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PubMed1986

The regulation of phosphofructokinase in epimastigote Trypanosoma cruzi.

Glycosomal (microbody)-enriched fractions prepared from epimastigote Trypanosoma cruzi were used as a partially purified source of phosphofructokinase. D-Fructose 6-phosphate showed sigmoidal kinetics at pH 7.0, but hyperbolic kinetics at pH 8.0. Various adenosine nucleotides were positive effectors; 5'-AMP was the most powerful. ATP showed hyperbolic kinetics under all conditions tested. Several described inhibitors and activators of mammalian phosphofructokinase were without significant effect on the trypanosomal enzyme; the absence of effect of D-fructose 2,6-bisphosphate is of particular note.

Adenosine Diphosphate↗
PubMed1986

Fructose 2,6-bisphosphate and glucose 1,6-bisphosphate in erythrocytes during chicken development.

In contrast to mammalian erythrocytes, chicken erythrocytes contain fructose 2,6-bisphosphate at levels (0.5 nmol/10(9) cells) similar to those of 2,3-bisphosphoglycerate (1.2 nmol/10(9) cells) and slightly lower than those of glucose 1,6-bisphosphate (5.2 nmol/10(9) cells). In chick embryo erythrocytes the levels of both fructose 2,6-bisphosphate and glucose 1,6-bisphosphate are much lower. They begin to increase at hatching and reach the levels in chicken in a few days.

Aging↗
PubMed1986

Activation of chicken liver fructose- 1,6-bisphosphatase by oxidized glutathione.

Treatment of chicken liver fructose- 1,6-bisphosphatase with oxidized glutathione (GSSG) leads to an increase in activity. This activation is markedly enhanced if treatment is performed in the presence of AMP or Mn2+. The effects of AMP and Mn2+ appear to be synergistic. The maximal activation is over 13-fold and is accompanied by the disappearance of 4 sulfhydryl groups per molecule of enzyme. Both fructose 1,6-bisphosphate and fructose 2,6-bisphosphate can largely prevent this activation. Activation can be reversed by dithiothreitol or cysteine. It appears that GSSG activates this enzyme by thiol/disulfide exchanges with the enzyme's specific sulfhydryl groups.

Adenosine Monophosphate↗
PubMed1987

Adenylate cyclase stimulating agents and mitogens raise fructose 2,6-bisphosphate levels in human fibroblasts. Evidence for a dual control of the metabolite.

Fructose 2,6-bisphosphate, the most potent activator of 6-phosphofructo-1-kinase, has been demonstrated to mediate the increase of glycolytic flux induced by mitogens human fibroblasts. In the present work the molecular basis of transmembrane control of fructose 2,6-bisphosphate has been investigated. Prostacyclin and isoprenaline, known to activate adenylate cyclase, are able to increase fructose 2,6-bisphosphate levels, indicating that in human fibroblasts cyclic AMP plays a positive role in the control of the metabolite concentration, opposite to that exerted in hepatocytes. Substances known to activate protein kinase C such as phorbol 12-myristate 13-acetate, or to stimulate phosphoinositide turnover such as thrombin and bradykinin are also effective in raising fructose 2,6-bisphosphate. Therefore, we conclude that cyclic AMP and protein kinase C are likely involved in the control of fructose 2,6-bisphosphate levels in human fibroblasts.

Adenylyl Cyclases↗
PubMed1987

Fructose 2,6-bisphosphate and glucose 1,6-bisphosphate in rabbit erythroid cells during differentiation.

Fructose 2,6-bisphosphate concentration and 6-phosphofructo-2-kinase activity markedly decrease during differentiation of rabbit erythroid cells, being higher in erythroblasts (654 +/- 97 pmol/10(9) cells; 238 +/- 81 U mu/10(9) cells) than in reticulocytes (40 +/- 15 pmol/10(9) cells; 11 +/- 3 U mu/10(9) cells) and much higher than in mature erythrocytes (10 +/- 0.8 pmol/10(9) cells; 2 +/- 1 U mu/10(9) cells). The enzymatic activities involved in glucose 1,6-bisphosphate metabolism also decrease, but the levels of aldohexose 1,6-bisphosphates remain essentially constant during differentiation of erythroid cells.

Animals↗
PubMed1987

Fructose 2,6-bisphosphate in isolated foetal hepatocytes.

Fru 2,6-P2 was present in isolated foetal hepatocytes at a concentration of 1.6 nmol per g cells. When foetal hepatocytes were exposed to glucagon no changes were observed either in the concentration of Fru 2,6-P2 and lactate release or in the activities of 6-phosphofructo-2-kinase and pyruvate kinase. Incubation of purified 6-phosphofructo-2-kinase with the catalytic subunit of protein kinase did not change the enzyme activity. The inhibition by sn-glycerol 3-phosphate was much lower for the foetal than for adult enzyme. These results suggest that an isoenzyme of 6-phosphofructo-2-kinase in foetal hepatocytes different from that of adult hepatocytes may be present.

