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)

In the paper we observed histochemically the distribution and activity of 16 enzymes in the normal rat gastric mucosa. The lysosomal enzymes were demonstrated by the method of semipermeable membranes (LOJDA 1972). At the proof of dehydrogenases aqueous and gel media were used. The parietal cells of the gastric mucosa contained a moderate activity of acid phosphatase, E-600 resistant esterase, and only a very slight activity of beta-glucuronidase and N-acetyl-beta-D-glucosaminidase. The macrophages of the interstice contained a high activity of beta-glucruonidase, acid phosphatase, E-600 resistant esterase and a low activity of N-acetyl-beta-D-glucosaminidase. The chief cells of the rat gastric mucosa, in contrast to the human, did not contain nonspecific esterase and also in them acid phosphatase was mostly lacking. The alkaline phosphatase was found only in the endothelium of the capillaries of the gastric mucosa. The parietal cells contained high activities of succinate dehydrogenase, alpha-glycerophosphate dehydrogenase, beta-hydroxybutyrate dehydrogenase, NADH tetrazolium reductase, a lower activity of NADPH tetrazolium reductase, as well as other soluable dehydrogenases. At the examination of dehydrogenases using aqueous as well as gel media with PMS during optimal short incubation periods, we found more and less active forms of parietal cells. The different oxidoreductase capacity of parietal cells in normal rat gastric mucosa can point to their unequal-functional load at the production of hydrochloric acid. The findings obtained are compared with the findings in older papers concerning different experimental animals and with the distribution of enzymes in the human gastric mucosa.
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PMID:Histochemical localization of enzymes in the normal rat gastric mucosa using the technique of the semipermeable membranes and the other methods. 82 7

Some enzymatic activities have been assayed in the gastrocnemius muscle of patients with obstructive arteriopathy of the lower limbs. The specific activities of all the examined glycolytic enzymes, of malate dehydrogenase and of glycerol-3-phosphate dehydrogenase are significantly decreased while the specific activities of two lysosomal enzymes, beta-glucuronidase and cathepsin A, are significantly higher than in the controls. Therefore it may be inferred that the metabolic capacity of glycolysis and of Krebs cycle are lowered. On the other hand the increased specific activity of lysosomal enzymes suggests the hypothesis that the above mentioned modifications and the morphologic alterations of the muscle and of the small blood vessels might be ascribed, at least partly, to a release of lysosomal hydrolases in active form.
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PMID:Changes in enzyme levels in human skeletal muscle during obstructive arteriopathy of the lower limbs. 105 91

Immunocytochemical analysis of aggregation chimeras made using either of the mutants, Lurcher or Purkinje cell degeneration, previously showed that only Bergmann glia close to surviving Purkinje cells expressed an apparently normal level of the enzyme, glycerol-3-phosphate dehydrogenase (GPDH) (Fisher and Mullen, 1988). In the present study, aggregation chimeras were made using embryos from a B6D2 hybrid mouse strain carrying the Lurcher (Lc/+) mutation and homozygous for an allele specifying a high level of beta-glucuronidase activity and embryos from a wild-type C3H strain with low beta-glucuronidase activity. Chimeric cerebella were analyzed immunocytochemically and histochemically to determine whether Lurcher mutant Bergmann glia could express a normal, high level of GPDH. Comparisons between pairs of alternately stained, 2 microns thick serial sections showed that Bergmann glia with high level of beta-glucuronidase (i.e., Lurcher) expressed normal GPDH immunoreactivity only when close to surviving, wild-type Purkinje cells. Interestingly, in Purkinje cell-free areas of cerebellar cortex that were sufficiently large that GPDH expression was diminished, Bergmann glia also showed a reduced level of histochemically detectable beta-glucuronidase activity, as do Bergmann glia in adult Lc/+ mice. The results indicate that Lc/+ mutant Bergmann glia are not intrinsically defective with regard to expression of the enzymes, GPDH and beta-glucuronidase, but rather, expression of these enzymes depends on glial interaction with wild-type Purkinje cells.
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PMID:Chimeric analysis of the site of Lurcher gene action with respect to glial enzyme expression. 235 67

Variations in specific activities of the marker enzymes of Sertoli and germ cells during breeding (November-December) and non-breeding (May-June) seasons were investigated in rhesus and bonnet monkeys maintained under laboratory conditions. The marker enzymes selected for testicular cells were-Sertoli cells: beta-glucuronidase, gamma-glutamyl transpeptidase; pre-meiotic germ cells: glucose 6-phosphate dehydrogenase, malate dehydrogenase, alpha-glycerophosphate dehydrogenase; mature germ cells: LDH-X, sorbitol dehydrogenase. Results have indicated significant seasonal variation in marker enzymes only in rhesus testis. Marker enzymes of Sertoli cell increased while those of germ cell decreased significantly during non-breeding season. Marker enzymes of mature germ cells were affected much more drastically than those of the pre-meiotic germ cells.
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PMID:Seasonal variations in Sertoli and germ cell marker enzymes in testis of rhesus and bonnet monkeys. 937 24

The Aspergillus nidulans high-osmolarity glycerol response (AnHOG) pathway is involved in osmoadaptation. We found that fludioxonil, a fungicide, causes improper activation of HogA mitogen-activated protein kinase (MAPK) in A. nidulans. Here we present novel reporter systems for monitoring activation of the AnHOG pathway. The promoter region of gfdB (glycerol-3-phosphate dehydrogenase), whose expression depends on the presence of HogA, was fused to a beta-glucuronidase uidA gene (GUS) to construct the reporter, which was introduced into A. nidulans wild type and hogADelta. Increased GUS activity was detected in the wild type only when it was treated with high osmolarity or fludioxonil, while reporter activity was scarcely stimulated in the hogADelta mutant. These results indicate that the reporter activity is controlled via HogA activation. Furthermore, we present possible applications of the reporter systems in screening new antifungal compounds.
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PMID:Novel reporter gene expression systems for monitoring activation of the Aspergillus nidulans HOG pathway. 1761 16