Search results for "Fructosediphosphates"

showing 10 items of 12 documents

Regulatory properties of 6-phosphofructokinase and control of glycolysis in boar spermatozoa.

2007

Glycolysis is crucial for sperm functions (motility and fertilization), but how this pathway is regulated in spermatozoa is not clear. This prompted to study the location and the regulatory properties of 6-phosphofructokinase (PFK, EC 2.7.1.11), the most important element for control of glycolytic flux. Unlike some other glycolytic enzymes, PFK showed no tight binding to sperm structures. It could readily be extracted from ejaculated boar spermatozoa by sonication and was then chromatographically purified. At physiological pH, the enzyme was allosterically inhibited by near-physiological concentrations of its co-substrate ATP, which induced co-operativity, i.e. reduced the affinity for the …

MaleEmbryologySwinePhosphofructokinase-1Allosteric regulationImmunoblottingMotilityBiologychemistry.chemical_compoundEndocrinologyAdenosine TriphosphateAllosteric RegulationFructosediphosphatesAnimalsGlycolysisCitrateschemistry.chemical_classificationObstetrics and GynecologyFructoseCell BiologyHydrogen-Ion ConcentrationSpermImmunohistochemistrySpermatozoaAdenosine MonophosphateEnzymeReproductive MedicinechemistryBiochemistryFlagellaElectrophoresis Polyacrylamide GelFlux (metabolism)AcrosomeGlycolysisPhosphofructokinaseReproduction (Cambridge, England)
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase from frog skeletal muscle: purification, kinetics and immunological properties.

1993

Fructose 2,6-bisphosphate is the most potent activator of 6-phosphofructo-1-kinase, a key regulatory enzyme of glycolysis in animal tissues. This study was prompted by the finding that the content of fructose 2,6-bisphosphate in frog skeletal muscle was dramatically increased at the initiation of exercise and was closely correlated with the glycolytic flux during exercise. 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, the enzyme system catalyzing the synthesis and degradation of fructose 2,6-bisphosphate, was purified from frog (Rana esculenta) skeletal muscle and its properties were compared with those of the rat muscle type enzyme expressed in Escherichia coli using recombinant DN…

PhysiologyPhosphofructokinase-2BiologyBiochemistrychemistry.chemical_compoundEndocrinologymedicineFructosediphosphatesAnimalsGlycolysisPhosphorylationEcology Evolution Behavior and Systematicschemistry.chemical_classificationMolecular massImmunochemistryMusclesPhosphotransferasesSkeletal muscleRana esculentaFructoseHydrogen-Ion ConcentrationMolecular WeightKineticsmedicine.anatomical_structureEnzymechemistryFructose 26-bisphosphateBiochemistryGRENOUILLEAnimal Science and ZoologyPhosphoenolpyruvate carboxykinaseProtein KinasesJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology
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Differential function of the phosphoglucomutase isozymes PGM1 and PGM2

1979

A total of 13 metabolites thought to be possibly inhibitory were tested for their influence on PGM isozyme activities, each at several different concentrations. The analysis of statistical significance was based on enzyme activities obtained by densitometric measurements of starch gels. Five of the substances were found to inhibit PGM activity, three of which definitely and a further one probably led to a significantly stronger inhibition of the isozymes of the PGM2 locus than of PGM1 isozymes. They are (1) fructose-1,6-diphosphate, (2) adenosine triphosphate, (3) citrate, and (4) possibly 2,3-diphosphoglycerate. Thus, PGM1 isozymes proved to function better in hard or perhaps marginal meta…

chemistry.chemical_classificationStarchChromosome MappingLocus (genetics)BiologyDiphosphoglyceric AcidsMolecular biologyIsozymeIsoenzymeschemistry.chemical_compoundAdenosine TriphosphateEnzymeGenesPhosphoglucomutasechemistryBiochemistryPGM1FructosediphosphatesGeneticsHumansPhosphoglucomutaseCitratesAdenosine triphosphateGeneGenetics (clinical)Human Genetics
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Antagonistic effects of hypertrehalosemic neuropeptide on the activities of 6-phosphofructo-1-kinase and fructose-1,6-bisphosphatase in cockroach fat…