Animals↗
PubMed1988

Anoxic brain function: molecular mechanisms of metabolic depression.

An examination of the kinetic parameters of phosphofructokinase, pyruvate kinase and glycogen phosphorylase, and the cellular concentration of fructose 2,6-bisphosphate during anoxia in the turtle Pseudemys scripta showed that the total activity of glycogen phosphorylase, and the phosphofructokinase inhibition constants for citrate and ATP were decreased in anoxic turtle brain. These results suggest that the ability of turtle brain to survive extended periods of anoxia is the result of metabolic rate depression regulated, at the molecular level, by enzyme inactivation through anoxia-induced covalent modification.

Adenosine Triphosphate↗
PubMed1988

Inhibition of glucose phosphorylation by fatty acids in the perfused rat heart.

The flux of glucose entering the glycolytic pathway under various metabolic conditions has been indirectly monitored in the Langendorff perfused rat heart using 31P-NMR spectroscopy. By totally inhibiting (greater than 95%) glyceraldehyde-3-phosphate dehydrogenase with low concentrations of iodoacetic acid (0.2 mM) in the perfusion medium, active glycolysis results in the accumulation of sugar phosphate species (fructose 1,6-bisphosphate, dihydroxyacetone phosphate, and glyceraldehyde 3-phosphate) which can be observed in the 31P-NMR spectrum. Using this technique, it has been shown that butyrate (10 mM) in the perfusion medium decreases the flux through the initial steps of the glycolytic pathway by at least 6-fold and that both glucose phosphorylation and glycogenolysis are inhibited. Upon total global ischemia in the presence of both glucose and butyrate, the glycolysis rate is stimulated approx. 100-fold.

Adenosine Triphosphate↗
PubMed1988

Regulation of fructose 2,6-bisphosphate levels in cold-acclimated brown adipose tissue of rat.

The effects of cold exposure and T4 administration on fructose 2,6-bisphosphate levels, phosphofructokinase-2 and pyruvate kinase activities were examined in rat brown adipose tissue. Cold adaptation (14 days) gave rise to a 2-fold increase in the amount of fructose 2,6-bisphosphate and phosphofructokinase-2 activity, and increased the pyruvate kinase activity 4-fold. If, in addition, the cold-acclimated rats were treated with T4, these parameters were again significantly enhanced. The effect on phosphofructokinase-2 was on the Vmax, without modification of the Km (for both fructose 6-phosphate and ATP) of the enzyme. In the hypothyroid state, however, the activity of pyruvate kinase remains unchanged. These data support previous observations on stimulation of glycolytic flux during cold adaptation in brown adipose tissue, and a permissive role of thyroid hormones in the process.

Adaptation, Physiological↗
PubMed1988

Allosteric inhibition of Dictyostelium discoideum fructose-1,6-bisphosphatase by fructose 2,6-bisphosphate.

It has been found that the inhibition of Dictyostelium discoideum fructose-1,6-bisphosphatase by fructose 2,6-P2 greatly diminished when the pH was raised to the range 8.5-9.5, which resulted in a marked decrease of the affinity for the inhibitor with no change in the Km for the substrate. This provides evidence for the involvement of an allosteric site for fructose 2,6-P2. Moreover, the fact that excess substrate inhibition also decreased at the pH values for minimal fructose 2,6-P2 inhibition, and was essentially abolished in the presence of fructose 2,6-P2, strongly suggests that this inhibition takes place by binding of fructose 1,6-P2 as a weak analogue of the physiological effector fructose 2,6-P2.

Allosteric Regulation↗
PubMed1989

Fructose 2,6-bisphosphate and glucose 1,6-bisphosphate levels in erythrocytes with high and low 2,3-bisphosphoglycerate content during postnatal development.

In rabbit and sheep erythrocytes the concentrations of 2,3-bisphosphoglycerate, fructose 2,6-bisphosphate and glucose 1,6-bisphosphate suffer important changes after birth, which differ in both species. The changes of fructose 2,6-bisphosphate and glucose 1,6-bisphosphate correlate with the changes in the levels of the enzymatic activities involved in their synthesis. The change of 2,3-bisphosphoglycerate levels in rabbit but not in sheep erythrocytes could be explained by the changes of the phosphofructokinase/pyruvate kinase and 2,3-bisphosphoglycerate synthase/2,3-bisphosphoglycerate phosphatase activity ratios.

2,3-Diphosphoglycerate↗
PubMed1989

Control of fructose 2,6-bisphosphate levels in rat macrophages by glucose and phorbol ester.

