Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Vanadate has been found to be a potent inhibitor of both the hydrolytic and synthetic activities of the multifunctional enzyme glucose-6-phosphatase (D-glucose-6-phosphate phosphohydrolase, EC 3.1.3.9). The enzyme, when studied in both microsomal preparations and in situ using permeable isolated hepatocytes, is inhibited by micromolar concentrations of vanadate. The inhibition by vanadate is greater in detergent-treated than in untreated microsomes. In both the microsomal preparations and permeable hepatocytes, the inhibition by vanadate is competitive with the phosphate substrate and is greater for the phosphotransferase than the hydrolase activity of the enzyme. The Ki values of vanadate for carbamyl-phosphate : glucose phosphotransferase and glucose-6-phosphate phosphohydrolase determined with permeable hepatocytes are in good agreement with the values determined with detergent-dispersed microsomes. The previously described inhibition of glucose-6-phosphate phosphohydrolase by ATP (Nordlie, R.C., Hanson, T.L., Johns, P.T. and Lygre, D.G. (1968) Proc. Natl. Acad. Sci. USA 60, 590-597) can now be explained by the vanadium contamination of the commercially available ATP samples used. In contrast with glucose-6-phosphatase, hepatic glucokinase and hexokinase were not inhibited by vanadate. Physiological implications and utilitarian experimental applicability of vanadate as a selective metabolic probe, based on these observations, are suggested.
 ...
PMID:Vanadate: a potent inhibitor of multifunctional glucose-6-phosphatase. 627 21

Due to the close correlation between glucose mobilization and utilization within animal tissues, in this paper, the stages of appearance of phosphorylase, glucose-6-phosphatase and hexokinase as well as the levels of some intermediates of glucose metabolism have been investigated during Bufo bufo development. Phosphorylase first appears at stage 13 and is dominant in the neural part of the embryo, but, after this stage, increases relatively more in the nonneural one. Hexokinase appears at stage 17 and glucose-6-phosphatase soon after. Phosphorylase appearance at stage 13 is correlated with an increase of lactate content in the embryo; this may indicate a metabolization of hexoses. On this basis, the subsequent appearance of hexokinase and glucose-6-phosphatase activities also seems coherent with hexose mobilization and utilization within embryo. No direct causative factor for the changes observed was evident.
 ...
PMID:Developmental aspects of hexose metabolism in Bufo bufo. 629 68

Deoxyglucose uptake and activities of hexokinase and glucose-6-phosphatase in auditory structures (organ of Corti, stria vascularis and spiral ligament, modiolar section of VIIIth nerve, inferior colliculus) and non-auditory tissues (heart, kidney, liver) of the mouse were analyzed. [3H]Deoxyglucose was given as a pulse into the tail vein and uptake was quantitated by microdissection of tissues and scintillation counting. Radioactivity in cochlear tissues was maximal after 45-60 min and declined with a half-life of 30-60 min. Deoxyglucose 6-phosphate represented ca. 60% of total radioactivity (heart, inferior colliculus, greater than 80%). The ratio of hexokinase to glucose-6-phosphatase activity was considerably lower in the auditory periphery than in brain. The rank order was inferior colliculus much greater than VIIIth nerve approximately equal to heart greater than stria vascularis and spiral ligament greater than kidney greater than organ of Corti approximately equal to liver. Exposure to broadband noise increased glucose utilization in all auditory structures. Uptake was maximally (2- to 3-fold) stimulated at moderate noise intensity (55-85 dBA). In addition, the auditory system showed two salient features: at high intensities (100 and 115 dBA) deoxyglucose uptake decreased from the maximum; and the non-sensory tissues of the cochlea (stria vascularis and spiral ligament) responded to sound parallel to the sensory structures at all levels of stimulus intensity. There were no effects of acoustic stimulation on serum glucose levels, serum kinetics of deoxyglucose, or deoxyglucose uptake into other body tissues.
 ...
PMID:Acoustic stimulation alters deoxyglucose uptake in the mouse cochlea and inferior colliculus. 630 1

