Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Castanospermine (1,6,7,8-tetrahydroxyoctahydroindolizine) was tested against a variety of commercially available glycosidases and found to be a potent inhibitor of almond emulsin beta-glucosidase, and also to inhibit fungal beta-xylosidase. This alkaloid was inactive on yeast alpha-glucosidase, alpha- or beta-galactosidase, alpha-mannosidase, beta-N-acetylhexosaminidase, beta-glucuronidase, alpha-L-fucosidase. Fifty-percent inhibition of beta-glucosidase required about 10 micrograms/ml of castanospermine. The amount of inhibition was uniform throughout the time course, and the inhibition with regard to substrate concentration (p-nitrophenyl-beta-D-glucopyranoside) appeared to be of the mixed type. Castanospermine was also a potent inhibitor of beta-glucocerebrosidase when assayed with fibroblast extracts using either a fluorimetric or a radioactive assay. Interestingly enough, castanospermine also inhibited the lysosomal alpha-glucosidase, and this inhibition required comparable levels of alkaloid to that required for inhibition of beta-glucocerebrosidase. However, a number of other lysosomal glycosidases were not sensitive to castanospermine (i.e., alpha- or beta-galactosidase, alpha- or beta-mannosidase, alpha- or beta-L-fucosidase, beta-N-acetylhexosaminidase, beta-glucuronidase).
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PMID:Castanospermine, a tetrahydroxylated alkaloid that inhibits beta-glucosidase and beta-glucocerebrosidase. 640 22

Changes in the activities of several lysosomal enzymes were studied during transformation of mouse spleen cells in vitro. The activity of beta-glucuronidase increased during culture in the presence of T or B-cell mitogens, and lymphoblasts contained higher levels of activity than did small, non-transformed lymphocytes. Moreover, lymphoblasts in well-transformed cultures had higher activities than those in poorly-transformed cultures. The activities of other lysosomal enzymes (N-acetyl-beta-glucosaminidase, alpha-mannosidase, beta-glucosidase) also increased during mitogenic stimulation, but each at different rates, although aryl sulphatase was unaffected. Such differences may be of importance when lymphocytes are used for diagnosis of inherited lysosomal deficiency diseases.
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PMID:Effects of mitogenic stimulation of lymphocytes on lysosomal enzyme activity. 643 92

In platelets of subjects affected with myeloproliferative disorders the following lysosomal enzymes were studied: alpha-mannosidase, alpha-fucosidase, beta-galactosidase, beta-glucosidase, beta-glucuronidase, beta-N-acetylglucosaminidase and acid phosphatase. For each enzyme the specific activity, the optimum of pH and buffer, Km and saturating substrate concentrations, as well as thermostability were determined. Control and patient enzymes showed no difference.
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PMID:Platelet lysosomal enzymes are normal in myeloproliferative disorders. 643 83

A new aminosugar named nojirimycin B (1) has been isolated as its bisulfite adduct from the culture broth of Streptomyces lavendulae SF-425, together with nojirimycin. Microbiological oxidation of 1 with Gluconobacter suboxydans IAM 1829 gave a delta-lactam (2). The structures of 1 and 2 were determined to be 5-amino-5-deoxy-D-mannopyranose and D-mannonic-delta-lactam, respectively, on the basis of 1H NMR spectroscopy and X-ray structural analysis. Both 1 and 2 exhibited powerful inhibitory activity against rat epididymal alpha-mannosidase and apricot beta-glucosidase.
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PMID:Novel glycosidase inhibitors, nojirimycin B and D-mannonic-delta-lactam. Isolation, structure determination and biological property. 654 15

Liver fibrosis was produced in rats by subcutaneous injections of carbon tetrachloride. The effect of anti-inflammatory steroids (hydrocortisone, prednisone, dexamethasone) on the activity of serum lysosomal hydrolases (beta-N-acetylglucosaminidase, beta-glucosidase and alpha-mannosidase) was investigated in healthy and CCl4 poisoned rats. The marked increase of enzymatic activity in blood serum was observed in animals with CCl4-induced liver fibrosis. Quite opposite results were found in normal rats treated with glucocorticosteroids. In rats which were given both carbon tetrachloride and corticosteroids the obtained values of serum enzymatic activity did not have a uniform character as compared to controls or CCl4 intoxicated rats. Presumable mechanisms of the results obtained are discussed.
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PMID:Effect of anti-inflammatory steroids on the activity of selected lysosomal hydrolases in serum of rats with experimental liver fibrosis. 668 81

