Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the newborn lamb, activities of lysosomal enzymes are lower in the duodenum and jejunum than in the ileum. In contrast, there are only minor differences, if any, in activities of lysosomal enzymes between the regions of the small intestine of 5-day-old lambs. In the duodenum, jejunum and ileum, activities of hexosaminidase, alpha-mannosidase, beta-mannosidase, alpha-L-fucosidase and phosphodiesterase are greater in newborn than in 5-day-old lambs. Only in the distal part of the small intestine are activities of beta-glucuronidase, alpha-glucosidase, alpha-galactosidase, beta-galactosidase, acid phosphatase and cathepsin B higher in the newborn than in 5-day-old lambs. Cathepsin B activity is lower in the duodenum and jejunum of the newborn than in 5-day-old lambs.
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PMID:Lysosomal enzymes in the intestine of the newborn lamb. 609 93

Human lymphocytes were isolated from defibrinated blood by Ficoll-Hypaque centrifugation with erythrocyte hypotonic lysis. Homogenates of mixed lymphocytes were subjected to analytical subcellular fractionation by sucrose gradient centrifugation in a Beaufay automatic zonal rotor. The principal organelles were characterized by their marker enzymes: cytosol (lactate dehydrogenase), plasma membrane (5'-nucleotidase), endoplasmic reticulum (neutral alpha-glucosidase), mitochondria (malate dehydrogenase), lysosomes (N-acetyl-beta-glucosaminidase), peroxisomes (catalase). gamma-Glutamyl transferase was exclusively localized to the plasma membrane. Leucine amino-peptidase, especially when assayed in the presence of Co2+, was also partially localized to the plasma membrane. Experiments with diazotized sulphanilic acid, a non-permeant enzyme inhibitor, showed that these plasma membrane enzymes are present on the cell surface. No detectable alkaline phosphatase was found in the lymphocytes. Acid phosphatase and beta-glucuronidase were localized to lysosomes and there was some evidence for lysosomal heterogeneity. Leucine amino peptidase, optimal at pH 8.0, showed a partial localization to intracellular vesicles, possibly lysosomes, especially when assayed in the presence of EDTA. These studies provide a technique for determining the intracellular distribution of hitherto unassigned lymphocyte constituents and serve as a basis for investigating the cell pathology of lymphocytic disorders.
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PMID:Enzyme analysis and subcellular fractionation of human peripheral blood lymphocytes with special reference to the localization of putative plasma membrane enzymes. 614 55

Glycosidase activities in the adults and juveniles of the lung fluke Paragonimus ohirai and P. westermani adults were demonstrated histochemically. For comparative studies, histochemical examination was also made on the adults of the liver fluke Fasciola hepatica. The enzymes examined were N-acetyl-beta-glucosaminidase (EC 3.2.1.30), beta-glucuronidase (EC 3.2.1.31), beta-galactosidase (EC 3.2.1.23), alpha-glucosidase (EC 3.2.1.20) and beta-glucosidase (EC 3.2.1.21). The distribution of beta-glucosaminidase was similar in juveniles and adults. Strong reaction sites for the enzyme were the caecal brush border, tegument, subtegumental cells and tests. In contrast, no staining reaction occurred in the caeca of F. hepatica, although the tegument and parenchymal cells were weakly stained. beta-glucuronidase activity was associated only with the luminal surface of the caeca in the juveniles. However, luminal contents also appeared stained and this might suggest that the activity in the caeca is not endogenous. beta-galactosidase was localized in the caeca, sub-tegmental cells and tegument in both juveniles and adults. No reaction occurred for the other two enzymes, alpha- and beta-glucosidase.
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PMID:Histochemical studies of glycosidase activity in juveniles and adults of the lung fluke Paragonimus. 622 Feb 58

The enzyme activities of alpha-fucosidase (pH 4.0 and pH 5.5), alpha-galactosidase, beta-galactosidase, alpha-glucosidase (pH 4.5 and pH 6.0), beta-glucosidase, beta-glucuronidase, beta-hexosaminidase, and alpha-mannosidase (pH 4.5 and pH 5.5) were investigated in sera from cystic fibrosis (CF) patients. Several of these activities were significantly increased in sera from patients compared to age-matched control children. CF-patients in a more advanced stage of the disease had a tendency to higher values of some of these hydrolases than those in better condition. No new isoenzymes of these hydrolases were found. Only minor differences could be detected in the pH-profiles of alpha-mannosidase and acid phosphatase from age-matched normal controls, heterozygotes and homozygotes for CF. With our technique, alpha-mannosidase and acid phosphatase showed the same thermostability in CF-patients. CF-heterozygotes and age-matched controls, except at 56 degrees C, when the activity of acid-phosphatase in the plasma from adult CF-heterozygotes decreased more than that from adult controls
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PMID:Acid hydrolases in sera and plasma from patients with cystic fibrosis. 626 20

