatase, beta-galactosidase, beta-glucosidase, b-fucosidase, cathepsin D, RNase, DNase, and an esterase are active in cell homogenates. Amylase has very low activity, and beta-glucuronidase, arylsulfatase, beta, N-acetyl-glucosaminidase, alpha-fucosidase, and alpha- and beta-mannosidase are inactive.
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PMID:Hydrolytic enzymes of Euglena gracilis: characterization and activity as a function of culture age and carbon deprivation. 0 4

Cardiac hypertrophy was produced in rats by constriction of the ascending aorta. Removal of the constricting band 10 days after operation resulted in rapid decline in left ventricular (LV) weight and total ventricular RNA. Activities of acid RNase and beta-glucuronidase were elevated 3 days after aortic constriction. Activities of cathepsin D and alkaline RNase were unchanges. Activities of cathepsin D and acid RNase were unchanged 1 and 3 days after removal of constricting band. Ca2+-activated, neutral protease (CAF) isolated from postmitochondrial muscle supernatant was partially purified and characterized. CAF specifically degrades alpha-actinin when incubated with isolated myofibriles in the presence of Ca2+.
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PMID:Lysosomal and neutral hydrolase activity during the regression of cardiac hypertrophy. 0 53

Six patients with liver metastases from carcinoid or colon carcinoma underwent hepatic derterialization. This operation, known to cause both tumor necrosis and liver cell damage, caused considerable increases of several lysosomal acid hydrolases in the circulation. Thus, beta-glucosidase showed a small temporary increase during the operation, followed by a slower but higher reaction reaching a maximum 12 to 36 hours postoperatively. Similar reactions were noted for beta-glucuronidase, acid phosphatase, beta-galactosidase, arylsuphatase A, and N-acetyl-beta-glucosaminidase while no reactions were found for cathepsin D. Very high enzyme levels occurred in a patient dying from bleeding complications in the postoperative period.
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PMID:Plasma activities of lysosomal enzymes after hepatic dearterialization in man. 0 1

Rat embryo fibroblasts, grown in Eagle's MEM with 10% serum, showed a rapid increase in autophagic vacuoles when placed in MEM with 0-1% serum. Concurrent with this response, degradation of cellular proteins showed a 2-fold increase. We did not find any increases in cathepsin D, beta-glucuronidase, beta-galactosidase, and beta-glucosidase, or proteolytic activity of cell homogenates at pH 3.7 towards endogenous substrates. Homogenates prepared in 250 mM sucrose at pH 7.0 showed a 40% increase in protein breakdown. These data support the hypothesis that the induced increase in proteolysis, characteristic of cells placed in a nutritionally deficient medium, is effected by an activated vacuolar apparatus (lysosomes and autophagic vacuoles). We suggest, however, that this mechanism is distinct from normal protein turnover in the cell, but can be rapidly induced by appropriate alterations in the cellular environment. Finally, this induced proteolytic mechanism is not dependent upon an increase in lysosomal enzymes, but rather a structural alteration within the cell which effects a transfer of cellular proteins into the vacuolar apparatus.
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PMID:Role of the vacuolar apparatus in augmented protein degradation in cultured fibroblasts. 2 52

The enzymatic activity of five acid hydrolases: acid phosphatase, arylsulfatase A, deoxyribonuclease, beta-glucuronidase, and cathepsin D, was assayed in fetal (fifteenth and eighteenth days of pregnancy) and neonatal (Days 0, 5, 10, and 15 post-partum) mouse liver. With the exception of cathepsin D, the activity increased around birth to levels varying according to the enzyme. Histochemical observations of other authors appear to justify, at least in part, the present results, which indicate that late days of fetal development and early neonatal life may constitute a transitional stage to full lysosomal enzyme functionality of the adult organ. The livers of the mothers were also assayed for the same enzymes. Each activity showed a peculiar pattern which was, in turn, different from that found in the liver of the litter for the same enzyme, probably as a cause of the metabolic requirement of the gland. The hypothesis that the lysosomes are heterogeneous in their enzyme composition is suggested by the variety of enzymatic patterns found in the liver of the litters and their mothers.
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PMID:The development of lysosomal apparatus. I. Lysosomal enzyme activities in the liver of mice at perinatal stages and those of their mothers. 2 3

