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)

The release of acid hydrolases from cultured skin fibroblasts into the cell culture medium was studied in several lysosomal storage disorders (GM1-gangliosidosis, Fabry's disease, Hurler's disease, mannosidosis, and mucolipidosis). The levels of different activities were proportional to time (up to 44 h after medium change) and cell density with the exception of beta-glucosidase, which was not released. Culture medium from the fibroblasts of mucolipidosis patients exhibited higher activity of acid hydrolases than medium from cells of patients with GM1-gangliosidosis, Fabry's disease, Hurler's disease, and mannosidosis. These cells, however, exhibited somewhat higher levels of enzyme activity in their culture medium than control fibroblasts. The total production of acid hydrolases was yet rather similar in fibroblasts from controls and patients. Differential centrifugation showed that the highest specific activity of acid hydrolases was seen, as expected, in the lysosomal fraction, except in fibroblasts from patients with mucolipidosis, where the supernatant exhibited most activity. beta-Glucosidase, however, showed a normal differential centrifugation pattern also in fibroblasts from these patients.
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PMID:Lysosomal enzymes in medium from cultured skin fibroblasts from normal individuals and patients with lysosomal diseases. 40 77

The sugars present in hydrolyzed extracts of human liver and brain were analyzed by gasliquid chromatography after conversion to their alditol acetates. The samples analyzed were obtained from control subjects, patients with gargoylism, and patients with a few other kinds of storage disorders. Accumulation of galactose was demonstrated in the liver and the brain of two patients with gargoylism, and in the liver samples, high levels of mannose were found too. We also studied the hydrolysis of a number of galactosides by homogenates from different tissues in the control subjects and in the patients. Separation methods and kinetic studies demonstrated the presence in normal human tissues of two different beta-galactosidases, which we call enzyme A and enzyme B, respectively. Enzyme A hydrolyzed all the beta-galactosides tested. Enzyme B hydrolyzed the synthetic substrates tested (4-methylumbelliferyl-, p-nitrophenyl-, o-nitrophenyl-, and phenyl-beta-galactoside) but not the natural substrates tested (ceramide-beta-galactoside, ceramide lactoside, transferrin glycopeptide, and keratan sulfate). Enzyme B also exerted beta-glucosidase activity. In various tissues from patients with gargoylism, deficiency of beta-galactosidase A could be demonstrated. It is suggested that the high level of galactose found in the hydrolyzed extracts of tissues from gargoylism patients is due to storage of galactose-rich glycosaminoglycans and glycopeptides, and that this storage is a result of the deficiency of beta-galactosidase A. The high level of mannose in the liver from gargoylism patients seems to indicate storage of glycopeptide, adding a new group of substances to those known to be stored in gargoylism.
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PMID:Gargoylism: hydrolysis of beta-galactosides and tissure accumulation of galactose- and mannose-containing compounds. 498 60

We performed a biochemical study on the patient with mucolipidosis III (ML-III, pseudo-Hurler polydystrophy) in Korea. Confluent fibroblasts from the patient and from normal controls were cultured for 4, 12, 24, 48, and 72 hr, respectively. Lysosomal enzyme activities in culture media after different incubation times and in plasma, leuko-cytes, and fibroblasts were determined. Most of the leukocyte lysosomal enzymes were within normal limits or slightly lowered; however, plasma lysosomal enzyme activities such as those of hexosaminidase and arylsulfatase A were markedly increased. Numerous phase-dense inclusions were present in the cytoplasm of cultured fibroblasts. Lysosomal enzyme activities of fibroblasts were markedly decreased except for beta-glucosidase. The rates of increase of the lysosomal enzyme activities with incubation time were greater in the culture medium of the patient than in normal control, whereas no difference in the beta-glucosidase activity of the culture media of the patient and the control was found. This study describes the first case of ML-III in Korea, with its typical biochemical characteristics, i.e., a problem with targeting and transporting of lysosomal enzymes which results in a marked increase in plasma lysosomal enzyme activities and a high ratio of extracellular to intracellular lysosomal enzyme activities in cultured fibroblasts.
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PMID:Biochemical characteristics of a Korean patient with mucolipidosis III (pseudo-Hurler polydystrophy). 1455 27