Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.9 (glucose-6-phosphatase)
 3,081 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

56 human liver biopsy specimens with insignificant or no histological changes, but with abnormally strong canalicular alkaline phosphatase activity, were studied histochemically for other enzyme changes. In comparison with normal specimens, more extensive and increased canalicular activity of gamma-glutamyl transferase, and increase of canalicular leucine aminopeptidase, was found, while the sinusoidal activity of the latter enzyme was decreased. Staining for adenosine triphosphatase regularly desclosed the normal pattern of sinusoidal and canalicular activity. The lysosomal enzymes, acid phosphatase and beta-glucuronidase, stained more intensely than ordinarily, while the reactions for enzymes present in the cytosol (lactic dehydrogenase), in the mitochondria (succinic dehydrogenase, imonoamine oxidase) and in the endoplasmic reticulum (glucose-6-phosphatase) were normal.
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PMID:On histochemical enzyme changes in association with canalicular activity of alkaline phosphatase in human liver. 24 Dec 3

The present study was undertaken to separate peroxisomes of the dog kidney cortex by the methods of discontinuous sucrose density gradient and zonal centrifugation. The separation of subcellular particles was evaluated by measuring the activities of reference enzymes, beta-glycerophosphatase for lysosomes, succinate dehydrogenase for mitochondria, glucose-6-phosphatase for microsomes, and catalase and D-amino acid oxidase for peroxisomes. The activities of D-amino acid oxidase and catalase were mainly observed in fractions 1 and 2 (1.6 and 1.7 M sucrose) obtained by discontinuous sucrose density-gradient centrifugation. Small amounts of acid phosphatase and succinate dehydrogenase contaminated these fractions. Considerably higher activity of catalase was determined in the supernatant, while D-amino acid oxidase showed a lower activity. By the method of zonal centrifugation, the highest specific activities of catalase and D-amino acid oxidase were found in fraction 50 (1.73 M sucrose) with no succinate dehydrogenase, acid phosphatase or glucose-6-phosphatase activity. These results suggested that peroxisomes of dog kidney cortex were clearly separated in 1.73 M sucrose from mitochondria, lysosomes and microsomes by zonal centrifugation.
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PMID:Isolation of peroxisomes from the dog kidney cortex. 24 25

When lead acetate was administered intraperitoneally to young rats at a dose of 20 mg/kg (five times a week for 6 weeks), their growth rate was retarded when compared with controls injected with sodium acetate. Only a small amount of the heavy metal reached the circulation and exerted limited effects on typical target organs. However, large, electron-dense inclusion bodies were found in the abdominal cavity. The in vivo intestinal absorption of glucose was reduced. When perfused at 40 mM concentration, the experimental animals had a mean absorption rate of 152.1 nmol/min . cm vs. 230.6 in the controls (p less than 0.01). Also, sodium and potassium transport was reduced. No effects were observed on amino acid transport and (Na+-K+)-ATPase. Mg++-ATPase, glucose-6-phosphatase, fructose-1, 6-diphosphatase, pyruvate kinase, succinic dehydrogenase, and tryptophan hydroxylase in the small intestinal mucosa and the kidney were unaltered. Renal alkaline phosphatase was decreased. These studies confirm the greater susceptibility of some active transport mechanisms of the small intestinal mucosa to lead toxicity, compared to those of the kidney.
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PMID:Alterations of intestinal and renal functions in rats after intraperitoneal injections of lead acetate. 46 71

