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)

Streptozotocin treatment (125 mg/kg) in the Chinese hamster induced hyperglycaemia, hypoinsulinaemia, hyperglucagonaemia and changes in body, liver, pancreas, stomach, kidney and adipose tissue weights. The pancreatic reserves of insulin and glucagon in the diabetic animals were low, but stomach glucagon high. These animals showed high levels of phosphoenolpyruvate carboxykinase and low levels of glucokinase, hexokinase, isocitrate dehydrogenase and malic enzyme, but normal levels of pyruvate kinase in the liver. Increases in lactate dehydrogenase subunit B and isozymes 2, 3 and 4 were also observed in the liver, but not in the epididymal fat pad, of the diabetic animals. N-Acetyl-beta-D-glucosaminidase was elevated in plasma, liver and heart, but not in the kidney of the treated animals. Renal alpha-galactosidase and beta-glucosidase were depressed, whereas beta-galactosidase and alpha-glucosidase remained essentially normal. These features indicated that there were considerable differences between the biochemical disorders associated with streptozotocin-diabetes in the Chinese hamster and the published observations in the rat.
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PMID:Streptozotocin-induced diabetes in the Chinese hamster. Biochemical and endocrine disorders. 59 Jun 51

Mannostatin A is a metabolite produced by the microorganism Streptoverticillium verticillus and reported to be a potent competitive inhibitor of rat epididymal alpha-mannosidase. When tested against a number of other arylglycosidases, mannostatin A was inactive toward alpha- and beta-glucosidase and galactosidase as well as beta-mannosidase, but it was a potent inhibitor of jack bean, mung bean, and rat liver lysosomal alpha-mannosidases, with estimated IC50's of 70 nM, 450 nM, and 160 nM, respectively. The type of inhibition was competitive in nature. This compound also proved to be an effective competitive inhibitor of the glycoprotein-processing enzyme mannosidase II (IC50 of about 10-15 nM with p-nitrophenyl alpha-D-mannopyranoside as substrate, and about 90 nM with [3H]mannose-labeled GlcNAc-Man5GlcNAc as substrate). However, it was virtually inactive toward mannosidase I. The N-acetylated derivative of mannostatin A had no inhibitory activity. In cell culture studies, mannostatin A also proved to be a potent inhibitor of glycoprotein processing. Thus, in influenza virus infected Madin Darby canine kidney (MDCK) cells, mannostatin A blocked the normal formation of complex types of oligosaccharides on the viral glycoproteins and caused the accumulation of hybrid types of oligosaccharides. This observation is in keeping with other data which indicate that the site of action of mannostatin A is mannosidase II. Thus, mannostatin A represents the first nonalkaloidal processing inhibitor and adds to the growing list of chemical structures that can have important biological activity.
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PMID:Mannostatin A, a new glycoprotein-processing inhibitor. 227 38

Rat spermatozoa were recovered from the caput, corpus, and cauda epididymides and assayed for glycosidase activity, total nonamino (neutral) carbohydrate, and protein content. The activities of beta-glucosidase, beta-galactosidase, beta-N-acetylglucosaminidase, and beta-N-acetylgalactosaminidase were fluorometrically assayed in spermatozoa and membrane-enriched fractions. Except for beta-glucosidase, the activities of the glycosidases based on protein content were greatest in whole sperm and membrane-enriched fractions obtained from the cauda epididymides. Based on sperm concentration, however, glycosidase activities increased proceeding from the caput to the corpus epididymides, then declined from the corpus to the cauda epididymides. Analyses of nonamino carbohydrate and protein content based on sperm number indicated regional trends similar to those of glycosidase activity. Total nonamino carbohydrate and protein content were highest in corpus sperm, and lowest in cauda sperm. These data indicate major quantitative changes in cell surface carbohydrate as spermatozoa traverse the epididymis. A positive correlation for the membrane-enriched fraction between increasing glycosidase activity and decreasing carbohydrate and protein content suggests that glycosidases may play a significant role in modifying the spermatozoon surface during epididymal transit and maturation.
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PMID:Changes in rat sperm membrane glycosidase activities and carbohydrate and protein contents associated with epididymal transit. 359 43