Like most psychoactive agents, cannabis and its active component delta-9-tetrahydrocannabinol (delta 9-THC) have been reported to affect the neuroendocrine axis in animals. The effect of delta 9-THC on some of the functionally important enzymes of the male reproductive organs are reported. The study indicates that delta 9-THC reduces the activities of the enzymes, beta-glucuronidase, alpha-glucosidase acid phosphatase and fructose-6-phosphatase in a dose related manner in the testis, prostate as well as in the epididymis. It may be concluded that delta 9-THC may interfere with the normal functioning of the male reproductive organs.
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PMID:Enzymatic changes in the male reproductive organs by delta-9-tetrahydrocannabinol. 628 Jul 29

Circulating non-T lymphocytes had higher activities of 5'nucleotidase (plasma membrane), neutral alpha-glucosidase (endoplasmic reticulum) and basal leucine amino-peptidase than did T lymphocytes. Activities of catalase (peroxisomes), malate dehydrogenase (mitochondria), lactate dehydrogenase (cytosol) and N-acetyl-beta-glucosaminidase, beta-glucuronidase and acid phosphatase (lysosomes), were similar in the lymphocyte subfractions. Lymphocyte 5'nucleotidase (plasma membrane) in patients with common variable hypogammaglobulinaemia is much lower than normal. However, the decrease is less marked in X-linked hypogammaglobulinaemia, chronic lymphatic leukaemia or protein loosing enteropathy or in lymphocytes isolated from cord blood. Cells from patients with nephrotic syndrome had normal levels of 5'nucleotidase. Other plasma membrane marker enzymes (gamma-glutamyl transferase, leucine amino-peptidase) were normal in lymphocytes from patients with common variable hypogammaglobulinaemia. There is a selective reduction of mitochondrial (malate dehydrogenase) and cytosolic (lactate dehydrogenase) enzymes, with normal activities of lysosomal, peroxisomal and endoplasmic reticulum enzymes, in patients with common variable hypogammaglobulinaemia. The lymphocyte subcellular organelles in normal subjects and patients with common variable hypogammaglobulinaemia have similar properties on sucrose density gradient centrifugation. It is suggested that lymphocytes from patients with common variable hypogammaglobulinaemia show a specific enzymopathy and that this is not simply a reflection of cellular immaturity.
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PMID:Lymphocyte enzyme activities in immunodeficiency syndromes with particular reference to common variable hypogammaglobulinaemia. 630 45

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

Mouse peritoneal macrophages that had been treated with a monovalent carboxylic ionophore, monensin, selectively secreted lysosomal and nonlysosomal granular enzymes into the medium. When macrophages were incubated with 1 to 10 microM monensin, the release of beta-glucuronidase, beta-hexosaminidase and beta-galactosidase was stimulated time and does dependently. Neither the beta-glucosidase nor acid phosphatase, enzymes bound to the lysosomal membranes, however, were released by monensin. Neutral alpha-glucosidase, shown recently to be localized in nonlysosomal granules of macrophages (15), was released by monensin at concentrations lower than those required for lysosomal enzyme release. Increased release of lysosomal enzymes also took place in a manner similar to that seen with monensin-treated macrophages after treatment of macrophages with weak bases, chloroquine and ammonium chloride. Neutral alpha-glucosidase, however, was not released when chloroquine was present in concentrations that stimulated the release of lysosomal enzymes. The UDP-galactosyltransferase activity of the Golgi apparatus in the macrophages markedly decreased after treatment with low concentration of monensin.
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PMID:Stimulation of the release of lysosomal and nonlysosomal granular enzymes from macrophages treated with monensin. 643 21

Chorionic villi from first trimester and term human placentas have been incubated in vitro and shown to release the lysosomal enzymes, beta-hexosaminidase, alpha-glucosidase and beta-glucuronidase. There was negligible release of the cytoplasmic enzyme, lactate dehydrogenase, under the same conditions. The first trimester villi released proportionally more of their lysosomal enzyme content than did the term villi. Extracellular levels of beta-hexosaminidase were raised and those of alpha-glucosidase and beta-glucuronidase were lowered when tissue was incubated with 1 microM colchicine, suggesting that microtubules are involved in the control of lysosomal enzyme release from placental villi.
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PMID:Secretion of lysosomal enzymes by human placental villi in vitro. 645 98

Ten enzymes, all known to be glycoproteins, were examined by electrophoresis or gel isoelectric focusing in 12 different patients with primary or secondary sialidase deficiency. Aberrant electrophoretic mobilities of many of the enzymes attributable to abnormal sialylation were found in all the patients. In ten of the patients seven of the enzymes were affected. The unaffected enzymes were beta-galactosidase, alkaline phosphatase and beta-glucuronidase. In the cells from the two patients with I cell disease (mucolipidosis II) in which sialidase is one of many deficient enzymes, beta-galactosidase, alpha-galactosidase, alpha-fucosidase and alpha-mannosidase were undetectable, alkaline phosphatase showed a normal electrophoretic mobility and acid phosphatase, adenosine deaminase, alpha-glucosidase and beta-D-N-acetylhexosaminidase showed aberrant mobilities.
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PMID:Electrophoretic analysis of glycoprotein enzymes in the sialidoses and mucolipidoses. 645 53


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