2001

Hypertrehalosemic neuropeptides from the corpora cardiaca such as the decapeptide Bld HrTH bring about a profound switch in the metabolic activity of cockroach fat body during which production of the blood sugar trehalose is stimulated while the catabolism of carbohydrate (glycolysis) is inhibited. The mechanisms of the metabolic switch are not fully understood. Incubation of isolated fat body from the cockroach Blaptica dubia with 10(-8) M Bld HrTH, for 10-60 min, stimulated glycogen breakdown and increased the content of the substrates of both the glycolytic enzyme 6-phosphofructo-1-kinase (PFK, EC 2.7.1.11) and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase, EC 3.1.3.11) in…

Malemedicine.medical_specialtyBlaptica dubiaPhosphofructokinase-1Fat BodyFructose 16-bisphosphataseCockroachesIn Vitro TechniquesBiologyBiochemistryGene Expression Regulation Enzymologicchemistry.chemical_compoundInternal medicineFructosediphosphatesmedicineAnimalsGlycolysisPhosphofructokinase 1Molecular BiologyCatabolismNeuropeptidesTrehaloseFructosebiology.organism_classificationAdenosine MonophosphateFructose-BisphosphataseKineticsEndocrinologyFructose 26-bisphosphatechemistryBiochemistryInsect HormonesInsect Sciencebiology.proteinGlycogenPhosphofructokinaseInsect Biochemistry and Molecular Biology
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Central Modulatory Neurons Control Fuel Selection in Flight Muscle of Migratory Locust

2003

Insect flight is one of the most intense and energy-demanding physiological activities. High carbohydrate oxidation rates are necessary for take-off, but, to spare the limited carbohydrate reserves, long-distance flyers, such as locusts, soon switch to lipid as the main fuel. We demonstrate that before a flight, locust muscles are metabolically poised for take-off by the release of octopamine from central modulatory dorsal unpaired median (DUM) neurons, which increases the levels of the potent glycolytic activator fructose 2,6-bisphosphate in flight muscle. Because DUM neurons innervating the flight muscles are active during rest but selectively inhibited during flight, they stimulate carbo…

Central Nervous SystemMalemedicine.medical_specialtyGrasshoppersBrief CommunicationInsect flightCarbohydrate catabolismInternal medicinemedicineFructosediphosphatesPremovement neuronal activityAnimalsGlycolysisProtein kinase AMuscle SkeletalOctopamineNeuronsbiologyGeneral NeuroscienceMigratory locustbiology.organism_classificationCyclic AMP-Dependent Protein KinasesEndocrinologyFlight AnimalOctopamine (neurotransmitter)FemaleGlycolysisLocustSignal Transduction
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Effects of glucocorticoid excess on the sensitivity of glucose transport and metabolism to insulin in rat skeletal muscle.

1997

This study examines the mechanisms of glucocorticoid-induced insulin resistance in rat soleus muscle. Glucocorticoid excess was induced by administration of dexamethasone to rats for 5 days. Dexamethasone decreased the sensitivity of 3-O-methylglucose transport, 2-deoxyglucose phosphorylation, glycogen synthesis and glucose oxidation to insulin. The total content of GLUT4 glucose transporters was not decreased by dexamethasone; however, the increase in these transporters in the plasma membrane in response to insulin (100 m-units/litre) was lessened. In contrast, the sensitivity of lactate formation to insulin was normal. The content of 2-deoxyglucose in the dexamethasone-treated muscle was …