Treatment with the antihistaminic agent methapyrilene led to a decrease of glucose-6-phosphatase activity and to an increase of glucose phosphorylating activity in the periportal zone of the liver acinus. However, the glucogenic capacity was maintained by a compensatory elevation of glucose-6-phosphatase and simultaneous reduction of hexokinase and glucokinase in the perivenous zone. The normal metabolic zonation with a glucogenic periportal and a glycolytic perivenous zone was not abolished but inverted by these alterations.
 ...
PMID:Inversion of the metabolic zonation of rat liver parenchyma by methapyrilene treatment. 631 82

The role of glucocorticosteroid and thyroid hormone and of glucagon and insulin in the pre- and postnatal developmental formation of carbamoyl-phosphate synthase, ornithine transcarbamoylase, arginase, glutamate dehydrogenase, tyrosine aminotransferase, glucose-6-phosphatase, hexokinase and glucokinase activities in rat liver was investigated. Glucocorticosteroids and a low insulin/glucagon ratio always stimulate formation of carbamoyl-phosphate synthase, ornithine transcarbamoylase, arginase, glutamate dehydrogenase, tyrosine aminotransferase and glucose-6-phosphatase, while glucocorticosteroids and a high insulin/glucagon ratio stimulate formation of glucokinase. Thyroid hormone stimulates the formation of carbamoyl-phosphate synthase, arginase and tyrosine aminotransferase only before birth, whereas it stimulates the formation of glutamate dehydrogenase and glucose-6-phosphatase both before and after birth. Ornithine transcarbamoylase activity is depressed after thyroid-hormone treatment before and after birth. DNA content is always decreased by glucocorticosteroids and increased by thyroid hormone. The effect of these hormones on hexokinase is complex, probably due to different responses of the constitutive isozymes. With the exception of the effects of thyroid hormone on carbamoyl-phosphate synthase, arginase and tyrosine aminotransferase before birth, which may be indirect, the responses of enzyme activities and DNA content to treatment with glucocorticosteroid hormones, glucagon, insulin and thyroid hormone are qualitatively the same in fetuses, neonates, sucklings, weanlings and adults. Thus, the developmental profiles of the enzyme clusters reflect the changing levels of the relevant hormones. The enzymes that are stimulated by glucocorticosteroids and the insulin/glucagon ratio show increases in enzyme activity perinatally and around weaning, and relatively low activities in between, while those enzymes that are additionally stimulated by thyroid hormone differ in exhibiting relatively high activities between birth and weaning.
 ...
PMID:Multihormonal control of enzyme clusters in rat liver ontogenesis. II. Role of glucocorticosteroid and thyroid hormone and of glucagon and insulin. 702 60

The plasma levels of corticosterone, insulin and glucagon, and the concomitant changes in the levels of several liver enzymes and metabolites were measured in intact rats in the basal state during 24 hours and under conditions of food deprivation and hypoxia. The levels of the following enzymes and metabolites were examined: phosphoenolpyruvate carboxykinase, glucose-6-phosphatase, pyruvate kinase, phosphofructokinase, glutamic-oxaloacetic transaminase, glutamic-pyruvic transaminase, glucose, glucose-6-phosphate, glycogen, fructose-6-phosphate, hexokinase, tyrosine amino-transferase and tryptophan oxygenase. During food deprivation, the increased gluconeogenesis is possibly a result of glucagon activity. In contrast, however, during hypoxia the increase in gluconeogenesis seems to be a result of the higher plasma level of corticosterone. During starvation, the insulin concentration dropped steadily and came close to zero.
 ...
PMID:Plasma concentrations of glucose, corticosterone, glucagon and insulin and liver content of metabolic substrates and enzymes during starvation and additional hypoxia in the rat. 703 Aug 99

The effect of daily intraperitoneal administration of Mn2+(4 mg/kg) was investigated on the metabolism of carbohydrates and certain enzymes involved in the oxidation of glucose in the rat liver and blood at the intervals of 30, 60 and 90 days after exposure. Mn2+ had no effect on the contents of blood reducing sugars and proteins, however the levels of pyruvic and lactic acids were reduced at 60 and 90 days after the metal treatment. The contents of liver glycogen and proteins remained unaffected while pyruvic acid content was decreased in Mn2+ treated rat liver throughout the experimental period. The activities of glycogen phosphorylase and lactate dehydrogenase decreased while that of phosphoglucoisomerase and glucose-6-phosphatase increased in the post mitochondrial supernatant at 60 and 90 days of Mn2+ exposure. The levels of hexokinase decreased and FDP-aldolase and fructose-1, 6-diphosphatase increased throughout the experimental period. The magnitude of alteration was found to be greater with the increase in the duration of Mn2+ treatment. Several of the mitochondrial enzymes in the liver were inhibited in the manganese exposed rats which may be responsible to inhibit the rate of dehydrogenation of Kreb cycle's intermediates along with the linked respiratory chain and eventually oxidation in the rat liver.
 ...
PMID:Effects of manganese on carbohydrate metabolism and mitochondrial enzymes in rats. 713 26

