Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
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 hexokinase, glucokinase, phosphofructokinase, glucose-6-phosphate dehydrogenase, glucose-6-phosphatase, and fructose-1,6-diphosphatase were determined in loach embryos developed in solutions of insulin, hydrocortisone, estrone and thyroxin at different stages of embryogenesis. Glucokinase and fructose-1,6-diphosphatase activties are shown not to change markedly under the influence of the above-mentioned hormones. During some periods of early development the hexokinase activity is inhibited by insulin, estrone and thyroxin. The glucose-6-phosphate dehydrogenase activity is suppressed by each of the used hormones at all the stages of early embryogenesis while the glocose-6-phosphatase activity decreased only under the influence of insulin at the cleavage, blastula and gastrula stages. Insulin increased the activity of phosphofructokinase at the cleavage, blastula and early gastrula stages and hydrocortisone, estrone and thyroxine during certain periods of these stages. From middle gastrula two last hormones decreased the phosphofructokinase activity in the loach embryos.
 ...
PMID:[Activity of carbohydrate metabolism enzymes in loach embryos under the influence of hormones]. 19 80

It is established that in embryos incubated until the early blastula stage in the solution of insulin with addition of cycloheximide or puromycin, there is neither a decrease in the hexokinase and glucose-61 phosphate dehydrogenase activities nor an increase in the phosphofructokinase activity, as it is shown under the influence of insulin only. Puromycin removes an inhibitory effect of insulin on the glucose-6-phosphatase activity, and actinomycin D removes this influence with respect to glucose-6-phosphate dehydrogenase and glucose-6-phosphatase activities. The addition of antibiotics removes inhibition of the hexokinase, glucose-6-phosphate dehydrogenase and glucose-6-phosphatase activities by the hormone in the unfertilized eggs as well. Actinomycin D alone inhibits the hexokinase and activates the phosphofructokinase activities in the embryos and eggs, puromycin decreases their hexokinase activity and cycloheximide has the same effect on the glucose-6-phosphatase activity in the embryos only.
 ...
PMID:[Effect of insulin on activity of carbohydrate metabolism enzymes in loach embryos in early development]. 19 74

Activities of glucose-6-phosphatase, glucose-6-phosphate dehydrogenase and content of glycogen in liver as well as content of sugar in blood were studied after denervation of dog liver tissue. Activities of these enzymes were increased and content of glycogen in hepatocytes was decreased within 1-2 weeks after the denervation. Within a month the enzymatic activities and content of glycogen in liver tissue approached the control levels; these patterns were similar to control ones within the subsequent periods of examination (3-months--1 year). Content of sugar in blood was the same within all the periods of study (3 days--3 months).
 ...
PMID:[Effect of denervation on carbohydrate metabolism in the liver]. 21 May 85

The activity of hexokinase (HK), its isoenzymes, glucose-6-phosphatase and glucose-6-phosphate dehydrogenase, and the triiodothyronine (T3) effect on this activity in the liver tissue of mice bearing transplantable hepatoma 22a were studied in different periods of the tumor growtn. It was shown that alterations in the activity of the enzymes in the liver of tumor-bearing mice occurred already in the presence of a small tumor. More profound alterations in the activity of all enzymes studied, apart from those in the enzymatic pattern of HK, could be observed starting from day 21after the tumor transplantation. In the initial stages of the hepatoma growth the activity of the test enzymes in the liver was regulated by thyroid hormone. The effect of Ta on the activity of the enzymes in the host liver was gradually lost in the course of the tumor growth.
 ...
PMID:[Carbohydrate metabolism enzymatic activity and its alteration under the influence of thyroid hormone during tumor growth]. 22 89

The activities of the key gluconeogenic, glycolytic, and pentose-shunt enzymes in chicken kidney were determined starting from 8 days before to 58 days after hatching. The activities of pyruvate carboxylase (PC), mitochondrial and cytosolic phosphoenolypruvate carboxykinase (PEPCK), fructose-1,6-diphosphatase (FDPase) and glucose-6-phosphatase (G6Pase) were low in the embryonic tissue but increased towards the time of hatching. After hatching, the activities of PC, mitochondrial PEPCK, and G6Pase continued to increase, but those of FDPase and cytosolic PEPCK decreased. Relatively little change in these activities was observed in chickens over 24 days old. The activities of hexokinase (HK), phosphofructokinase (PFK), pyruvate kinase (PK), and lactate dehydrogenase (LDH) increased during embryonic growth. After hatching, HK activity continued to increase and then decrease, whereas PFK appeared to decrease and then increase to prehatch levels in 28-day-old birds. LDH activity continued to increase until 8 days after hatching and remained constant thereafter. No definite pattern was discernible in the case of PK. As for the pentose-shunt enzymes, there was no significant change in glucose-6-phosphate dehydrogenase activity (G6PDH), but the activity of 6-phosphogluconate dehydrogenase (6PGDH) increased until the chickens were 14 days old and then remained relatively constant.
 ...
PMID:Development of gluconeogenic, glycolytic, and pentose-shunt enzymes in the chicken kidney. 22 78