The activity levels of beta-N-acetylglucosaminidase, beta-N-acetylgalactosaminidase, beta-galactosidase and beta-glucosidase were fluorometrically assessed in spermatozoa, principal cells, basal cells and fibroblasts isolated from the rat epididymis by centrifugal elutriation. Among the various cell types, corpus principal cells had the highest activities for beta-N-acetylglucosaminidase, beta-N-acetylgalactosaminidase and beta-galactosidase. These enzymes characteristically react with membrane structural carbohydrates. Corpus/caput principal cell activity ratios of these glycosidases remained constant when determinations were done at an alternate pH and substrate concentration, suggesting that similar enzyme forms were present in both regions. Based on cell number and cell volume, sperm glycosidase activities generally increased from the caput to the corpus region of the epididymis, while decreasing from corpus to cauda. However, when data were expressed on the basis of cell protein, sperm glycosidase activities increased from caput to cauda. Since the total protein of sperm decreases dramatically from caput to cauda, the increase in glycosidase activity based on total protein suggests that relative to other sperm proteins, glycosidases may be selectively retained or taken up during epididymal transit. High levels of glycosidase activity associated with the corpus epididymidis may contribute to modification of sperm glycoproteins and observed increases in fertility of sperm as they emerge from this region.
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PMID:Glycosidase activities in principal cells, basal cells, fibroblasts and spermatozoa isolated from the rat epididymis. 643 54

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

Activity of glycosidases in the epididymis was influenced by several factors originating in the testis. Activities of all the three glycosidases studied viz., beta-glucosidase, beta-galactosidase and alpha-mannosidase were found to be significantly lower in the epididymis of orchidectomized animals than in sham operated rats. However, an enhanced activity of epididymal beta-galactosidase and alpha-mannosidase was noticed in prolactin treated orchidectomized rats compared to orchidectomized rats given vehicle alone. On the other hand, activity of these two enzymes in bromocriptine treated orchidectomized rats was even lower than that found in orchidectomized rats given vehicle. Neither prolactin nor bromocriptine treatment had any significant influence on the epididymal beta-glucosidase. The results suggest a selective but definite action of prolactin on epididymal glycosidases.
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PMID:Modulation in activity of some epididymal glycosidases by prolactin. 835 47

The impact of hyperthyroidism on epididymal glycosidases was studied in albino rats. Hyperthyroidism was induced in Wistar rats aged 30 days by daily injection of T4 (25 microg/100 g body weight/day intramuscularly) for 30 or 60 days; control rats were injected with vehicle (alkaline saline, pH 7.8). One set of hyperthyroid rats was reverted to euthyroid status by withdrawing T4 treatment after 30 days of hyperthyroidism. To asses the direct effect of thyroid hormone on epididymal hexosaminidases, caput, corpus and cauda tissues were stimulated with 25, 50 or 100 ng/mL T3 for 24 h, after an initial culture of 24 h. The activity of beta-glucosidase decreased in caput, corpus and cauda epididymis of hyperthyroid rats. beta-Galactosidase activity increased in the caput epididymis irrespective of the duration of hyperthyroidism. While a similar decrease occurred in the corpus and cauda epididymis in the 30 day hyperthyroid group, an opposite trend was observed in 60 day hyperthyroid rats. Caput beta-N-acetylglucosaminidase activities increased at both time points, whereas activity decreased in the corpus and cauda in 30 day, but increased in 60 day hyperthyroid rats. Hyperthyroidism consistently increased caput and corpus beta-N-acetylgalactosaminidase activity irrespective of the duration. Cauda epididymal beta-N-acetylgalactosaminidase activity was decreased in 30 day and increased in 60 day hyperthyroid rats. Hyperthyroidism induced changes in caput beta-galactosidase, beta-N-acetylgalactosaminidases, corpus beta-N-acetylglucosaminidase and cauda beta-N-acetylgalactosaminidase which were irreversible while the remaining actvities were brought back to normal when T4 treatment was withdrawn. In vitro studies showed that T3 stimulates epididymal hexosaminidases (beta-N-acetylglucosaminidase and beta-N-acetylgalactosaminidase) irrespective of the dose. These data suggest that thyroid hormones have a specific and direct influence on glycosidases in specific regions of the epididymis.
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PMID:Differential effect of hyperthyroidism on rat epididymal glycosidases. 1145 72