The influence of fructose feeding for 1 to 12 days on the activity of enzymes of glycolysis and gluconeogenesis was studied in the jejunal mucosa and the liver of rats. In the jejunal mucosa fructose feeding leads to an increase in the activity of 6-phosphofructokinase (p less than 0.05) and fructose-1.6-bisphosphate aldolase (p less than 0.05), while the activity of hexokinase and glucose-6-phosphate dehydrogenase remains unchanged. Fructose feeding increases the activity of fructose-bisphosphatase in the jejunal mucosa, however, the absolute values of this enzyme remain low (less than 10%) when compared to those in the liver. In the liver fructose feeding is followed by a marked increase of the activity of fructose-bisphosphatase and glucose-6-phosphate dehydrogenase. In contrast, the activity of glucose-6-phosphatase decreases significantly under a fructose enriched diet. The enzyme activity rose to a maximum within 3 days; in the following time of observation no major changes occurred. The results are in accordance with the assumption that fructose feeding leads in the jejunal mucosa mainly to adaptive alterations of the activity of those enzymes which are involved in the breaking-down of fructose, whereas in the liver the activity of those enzymes is increased, which take part in the new synthesis of glucose-6-phosphate or which direct glucose-6-phosphate into the pentose-phosphate.
 ...
PMID:Effect of fructose feeding on the activity of enzymes of glycolysis, gluconeogenesis, and the pentose phosphate shunt in the liver and jejunal mucosa of rats. 727 91

The role of glucocorticosteroid hormones in the developmental formation of carbamoyl-phosphate synthase, ornithine transcarbamoylase, arginase, glutamate dehydrogenase, tyrosine aminotransferase, glucose-6-phosphatase, hexokinase and glucokinase activities in rat liver was investigated. Steroid hormone producing glands were either inactivated by hypophysectomy (before birth) or removed by adrenalectomy and/or gonadectomy (after birth). These procedures strongly depressed corticosterone levels. Furthermore, they decreased enzyme activities when performed before birth or after the second postnatal week. However, adrenalectomy at 1 week of age was less effective: the developmental increases in carbamoyl-phosphate synthase, ornithine transcarbamoylase, arginase, tyrosine aminotransferase and glucose-6-phosphatase activity persisted despite the absence of increasing levels of circulating corticosterone.
 ...
PMID:Multihormonal control of enzyme clusters in rat liver ontogenesis. I. Effects of adrenalectomy and gonadectomy. 727 92

Existing models for glycolytic oscillations are not based on detailed experimental kinetics of the glycolytic enzymes. Here, a model is constructed to fit the kinetics of skeletal muscle phosphofructokinase with respect to variations in AMP, ATP, fructose-6-P, and fructose 1,6-P2 levels. A Monod-Wyman-Changeux model for a tetrameric enzyme is considered. However, it is found that the kinetic data fit considerably better with an assumption of identical, independent subunits. With parameters that fit these data and with a previous model for the rest of glycolysis, product activation of phosphofructokinase leads to oscillations of glycolytic intermediates and [ATP] resembling those observed experimentally in muscle extracts. The period is several minutes. The model can also produce oscillations at neutral pH and with [ATP] representative of an intact cell. Under both conditions the mean concentrations and oscillations vary with the rate of glucose phosphorylation in a plausible manner only if some amount of glucose-6-phosphatase or glucose-6-P dehydrogenase activity is assumed or if hexokinase is inhibited by glucose-6-P. Also, the model can be reduced to two variables for ease of analysis and the oscillation mechanism thereby illustrated.
 ...
PMID:A model for glycolytic oscillations based on skeletal muscle phosphofructokinase kinetics. 764 10


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