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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)
Glucocorticoids significantly affected the developmental appearance of fructose-1,6-bisphosphatase [EC 3.1.3.11] and
glucose-6-phosphatase
[
EC 3.1.3.9
] in fetal mouse liver. In fragments of 15- or 16-day-old fetal livers maintained in organ culture in the absence of serum, induction of the bisphosphatase by dibutyryl cyclic AMP was repressed completely when the tissue was treated with 10(-7)M dexamethasone for 24 h during the second day of culture. The induction of the glucose phosphatase was greatly stimulated after a lag of 1 to 2 days. The glucocorticoid action continued over a period of 2 days even though the steroid had been washed out. The dose response curve of hydrocortisone with the half-maximally effective concentration of roughly 2 X 10(-8)M is in the physiological range. The corticoid action was specific for glucocorticoids, and aldosterone or progesterone was ineffective. When the tissue was cultured for 4 days before addition of dexamethasone, the bisphosphatase induction became insensitive to the steroid.
Glucose-6-phosphatase
induction, however, remained sensitive, but the long latent period required for the appearance of the hormone action disappeared. These results indicate the involvement of glucocorticoids in the developmental appearance of
glucose-6-phosphatase
in fetal liver.
...
PMID:Effect of glucocorticoids on induction of fructose bisphosphatase and glucose-6-phosphatase in fetal mouse liver. 609 79
The histochemical characteristics of spontaneous hepatocellular neoplasms in mice of both sexes were examined and compared with those of hepatocellular neoplasms induced in female mice by administration of polycyclic aromatic hydrocarbon carcinogens as initiators with or without subsequent phenobarbitone treatment. Controls treated with phenobarbitone alone was also induced. Spontaneous neoplasms in the livers of mice rendered siderotic by subcutaneous iron injection were deficient in cellular accumulation of stainable iron.
Glucose-6-phosphatase
activity was deficient in the majority of spontaneous and induced neoplasms. ATPase activity was increase in about half of spontaneous and carcinogen-induced neoplasms but all induced neoplasms in mice treated with phenobarbitone showed deficient activity. Gamma-glutamyltransferase activity was present in very few of the spontaneous neoplasms or in the neoplasms induced in the absence of phenobarbitone administration. However, all induced neoplasms in the mice receiving phenobarbitone showed some degree of gamma-glutamyltransferase activity together with deficient
glucose-6-phosphatase
and ATPase activities. It is concluded that the histochemical characteristics of spontaneous or induced mouse hepatocellular neoplasms are variable and may be influenced by the inducing factors.
...
PMID:Histochemical characteristics of spontaneous and chemically induced hepatocellular neoplasms in mice and the development of neoplasms with gamma-glutamyl transpeptidase activity during phenobarbital exposure. 611 14
Glucose-6-phosphatase
activity decreases whereas gamma glutamyltranspeptidase activity increases during hepatocarcinogenesis and the maintenance of hepatocytes in primary culture. This report describes the effect of culture conditions that are known to preserve hepatic
glucose-6-phosphatase
activity on gamma glutamyltranspeptidase activity. The results indicate that the regulation of
glucose-6-phosphatase
and gamma glutamyltranspeptidase activities is not coordinated in primary cultures of hepatocytes.
...
PMID:Lack of coordination between glucose-6-phosphatase and gamma glutamyltranspeptidase activities in rat hepatocytes maintained in primary culture. 615 45
1. Specific
glucose-6-phosphatase
and fructose-1,6-diphosphatase activity were found to be biochemically compartmentalized in four parts of the brain in nine nutritionally important fishes. 2.
Glucose-6-phosphatase
and fructose-1,6-diphosphatase activity were highest in the cerebrum and lowest in the cerebellum. 3. Piscivorous fishes had the highest gluconeogenic enzyme content, followed by catfishes and major carps. 4. After the liver and muscles, the various parts of the brain play an important role in carbohydrate metabolism. 5. A direct relationship between the stage of evolution and elevation of gluconeogenic enzyme levels was observed. 6. It is evident from the results and the discussion that evolution modifies the biochemical organization of fishes in general and of their brain in particular.
...
PMID:Biochemical compartmentation of fish tissues. Distribution of gluconeogenic enzymes in the brain. 627 36
Glucose-6-phosphatase
(
EC 3.1.3.9
) activity in kidney and liver was found to be markedly elevated 3 hr after a single large dose of fluoride (NaF, 35 mg/kg, i.p.). The increases in renal and hepatic
glucose-6-phosphatase
activity were completely suppressed by adrenalectomy. Moreover, the increments were markedly suppressed by injection of dibenamine as an alpha-adrenergic blocker or by injection of propranolol as a beta-adrenergic blocker.
...
PMID:A possible mechanism for elevation of glucose-6-phosphatase activity in kidney and liver of fluoride-treated rats. 628 68
Glucose-6-phosphatase
is primarily a liver and kidney enzyme. This enzyme was studied in various tumors, however,
glucose-6-phosphatase
activity was found only in tumors of liver, kidney, or adrenal origin.
