Role of fructose 2,6-bisphosphate in the control of glycolysis in mammalian tissues
Biochemical JournalPublished 15 July 1987Open access
Louis Hue, Mark H. Rider
Citations424
SJR quartileQ1
SJR score2.06
SNIP0.98
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TL;DR
The purpose of this article is to specify the conditions under which Fru-2,6-P2 plays a role in the control of glycolysis, and to review recent studies dealing with Fru’s metabolism in mammalian tissues other than liver.
Abstract
bisphosphate; Fru-2,6-P2, fructose 2,6-bisphosphate; PFK-1, 6-phosphofructo-I-kinase; PFK-2, 6-phosphofructo-2-kinase; FBPase-1, fructose 1
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
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It is concluded that a glucose load diverts the final product of hepatic gluconeogenesis from blood glucose to liver glycogen; these metabolic changes in the liver are an important determinant of glucose tolerance.
Journal of Biological ChemistryEvidence for a phosphoenzyme intermediate in the reaction pathway of rat hepatic fructose-2,6-bisphosphatase.
54 Citations1985H. B. Stewart, M. Raafat El‐Maghrabi +1 more
The phosphoenzyme is a reaction intermediate in the hepatic fructose-2,6-bisphosphatase reaction and is supported by a number of observations that support the proposition that the phosphoen enzyme is a necessary participant in catalysis.
Biochemical JournalThe ability of adenosine to decrease the concentration of fructose 2,6-bisphosphate in isolated hepatocytes. A cyclic AMP-mediated effect
54 Citations1984Ramón Bartrons, Emile Van Schaftingen +1 more
The data indicate that the effect of adenosine to decrease the concentration of fructose 2,6-bisphosphate is mediated by the stimulation of adenylate cyclase, secondary to the binding of adenoine to membranous receptors.
Journal of Biological ChemistryDifferential effects of proteolysis and protein modification on the activities of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.
53 Citations1984M. Raafat El‐Maghrabi, T M Pate +2 more
The different responses of the kinase and bisphosphatase reactions to the action of these various protein-modifying agents and to thermolysin digestion support the existence of a separate site for each reaction and an essential role for sulfhydryl groups at the sugar-phosphate-binding site(s) of the Kinase.
Biochemical JournalExpression of the v-<i>src</i> or v-<i>fps</i> oncogene increases fructose 2,6-bisphosphate in chick-embryo fibroblasts. Novel mechanism for the stimulation of glycolysis by retroviruses
53 Citations1986Lisardo Boscá, Marina Mojena +3 more
Comparison of the effects of the Rous sarcoma virus with those of phorbol myristate acetate on fructose 2,6-bisphosphate suggests that both result from the stimulation of a step which is rate-limiting for 6-phosphofructo-2-kinase activation and which is also controlled by protein kinase C.
European Journal of BiochemistryActivation of glycolysis by insulin with a sequential increase of the 6‐phosphofructo‐2‐kinase activity, fructose‐2,6‐bisphosphate level and pyruvate kinase activity in cultured rat hepatocytes
52 Citations1985Irmelin Probst, Kirsten Unthan‐Fechner
It is concluded that in this insulin-sensitive cell system: the changes of glycolytic flux did not correlate with changes in the level of total Fru(2,6)P2 either in insulin or in control cells, and the apparent existence of a threshold concentration for Fru-P2 suggest a permissive action for this effector in enzyme interconversion.
European Journal of BiochemistryThe protein phosphatases involved in cellular regulation. Glycolysis, gluconeogenesis and aromatic amino acid breakdown in rat liver
52 Citations1984Steven Pelech, Philip Cohen +4 more
It is shown that under the assay conditions used, protein phosphatase-2A is the most powerful phosphatases acting on each substrate, although proteinosphatases-2C contributes a significant percentage of the activity towards 6-phosphofructo-1-kinase.
Biochemical JournalMetabolic control of hepatic gluconeogenesis during exercise
48 Citations1983G. Lynis Dohm, Eric A. Newsholme
The changes in metabolite concentrations suggest that hepatic pyruvate kinase is less active during exercise, possibly owing to phosphorylation of the enzyme, and this may play a role in increasing the rate of gluconeogenesis.