In the present paper measurements of DNA and protein content and lysosomal enzyme (beta-glucuronidase, beta-acetylglucosaminidase, cathepsin D) acitivities were performed in the rat liver following partial hepatectomy. The rats were divided into three age groups: 6 weeks, 10 months and 18 months. The regenerating liver of the 6 week and 10 month old animals disclosed significant higher concentrations of DNA than the controls. The 18 month old rats revealed no differences of the DNA content. In all age groups the protein content of the regenerating liver was significant diminished. There were age dependent differences of the activities of the three lysosomal enzymes. In comparison to the controls the beta-glucuronidase activity of the regenerating liver was significantly decreased in the 6 week and 18 month old animals, but significantly increased in the 10 month old rats. Refering to the protein content there were no differences of the activities of beta-acetylglucosaminidase and cathepsin D between the regenerating and control livers. Refering to the liver fresh weight the beta-acetylglucosaminidase activity of the regenerating liver was significant diminished in the 10 and 18 month old rats.
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PMID:[Influence of age on biochemical parameters of the rat liver following partial hepatectomy (author's transl)]. 3 15

Twelve acid hydrolases, 4 near-neutral hydrolases, and alkaline phosphatase were demonstrated in 0.34 M sucrose homogenates of Trypanosoma cruzi strain Y: p-nitrophenylphosphatase and alpha-naphthylphosphatase, with optimum pH at approximately 6.0; alpha=ga;actpsodase. beta=ga;actpsodase. beta=g;icpsodase, N-acetyl-beta-glucosaminidase, cathepsin A and peptidase I and III, with optimum pH between 5.0 and 6.0; and arylsulfatase, cathepsin D, alpha-arabinase and alpha-mannosidase with optimum pH at approximately 4.0. alpha-Glucosidase, glucose-6-phosphatase and peptidase II had optimum pH at approximately 7.0. beta-Glycerophosphatase had a broad pH-activity curve from 4,0 to 7.4, with maximum activity at pH 7.0. The main kinetic characteristics of these enzymes and their quantitative assay methods were studied. No activity was detected for alpha-fucosidase, beta-xylosidase, beta-glucuronidase, elaidate esterase, acid lipase, and alkaline phosphodiesterase.
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PMID:Acid and neutral hydrolases in Trypanosoma cruzi. Characterization and assay. 4 19

The object of this investigation was to determine whether the pathological events which occur during the Arthus and mixed hypersensitivity reaction could be monitored biochemically and whether changes in enzyme concentrations would reflect the severity of tissue damage either in the skin itself or in the lymph draining the lesion. The initial increase in vascular permeability which resulted in oedema formation in the tissue was reflected by a large increase in the water and protein content of the tissues, however, there was no increase in either the protein concentration or flow of the lymph. The increases in the total enzyme content in the lesion could not always be related to the macroscopic appearance of the reaction site. However, the severity of the reaction did appear to be related to the concentration of cathepsin D in the oedema fluid present at the reaction site. Although the release of enzymes was reflected in the local lymph in the case of LDH and beta-glucuronidase there was no increase in of the concentration cathepsin D in the lymph draining the lesion.
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PMID:Biochemical and cellular changes in skin and lymph during Arthus and mixed hypersensitivity reactions in rabbits. 13 25

The present study investigated the activities of lysosomal enzymes of the liver after administration of Furosemid. 10 weeks and 1-year old male albino rats were treated with 40 mg Furosemid for 4 subsequent days. According to the method devised by de Duve a sediment rich in lysosomes was produced by fractionated centrifugation and subsequently the enzyme activity of beta-glucuronidase, beta-acetylglucosaminidase, cathepsin D and a collagenolytic enzyme was measured in the sediment as well as in the corresponding lysosomal supernatant. The protein content served as a reference for the enzyme activities. In addition, we investigated the activities of cytoplasmic enzymes such as GOT, GPT, gamma-GT and the alkaline phosphatase. The enzyme activity changes were age-dependent. With Furosemid treatment the activities of beta-glucuronidase and cathepsin D increased in the lysosomal supernatant and the lysosomal sediment of the 1-year old rats, whereas the activities of the collagenolytic enzyme increased in the lysosomal sediment of the same group. In the lysosomal sediment of the 10-weeks old rats a decrease of beta-glucuronidase, beta-acetylglucosaminidase and cathepsin D was observed. These results are discussed in the light of reports from the literature.
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PMID:[Age-dependent biochemical studies on the extrarenal effect of furosemid (author's transl)]. 16 81


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