Evidence is presented that the antitumor agent helenalin, a sesquiterpene lactone, suppresses anaerobic glycolytic enzymes of tumor cells at a number of sites and not exclusively at glycogen synthetase and phosphofructokinase, previously proposed sites for inhibition by alpha-methylene-gamma-lactones. Of the enzymes tested, the sulfhydryl-containing enzyme hexokinase was inhibited the maximum, i.e., 83%, by helenalin treatment, whereas phosphofructokinase and glycogen synthetase were suppressed approximately 45%. Another sulfhydryl-bearing enzyme, aldolase, was decreased approximately 43%. Phosphorylase a was inhibited 65%, glucose-6-phosphatase was inhibited 46%, and succinic dehydrogenase was inhibited 59% by helenalin treatment. Mitochondrial oxidative phosphorylation processes were also significantly depressed in the presence of helenalin in vitro with either succinate or alpha-ketoglutarate as substrates. Thus, a number of enzymes of anaerobic and aerobic carbohydrate metabolism of Ehrlich ascites cells appear to be inhibited by helenalin, which supposedly can alkylate functional groups, e.g., sulfhydryl groups of these enzymes, by a rapid Michael-type addition.
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PMID:Antitumor agents XXVII: Effects of helenalin on anaerobic and aerobic metabolism of Ehrlich ascites cells. 64 68

An analysis of starvation and starvation followed by refeeding was undertaken to characterize some organismic, organ, and mitochondrial responses to these two circumstances. Body weight, organismic respiration as well as weight protein and succinic dehydrogenase activity for liver, kidney, and heart were determined over the course of 6 days of starvation and 5 days refeeding for adult male rats. Assays of marker enzyme activities for mitochondria (cytochrome oxidase), lysosomes (acid phosphatase), endoplasmic reticulum (glucose-6-phosphatase), and plasma membranes (5'-nucleotidase) were conducted for liver in addition to quantitations of mitochondrial protein. All enzyme determinations were done on whole tissue homogenates and reported as total organ activity. Liver mitochondria were harvested quantitatively directly from whole liver homogenates by zonal centrifugation for determination of mitochondrial protein. Starvation resulted in a major loss of body weight, organ weight, and organ protein; liver greater than kidney greater than heart. These changes were accompanied by a major reduction in organ succinic dehydrogenase activity; liver greater than kidney. In heart, succinic dehydrogenase was doubled in activity at day 2 of starvation and subsequently diminished to values not significantly lower than controls. In liver, mitochondrial mass (protein) was severely diminished. From analysis of marker enzyme activities, it appeared that lysosomes, endoplasmic reticulum, and plasma membrane were also decreased. Refeeding restored the greatest part of these losses within 5 days.
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PMID:Starvation and refeeding in rats: effect on organismic respiration, cytoplasmic constituents of liver, and succinic dehydrogenase activity in liver, kidney, and heart. 70 2

Pollen grains and pollen tubes of Pinus roxburghii were subjected to histochemical technique with a view to determining the distributional pattern of reserve substances (ascorbic acid, proteins starch, polysaccharides, nucleic acids) and some enzymes (acid phosphatase, glucose-6-phosphatase, peroxidase, esterase, cytochrome oxidase, succinate dehydrogenase). An attempt is made to correlate the activity of different enzymes in relation to pollen tube growth.
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PMID:Studies on the physiology of pollen and pollen tube growth. 1. pinus roxburghii. 82 83

In the presented study the influence of freezing and freeze-drying on enzyme activity is described. Attention is paid to 16 enzymes which can be used for quantitative enzyme histochemical techniques. With the exception of succinate dehydrogenase only, no significant inactivation during freezing and freeze-drying procedures could be demonstrated with lactate dehydrogenase, malate dehydrogenase (NAD+), malate dehydrogenase (decarboxylating) (NADP+), isocitrate dehydrogenase (NADP+), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, NADH-oxydoreductase, mitochondrial glycerol-3-phosphate dehydrogenase, cytochrome c oxidase, phosphoglucomutase, glucosephosphate isomerase, glucose-6-phosphatase, acid phosphatase, beta-glucuronidase and non specific aryl esterase. Therefore, the results supply a sound foundation for those quantitative enzyme histochemical techniques in which tissue specimens are frozen or frozen-dried before enzyme estimations are performed.
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PMID:The influence of freezing and freeze-drying of tissue specimens on enzyme activity. 87 Apr 61