Journal of Biological ChemistryMode of interaction of phosphofructokinase with the erythrocyte membrane.
46 Citations1985J D Jenkins, F. J. Kezdy +1 more
It is demonstrated that ADP, ATP, and NADH, all of which are known to bind to the enzyme's adenine nucleotide activation site, are particularly potent in eluting the enzyme from the membrane.
Biochemical JournalFructose 2,6-bisphosphate in rat skeletal muscle during contraction
46 Citations1984Yohsuke Minatogawa, Louis Hue
Fructose 2,6-bisphosphate does not play a role in the stimulation of glycolysis during tetanus; it may, however, be involved in the control of gly colysis when the muscles are stimulated at low frequencies for short periods of time.
Journal of Biological ChemistryInhibition of gluconeogenesis and glycogenolysis by 2,5-anhydro-D-mannitol.
45 Citations1984R.L. Hanson, Robert S. Ho +4 more
The phosphate esters of 2,5-anhydro-D-mannitol would, therefore, be expected to inhibit glycogenolysis and gluconeogenesis and stimulate glycolysis in liver.
BiochemistryBinding of hexose bisphosphates to muscle phosphofructokinase
44 Citations1983Lawrence G. Foe, Steven P. Latshaw +1 more
Equilibrium binding experiments showed that both fructose bisphosphates bind to phosphofructokinase with negative cooperativity; the affinity for fructose 2,6-bisphosphate was about 1 order of magnitude greater than the affinity on the basis of kinetic activationAssays concluded that the sugar bisph phosphate bind to a single site on the enzyme.
Journal of Clinical InvestigationTime course and significance of changes in hepatic fructose-2,6-bisphosphate levels during refeeding of fasted rats.
43 Citations1984M Kuwajima, Christopher B. Newgard +2 more
The time course of changes in hepatic fructose-2,6-bisphosphate and glycogen content was examined in fasted rats infused with glucose intragastrically or allowed to eat a chow diet ad lib, indicating that much of the glycogen deposited in liver in the early postprandial phase is gluconeogenic in origin.
Journal of Biological ChemistryInfluence of polyethylene glycols on the kinetics of rat liver phosphofructokinase.
43 Citations1980Gregory D. Reinhart
The results support the proposal that more aggregated forms of rat liver phosphofructokinase have a decreased Km value for fructose 6-phosphate when assayed with inhibiting concentrations of MgATP.
Biochemical JournalStimulation of glycolysis and accumulation of a stimulator of phosphofructokinase in hepatocytes incubated with vasopressin
43 Citations1981Louis Hue, Emile Van Schaftingen +1 more
Vasopressin stimulates glycolysis in hepatocytes prepared from fed rats, or from starved rats when incubated with glucose, which is probably fructose 2,6-bisphosphate, the recently discovered stimulatory of phosphofructokinase.
American Journal of Physiology-Endocrinology and MetabolismInhibition of hepatic glucose production by insulin in vivo in rats: contribution of glycolysis
42 Citations1986J. Terrettaz, F. Assimacopoulos‐Jeannet +1 more
In normal rat liver, when glycemia is maintained at constant basal level, insulin promotes no change in glycogen metabolism, whereas the hormone stimulates the glycolytic pathway, which contributes to the suppression of hepatic glucose production observed after the addition of the hormone.
Biochemical JournalRole of fructose 2,6-bisphosphate in the control by glucagon of gluconeogenesis from various precursors in isolated rat hepatocytes
39 Citations1984Louis Hue, Ramón Bartrons
The extent of inactivation of pyruvate kinase by glucagon was not affected by the presence of the various gluconeogenic precursors and the role of fructose 2,6-bisphosphate in the effect of glucagon on gluconeogenesis from precursor entering the pathway at the level of triose phosphates or pyruVate is discussed.
Biochemical JournalPhosphorylation of purified bovine heart and rat liver 6-phosphofructo-2-kinase by protein kinase C and comparison of the fructose-2,6-bisphosphatase activity of the two enzymes
39 Citations1986Mark H. Rider, Louis Hue
The bovine heart enzyme contains 10 times less fructose 2,6-bisphosphatase activity and is phosphorylated at a slower rate and to a lesser extent than the liver enzyme.
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