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)

The activities of various enzymes involved in detoxication and carbohydrate metabolism in the liver and the gastrointestinal tract of germfree (GF) and conventional (CV) rats, 8 and 40 weeks' old, were measured in relationship to intestinal microflora and aging. In 8-week-old rats, the activities of nitroreductase (NR) and aniline hydroxylase (AH) in the liver, and of alkaline phosphatase (ALP), maltase and lactase in the duodenum were higher in GF than in CV rats, but the activities of arginosuccinate synthetase (ASS) and lactate dehydrogenase (LDH) in the liver were higher in CV than in GF rats. In 40-week-old rats, the activities of NR and glucose-6-phosphatase dehydrogenase (G-6-PDH) of the liver and ALP, maltase and lactase of the duodenum were higher in GF than in CV rats, but those of ASS, UDP-glucuronyl transferase (UDP-GT), AH, beta-glucuronidase, and LDH of the liver were higher in CV than in GF rats. Compared between 8- and 40-week-old rats the activities of NR, beta-glucuronidase, LDH, and acid phosphatase increased with aging in both GF and CV rats. The specific activities of ASS in CV and UDP-GT and AH in GF rats decreased with aging. The total activities of ASS and AH in GF rats also decreased with aging. The activities of ALP, maltase and lactase decreased with aging in both GF and CV rats. Thus, these data suggested that there are influences of indigenous intestinal microflora and aging on the activities of various enzymes in the liver and gastrointestinal tract.
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PMID:Intestinal microflora and aging: age-related change of enzymes in the liver and the small intestine of germ-free and conventional rats. 679 85

The subcellular distribution of the NADPH oxidase of guinea-pig peritoneal-elicited macrophages was investigated. Post-nuclear supernatants obtained from PMA-stimulated macrophages were fractionated in discontinuous sucrose gradients. The NADPH oxidase was found to be enriched at the interface between 20 and 34 per cent sucrose. This interface was also enriched in 5'-nucleotidase, a plasma membrane marker and in glucose-6-phosphatase and NADPH-cytochrome c reductase, two endoplasmic reticulum markers. The distribution in the gradient of beta-glucuronidase, a marker of lysosomes and of succinate dehydrogenase, a marker of mitochondria was clearly different from that of NADPH oxidase and of the markers of plasma membrane and of endoplasmic reticulum. These results indicated that in stimulated-elicited macrophages the NADPH oxidase is associated with a membrane fraction. With the fractionation technique employed it was not possible to clarify whether the oxidase is located in the plasma membrane or in the endoplasmic reticulum. In order to clarify this matter the isolation of phagosomes was performed. NADPH oxidase was found to be enriched in the phagosomal fraction. Phagosomes were also found to be enriched in the plasma membrane marker 5'-nucleotidase. Glucose-6-phosphatase,, a marker of endoplasmic reticulum, and beta-glucuronidase, a marker of lysosomes were not enriched in the phagosomal fraction. The results obtained clearly suggest that the activated NADPH oxidase of peritoneal elicited macrophages of guinea pig is located in the plasma membrane.
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PMID:Plasma membrane and phagosome localisation of the activated NADPH oxidase in elicited peritoneal macrophages of the guinea-pig. 706 27

Adult male rats receiving styrene by gavage (200 or 400 mg kg-1, 6 days a week) for 100 days exhibited a significant dose-dependent increase in hepatic benzo[a]pyrene hydroxylase and aminopyrine-N-demethylase, a decrease in glutathione-S-transferase and no change in glucose-6-phosphatase. A decrease in the activity of mitochondrial succinic dehydrogenase and beta-glucuronidase was also observed. Activity of acid phosphatase was decreased only at the higher dose level. Levels of serum glutamic oxaloacetic transaminase and glutamic pyruvic transaminase were elevated only at the higher dose level. The absolute and relative weights of the liver of control and treated animals showed no significant difference. Histopathological studies of the liver tissue revealed tiny areas of focal necrosis, consisting of few degenerated hepatocytes and inflammatory cells at the higher dose level only.
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PMID:Hepatic effects of orally administered styrene in rats. 718 5

The pregnant rats were treated with formaldehyde (0.5 mg/kg daily per os) during whole period of pregnancy. The activity of cytochrome-c-oxidase, malate dehydrogenase, nucleotidase, glucose-6-phosphatase, beta-glucuronidase, N-acetyl-beta-glucosaminidase, beta-galactosidase, H(+)-ATPase, glutamate dehydrogenase, NAD- and NADP-isocitrate dehydrogenase, fructose-bisphosphate aldolase, glucose-6-phosphate dehydrogenase and content of protein in liver celts of offsprings (newborns, 2 weeks age and 2 months age) were studied. It was shown differences in development enzyme systems of control and experimental animals during ontogenesis.
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PMID:[Experimental study of the effect of formaldehyde during embryogenesis on the activity of rat liver enzyme systems in ontogenesis]. 913 53

Contribution of translocon peptide channels to the permeation of low molecular mass anions was investigated in rat liver microsomes. Puromycin, which purges translocon pores of nascent polypeptides, creating additional empty pores, raised the microsomal uptake of radiolabeled UDP-glucuronic acid, while it did not increase the uptake of glucose-6-phosphate or glutathione. The role of translocon pores in the transport of small anions was also investigated by measuring the effect of puromycin on the activity of microsomal enzymes with intraluminal active sites. The mannose-6-phosphatase activity of glucose-6-phosphatase and the activity of UDP-glucuronosyltransferase were elevated upon addition of puromycin, but glucose-6-phosphatase and beta-glucuronidase activities were not changed. The increase in enzyme activities was due to a better access of the substrates to the luminal compartment rather than to activation of the enzymes. Antibody against Sec61 translocon component decreased the activity of UDP-glucuronosyltransferase and antagonized the effect of puromycin. Similarly, the addition of the puromycin antagonist anisomycin or treatments of microsomes, resulting in the release of attached ribosomes, prevented the puromycin-dependent increase in the activity. Mannose-6-phosphatase and UDP-glucuronosyltransferase activities of smooth microsomal vesicles showed higher basal latencies that were not affected by puromycin. In conclusion, translationally inactive, ribosome-bound translocons allow small anions to cross the endoplasmic reticulum membrane. This pathway can contribute to the nonspecific substrate supply of enzymes with intraluminal active centers.
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PMID:Translocon pores in the endoplasmic reticulum are permeable to small anions. 1661 37


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