Immunization of rabbits with increasing doses of Cl. botulinum toxoid, type B, led to the development in the kidneys of a focal intracapillary productive glomerulonephritis, and also of productive endo- and perivasculites. Blood letting (in the amount of 1% of body weight) aggravated the morphological picture of the affection on account of supervention of the alternative and exudative components. At the same time blood letting led to reduction of the NAD-diaphorase, succinic dehydrogenase and glucose-6-phosphatase activity in the epithelium of the proximal portions of the nephrons.
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PMID:[Histological and histochemical changes in the kidneys of rabbits immunized with Cl. botulinum toxoid type B in combination with blood loss]. 100 41

Histochemical studies have revealed hydrolytic enzyme activity in the redial tegument and caecal epithelium of Fasciola hepatica. A number of the hydrolases are known to be lysosomal marker enzymes and it is thought that they may be involved in intracellular digestion. The larval stages have also been shown to be reactive for succinate dehydrogenase and phosphorylase, but not for glucose-6-phosphatase.
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PMID:A histochemical study of the rediae and cercariae of Fasciola hepatica. 118 76

In the subcommissural organ (SCO) of the guinea pig, rat, golden hamster, and mouse the activity and distribution of enzymes related to the energy-supplying metabolism and of some marker enzymes of different cell organelles have been investigated by means of mostly modified histochemical methods. The results were compared with findings in the ciliated ependyma of the ventricular wall and with those in the ependyma of the choroid plexus of the third ventricle. In the ependymal part of the SCO only a moderate activity of hexokinase is observed in its specialized columnar cells whereas a high activity is present both in the ciliated ependyma and the choroid plexus. - The staining pattern of glucose-6-phosphatase is similar to that of hexokinase but this enzyme is found is the SCO only. - Likewise hexokinase, glycogen granules and enzymes related to glycogen metabolism (phosphoglucomutase, uridine-diphosphoglucose pyrophosphorylase, glycogen synthetase and phosphorylase) are regularly found most numerous and active in the nuclear and supra-nuclear area of the ependymal part. These enzymes are less active in both the other ependymal regions. - Uridine-diphosphoglucose dehydrogenase could not be demonstrated in the SCO. The NADP-linked enzymes of the pentose phosphate shunt, glucose-6-phosphate and 6-phosphogluconate dehydrogenase, show a moderate activity which decreases also from the nuclear towards the apical area of the ependymal cells of the SCO. Enzymes of the glycolytic pathway, such as glucosephosphate isomerase, fructose-6-phosphate kinase, fructose-I,6-diphosphate aldolase, glyceraldehyde-3-phosphate and lactate dehydrogenase, are highly active in the SCO and are located mainly in the supranuclear area, too. Fructose-1,6-diphosphatase could not be demonstrated thus indicating that in the SCO the pathway is most probably only glycolytic but not gluconeogenetic. Compared to the ependyma of the ventricular wall and of the choroid plexus, in the SCO the M type subunits of lactate dehydrogenase predominate. Glycolytic enzymes are also very active in the choroid plexus but less in the ciliated ependyma. Compared to the ciliated ependyma and especially to the ependyma of the choroid plexus, the activities of enzymes which are only present in mitochondria (NAD-linked isocitrate dehydrogenase, succinate dehydrogenase, NAD-linked malate dehydrogenase after preextraction, cytochrome oxidase, 3-hydroxybutyrate and glycerolphosphate and glutamate dehydrogenase) are relatively low. Mitochondria are accumulated near the superior pole of the nuclei as well as in the most apical part of the ependymal cells. - The staining pattern of NADP-linked isocitrate and malate dehydrogenase as well as of NADH dehydrogenase suggests that these enzymes are localized both in and out of mitochondria. The extramitochondrial activity of the first two enzymes might be localized in the cytosol. The extramitochondrial activity of NADH dehydrogenase might be localized in the endoplasmic reticulum...
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PMID:Enzymatic organization of the subcommissural organ. 123 49


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