The presence of fructose 2,6-bisphosphate (Fru 2,6-P2) in elicited peritoneal macrophages of rat was examined. These cells possess an active phosphofructokinase-2 which is diminished by citrate and only slightly inhibited by glycerol 3-phosphate. Phosphofructokinase-1 submaximal activity was increased 26-fold by the addition of 1 microM Fru 2,6-P2. Incubation of cells without glucose decreased the amount of Fru 2,6-P2 to zero, but further addition of 5 mM glucose increased the levels of the sugar ester 20-fold. In addition, the presence of phorbol ester potentiated the synthesis of Fru 2,6-P2. By contrast phenylisopropyladenosine or prostaglandin F2 alpha inhibited the production of Fru 2,6-P2.

Animals↗
PubMed1989

Thyroid hormone stimulates expression of 6-phosphofructo-2-kinase in rat liver.

The activity of liver 6-phosphofructo-2-kinase (PFK-2), the enzyme that catalyses the synthesis of fructose 2,6-bisphosphate, was markedly decreased in hypothyroid rats and partially restored after 3 days of treatment with triiodothyronine. The changes in PFK-2 activity were accompanied by parallel changes in enzyme content measured by immunotitration and in PFK-2 mRNA determined by dot blot and Northern blot hybridization with cDNA probes. It is concluded that thyroid hormone stimulates liver PFK-2 gene expression by a pre-translational mechanism.

Animals↗
PubMed1989

Effect of adenosine on fructose 2,6-bisphosphate levels and glucose metabolization by chicken erythrocytes.

Adenosine can be metabolized by chicken erythrocytes as a carbon source maintaining ATP levels. In addition, it stimulates glucose uptake and lactate production. Adenosine effects do not involve binding to membrane receptors. They are dependent on the provision of a carbon source to glycolysis and correlate with the increase of fructose 2,6-bisphosphate levels that activating phosphofructokinase would increase the glycolytic flux.

Adenosine↗
PubMed1990

Fructose 2,6-bisphosphate and glycolytic flux in skeletal muscle of swimming frog.

Glycolytic flux in skeletal muscle is controlled by 6-phosphofructokinase but how this is achieved is controversial. Brief exercise (swimming) in frogs caused a dramatic increase in the phosphofructokinase activator, fructose 2,6-bisphosphate, in working muscle. The kinetics of phosphofructokinase suggest that in resting muscle, the enzyme is inhibited by ATP plus citrate and that the increase in fructose 2,6-bisphosphate is part of the mechanism to activate phosphofructokinase when exercise begins. When exercise was sustained, fructose 2,6-bisphosphate in muscle was decreased as was the rate of lactate accumulation. Glycolytic flux and the content of fructose 2,6-bisphosphate appear to be closely correlated in working frog muscle in vivo.

Animals↗
PubMed1991

Altered glucose 1,6-bisphosphate and fructose 2,6-biphosphate levels in low-frequency stimulated rabbit fast-twitch muscle.

Glucose 1,6-bisphosphate (Glc-1,6-P2) and fructose 2,6-bisphosphate (Fru-2,6-P2) concentrations display pronounced increases in rabbit fast-twitch muscle during chronic low-frequency stimulation. These increases are first seen after stimulation periods exceeding 3 h and reach maxima after 12-24 h of stimulation (approximately 3-fold for Glc-1,6-P2 and 5-fold for Fru-2,6-P2). Both metabolites regress to normal values after stimulation periods longer than 4 days. The fact that their increases coincide with the replenishment of glycogen after its initial depletion, could point to a role of Glc-1,6-P2 and Fru-2,6-P2 in glycogen metabolism.

Animals↗
PubMed1991

A rat gene encoding heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.

There are at least 3 isozymes of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, a bifunctional enzyme which catalyzes the synthesis and degradation of fructose 2,6-bisphosphate. A 22-kb rat gene that encodes the heart isozyme has been identified and compared with the 55-kb rat gene encoding the liver and muscle isozymes which had been described earlier. Although these 2 genes include 12 successive similar exons, they contain dissimilar exons at both ends, consistent with the occurrence of different regulatory domains at the N- and C-termini in the 3 isozymes.

Amino Acid Sequence↗
PubMed1991

Glycogen hyperaccumulation in Saccharomyces cerevisiae ras2 mutant. A biochemical study.

The mechanism by which yeast ras2 mutant hyperaccumulates glycogen has been investigated. Total glycogen synthase activity was between 2.5 and 1.3 times higher in the ras2 mutant than in an isogenic strain. In addition, while in the normal strain the glycogen synthase activation state decreased along the exponential phase, in the mutant strain the opposite behaviour was observed: glycogen synthase activation state rose continuously reaching full activation at the beginning of the stationary phase. Glycogen phosphorylase a activity was up to 40 times higher in the mutant than in the normal strain. Glucose 6-phosphate and fructose 2,6-bisphosphate levels were slightly more elevated in the mutants. The increase in total glycogen synthase and, particularly, the full activation of this enzyme may explain glycogen hyperaccumulation in the ras2 mutant even in the presence of elevated levels of glycogen phosphorylase a.

Cyclic AMP↗