The inducing effect of certain barbiturates (secobarbitone, thiopentone, pentobarbitone, allobarbitone, phenobarbitone and barbitone) on the levels of the hepatic microsomal drug-metabolizing enzymes has been studied in the rat both in vivo and in vitro. The extent of induction was related to the plasma half-lives of the barbiturates; compounds with low rates of metabolism and long half-lives were the most potent inducing agents. The latter (phenobarbitone, pentobarbitone and allobarbitone) were shown by spectral technique to interact with cytochrome P-450 suggesting that their mechanism of enzyme induction was 'substrate induction' in type. Barbiturates containing an allyl group (secobarbitone and allobarbitone) had a weaker inducing effect than expected, possibly due to their destruction of cytochrome P-450. Despite its short plasma half-life of 0-5 h thiopentone was a relatively potent inducer probably due to its metabolism to pentobarbitone, which has a much longer plasma half-life (1-3 h). Barbitone is an effective inducer of the drug-metabolizing enzymes, yet does not interact spectrally with cytochrome P-450; this is in accord with the observations that although there are increases in NADPH-cytochrome c reductase and cytochrome b5, following administration of barbitone there is no increase in cytochrome P-450. Barbiturate pretreatment does not affect the activities of glucose-6-phosphatase, glucose-6-phosphate dehydrogenase or 6-phosphogluconate dehydrogenase.
 ...
PMID:Mechanism of induction of hepatic microsomal drug metabolizing enzymes by a series of barbiturates. 24 86

1. The relationships between food intake self-selection and liver substrates (glycogen, fat) or activities of pyruvate kinase, glucose-6-phosphate dehydrogenase, malic enzyme, acetyl CoA carboxylase, glucose-6-phosphatase and phosphoenolpyruvate carboxykinase were determined during the spontaneous variations of body weight in the dormouse. 2. The results show that during the phase of increasing body weight, carbohydrate intake and enzyme activities involved in lipogenesis are on a high level. 3. On the last part of the body weight increasing phase, when lipid intake occurs, lipogenesis is depressed and a gluconeogenetic activity is set on, while total caloric intake is important and body weight is still increasing. 4. These metabolic changes are interpreted as a preparation to hibernating conditions in the dormouse.
 ...
PMID:Relationships between spontaneous food intake and metabolic activities in the dormouse (Glis glis L.). 31 73

Soybeans inoculated with Phomopis sp. were incubated for weeks and then extracted with methanol and ether, and the culture filtrates were intubated into crops of chicks. Activities of glucose-6-phosphatase and glucose-6-phosphate dehydrogenase in liver were increased, and glycogen stores and plasma glucose concentrations were reduced. Histologically, severe hepatocytic necrosis was found in chicks treated with the toxic culture filtrate. Significant clinical signs were loss of body weight and reduced feed consumption. The metabolic changes responsible for the findings are discussed.
 ...
PMID:Carbohydrate metabolism in chicks after administration of toxins from a Phomopsis sp. 57 12

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.
 ...
PMID:The influence of freezing and freeze-drying of tissue specimens on enzyme activity. 87 Apr 61

Biochemical pathways which are involved in energy metabolism were examined in the kidney of heat-acclimated hamsters. It was found that heat acclimation caused 47% reduction in glucose-6-phosphatase (G1c-6-Pase) activity and 40% lower rate of gluconeogenesis. No changes were found in the activity of hexokinase, glucose-6-phosphate dehydrogenase, pyruvate kinase, lactic dehydrogenase, or in kidney glycogen content. Isolated kidney mitochondria of heat-acclimated hamsters utilized 15% less oxygen than that of controls, but no differences were found in the P/O ratio. Determination of the content of some cytochromes showed a significant reduction in cytochromes c + c1, but no difference was found in the content of cytochromes a, a3, and b. These results suggest that the kidney plays a role in the reduction of energy metabolism during the process of heat acclimation.
 ...
PMID:Energy metabolism in kidney of heat-acclimated hamsters. 120 Jan 40


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>