Glucose-6-phosphatase
activity was useful in identifying the tissue origin of extrarenal Wilms'. Metastatic tumors within the liver or kidney that originated from other tissues did not have
glucose-6-phosphatase
activity. Therefore, it is suggested that
glucose-6-phosphatase
can be used as a specific enzyme marker for tumors of liver and kidney origin.
...
PMID:Glucose-6-phosphatase as a marker for tumors of liver and kidney origin. 631 74
Parenchymal activities (mumol . min-1 . g liver-1) and distributions of mitochondrial succinate dehydrogenase, cytosolic phosphoenolpyruvate carboxykinase and microsomal
glucose-6-phosphatase
were studied in regenerating rat liver after two thirds partial hepatectomy. Succinate dehydrogenase activity remained constant with a slight and transient increase for a few hours after operation. The typical periportal localization was changed to an almost even distribution from 8 h to 7 days; it was fully restored after 14 days. Phosphoenolpyruvate carboxykinase activity was increased by 1.8 fold 24 h after surgery; it remained enhanced until about 72 h. The normal periportal to perivenous enzyme gradient was diminished or replaced by a homogeneous distribution between 8 h and 7 days; the zonal heterogeneity was regained after 14 days.
Glucose-6-phosphatase
activity remained constant after partial hepatectomy. The normal periportal maximum was lost between 4 h and 36 h; the activity became more equally distributed and was even shifted towards the perivenous zone. After 48 h the zonal distribution was reestablished. The results indicate that after partial hepatectomy the gluconeogenic capacity of the liver remnant is increased and that this increase is accompanied by a loss of the normal heterogeneity which is typical for the glucostat function of the organ. They reveal in addition that the three enzymes, representing three different subcellular compartments, change their zonal heterogeneity individually rather than synchronously.
...
PMID:Alteration in zonation of succinate dehydrogenase, phosphoenolpyruvate carboxykinase and glucose-6-phosphatase in regenerating rat liver. 632 5
Optimum conditions were established for the assay of glycogen, glycogen synthase, glycogen phosphorylase, phosphoglucomutase, and
glucose-6-phosphatase
in rabbit fetal heart, lung, and liver. Using these methods, the pattern of appearance of glycogen and the above four enzymes was established from day 18 of gestation to day 8 after birth. The results indicate that total tissue glycogen reaches maximum levels between days 22 and 24 in the heart, days 24 and 26 in the lung, and days 30 and 31 in the liver. In all three tissues, the rapid rise or depletion of glycogen is coincident with a corresponding increase in glycogen synthase and glycogen phosphorylase activities. However, substantial amounts of glycogen synthase are present both prior to and after the accumulation of glycogen. Similarly, considerable amounts of glycogen phosphorylase are present early in gestation, yet deposition of glycogen occurs. Both the I and D forms of glycogen synthase are present in the three tissues, the major being the physiologically inactive D form. Similarly both the a and b forms of glycogen phosphorylase are present, with the a form (active form) making up about 30-60% of the total phosphorylase activity.
Glucose-6-phosphatase
was absent in fetal heart and lung throughout the period of gestation investigated. Low levels of this enzyme were detectable in fetal liver near term. The phosphoglucomutase activity increased progressively from day 22 of gestation in all three tissues and continues to increase after birth. The disappearance of fetal lung glycogen occurs between days 27 and 28 at a time when surfactant phospholipids first appear. These findings indicate that the breakdown of glycogen is providing the fetal lung cells with energy necessary for surfactant phospholipid biosynthesis.
...
PMID:Ontogeny of some enzymes of glycogen metabolism in rabbit fetal heart, lungs, and liver. 685 Apr 15
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.
...
PMID:Plasma membrane and phagosome localisation of the activated NADPH oxidase in elicited peritoneal macrophages of the guinea-pig. 706 27
The livers of rats treated for 12 weeks with N-nitrosomorpholine (80 mg/1 drinking water) were investigated on the day of carcinogen withdrawal (12 + 0 weeks) and 8 weeks after cessation of treatment (12 + 8 weeks). The glycogen content in relation to the DNA and protein content of the liver and the activities of glycogen synthetase, glycogen phosphorylase,
glucose-6-phosphatase
, and glucose-6-phosphate dehydrogenase were determined in the liver homogenates. The glycogen content of the livers was slightly elevated at both times investigated. Phosphorylase and synthetase activities showed no clear alterations in livers of treated animals as compared with controls.
Glucose-6-phosphatase
activity was significantly reduced at 12 + 0 weeks and returned to normal values at 12 + 8 weeks. The activity of glucose-6-phosphate dehydrogenase was unchanged at 12 + 0 weeks, but exhibited a significant increase at 12 + 8 weeks. Polyacrylamide gel electrophoresis with staining of the gels by an assay specific for the glucose-6-phosphate-dehydrogenase-catalysed reaction revealed the same pattern of active bands in treated and untreated animals but with higher activities in two bands originating from extracts of nitrosomorpholine-treated livers.
...
PMID:Biochemical correlation of glycogen content and activity of some enzymes of carbohydrate metabolism in rat liver during early stages of carcinogenesis. 713 Feb 54
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