Studies have been carried out on the activities and properties of the isozymes of alpha-mannosidase, alpha-glucosidase and beta-glucosidase in granulocytes, monocytes, lymphocytes and platelts from peripheral blood of heatlhy adult donors. The findings reveal the differences in activities as well as a characteristic distribution of the different molecular forms of these lysosomal hydrolases in specific cell types. Therefore, the results obtained with unfractionated total leukocyte smples from different subjects may vary according to the distribution of cell types in the circulation. Granulocytes and monocytes show only the acid alpha-mannosidase activity whereas lymphocytes and platelets show both acid and neutral activities. The specific activity of acid alpha-mannosidase in granulocytes and monocytes is higher than in lymphocytes and platelets. By DEAE-cellulose chromatography, the acid alpha-mannosidase in granulocyte and monocyte extracts elutes as two peaks, but only one peak is seen in lymphocytes. All cell types show both acid and neutral alpha-glucosidase activities. The specific activities of both isozymes are higher in granulocytes and monocytes than in lymphocytes and platelets. Monocytes show a higher acid than neutral activity. All other cell types show a higher neutral activity. Beta-Glucosidase in all cell types is mainly membrane-bound and it can be released by Triton X-100 and sodium taurocholate. Taurocholate also stimulates the beta-glucosidase activity of granulocytes, monocytes and lymphocytes whereas it inhibits the activity of this enzyme in platelets. These results indicate that variations in the total number of leukocytes and in the relative proportion of the various cell types in health and disease may yield inconsistent or unreliable values for enzyme activity in the diagnosis of lysosomal storage disease and in carrier detection.
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PMID:Studies on the activities and properties of lysosomal hydrolases in fractionated populations of human peripheral blood cells. 676 26

Several lysosomal glycosidase activities were examined in vitro during heat-induced germination of Dictyostelium discoideum spores and were found not to be coordinately controlled. The level of beta-glucosidase activity increased significantly during the emergence stage of germination. Both alpha-glucosidase and N-acetyl-beta-glucosaminidase activities remained relatively constant until postemergence, when they increased slightly; alpha-mannosidase activity decreased during all stages of germination. The activity of beta-galactosidase increased slightly during spore swelling, fell below the level initially found in spores at zero time, and increased slightly during postemergence. The expression of all of these enzyme activities, except the increase in beta-galactosidase, appeared to require protein synthesis. Spores in the lag phase of germination which were exposed to severe environmental stress were deactivated and exhibited reduced levels of alpha-glucosidase, beta-glucosidase, and N-acetyl-beta-glucosaminidase activities. Prolonged heat activation treatment reduced the levels of lysosomal glycosidase activities in postactivated spores but did not change the subsequent enzyme patterns during the spore-swelling and emergence stages of germination.
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PMID:Expression of glycosidase activities during germination of Dictyostelium discoideum spores. 676 80

The present study examines the role of cardiac lysosomal enzymes in the pathogenesis of the cardiomyopathy that develops in genetically diabetic C57BL/KsJ db+/db+ mice. Db+/db+ mice and littermate controls were sacrificed as age-matched pairs between 5-26 weeks of age. C57BL/6J ob/ob mice and littermates served as other controls. The hearts were excised, homogenized, and the following enzymatic activities measured: N-Acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-glucosaminidase, aryl sulphatase, alpha-mannosidase, alpha-glucosidase, beta-galactosidase, beta glucosidase, total p-nitrophenyl phosphatase, acid phosphatase and 5'-phosphodiesterase type IV. There is a progressive decrease in cardiac lysosomal enzyme activities of db+/db+ mice for the period 5-21 weeks of age. All enzyme activity is depressed significantly during the 9-21 week interval with beta-glucuronidase, aryl sulphatase and beta-glucosidase decreased about 40-50%. The decrease in lysosomal enzyme activity can explain the accumulation of large residual bodies and interstitial material in the myocardium of the db+/db+ animals
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PMID:Lysosomal enzymes in experimental diabetic cardiomyopathy. 678 Feb 37

Several glycosidase activities were measured in frontal gray matter of 4 brains from subjects affected by Creutzfeldt-Jakob disease. The changes of N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-glucosidase, alpha-fucosidase and alpha-mannosidase were not statistically significant but significant increases of beta-glucuronidase and beta-galactosidase activities were found. These results are in accordance with several reports on brain glycosidases in scrapie and Semliki Forest virus-infected brain and could explain some changes in brain glycoconjugate content previously observed in human and experimental Creutzfeldt-Jakob disease.
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PMID:Brain glycosidases in Creutzfeldt-Jakob disease. 678 37

Nine lysosomal enzymes and alkaline phosphatase have been assayed in human pancreatic juice from controls and patients with chronic calcifying pancreatitis. Specific activities were evaluated by a nonparametric test (Wilcoxon) with a probability of 2 P less than or equal to 0.5. The values of acid phosphatase, alpha-glucosidase, beta-glucosidase and alpha-galactosidase are significantly higher in pathological juices; the values of alpha-mannosidase and beta-glucuronidase are also increased in the same patients but at the limit of significance. Alkaline phosphatase, beta-hexosaminidase and alpha-fucosidase follows the same trend but the values are not statistically significant between the two groups of patients. Studies on skin cultures of four patients with chronic calcifying pancreatitis demonstrate that the increased specific activities of lysosomal enzymes in the pathological juices do not correspond to a leakage of these enzymes into the extracellular space as described for cystic fibrosis.
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PMID:Alkaline phosphatase and acid lysosomal hydrolases in pancreatic juice and fibroblast cell cultures of patients with chronic calcifying pancreatitis. 680 85


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