Malemedicine.medical_specialtyMonosaccharide Transport Proteinsmedicine.medical_treatmentBlotting WesternGlucose-6-PhosphateMuscle ProteinsDeoxyglucoseBiochemistryDexamethasonechemistry.chemical_compoundInsulin resistanceInternal medicineHexokinasemedicineFructosediphosphatesAnimalsInsulinGlycolysisLactic AcidPhosphorylationRats WistarGlycogen synthaseMuscle SkeletalMolecular BiologyGlucocorticoidsHexokinaseGlucose Transporter Type 4biologyInsulinGlucose transporterCell BiologyMetabolismmedicine.diseaseRatsEndocrinologyGlucosechemistrybiology.protein3-O-MethylglucoseGLUT4GlycogenResearch Article
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Fructose 2,6-bisphosphate and glycolytic flux in skeletal muscle of swimming frog

1990

AbstractGlycolytic 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 appea…

medicine.medical_specialtyPhosphofructokinase-1Rana temporariaBiophysicsSkeletal musclePhysical exerciseMotor ActivityBiologyBiochemistrychemistry.chemical_compoundStructural BiologyInternal medicineFructosediphosphatesGeneticsmedicineAnimalsGlycolysisLactic AcidExerciseMolecular BiologySwimmingchemistry.chemical_classificationMusclesSkeletal muscleFructoseCell BiologyEnzyme ActivationKineticsFructose 26-bisphosphateEndocrinologymedicine.anatomical_structureEnzymeBiochemistrychemistryFructose 26-bisphosphateLactates6-PhosphofructokinaseAnuraHexosediphosphatesGlycolysisFlux (metabolism)PhosphofructokinaseFEBS Letters
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Thimerosal induces calcium mobilization, fructose 2,6-bisphosphate synthesis and cytoplasmic alkalinization in rat thymus lymphocytes

1991

The effect of thimerosal on intracellular calcium ([Ca2+]i), pH (pHi) and fructose 2,6-bisphosphate (Fru 2,6-P2) in thymus lymphocytes was investigated. The effect of thimerosal on cell growth was also examined. Thimerosal produced a dose-dependent increase in [Ca2+]i, pHi and in the level of fructose 2,6-bisphosphate. Thimerosal was, however, unable to produce cell proliferation and inhibited [3H]thymidine incorporation when cells were challenged with PHA and costimulator. In the absence of external calcium, thimerosal produced only a slight increase in [Ca2+]i. In Na(+)-containing buffer, thimerosal induced an initial acidification (0.05 +/- 0.01 pH units), followed by an alkalinization o…

Malemedicine.medical_specialtyCytoplasmT-LymphocytesFluorescence spectrometrychemistry.chemical_elementBiologyCalciumLymphocyte ActivationTritiumCalcium in biologychemistry.chemical_compoundInternal medicinemedicineFructosediphosphatesAnimalsLactic AcidMolecular BiologyIon transporterProtein kinase CThimerosalSodiumThimerosalFructoseRats Inbred StrainsCell BiologyHydrogen-Ion ConcentrationRatsEndocrinologyFructose 26-bisphosphatechemistryLactatesCalciumGlycolysisHydrogenThymidine
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Effects of insulin-like growth factor I on the rates of glucose transport and utilization in rat skeletal muscle in vitro.

1992

1. The effects of insulin-like growth factor I (IGF-I) on the rates of glucose transport and utilization and its interaction with insulin were investigated in rat soleus muscle in vitro. IGF-I increased the rates of glucose transport, lactate formation, glycogen synthesis and the flux of glucose to hexose monophosphate, but it had no effect on the rate of glucose oxidation or glycogenolysis. 2. In the absence of insulin, low levels of IGF-I (0-30 ng/ml) increased the rate of glycolysis and the content of fructose 2,6-bisphosphate, but the content of glucose 6-phosphate remained unaltered; at higher levels of IGF-I (300-3000 ng/ml) the rate of glycolysis and the content of fructose 2,6-bisph…

Malemedicine.medical_specialtyGlycogenolysismedicine.medical_treatmentGlucose-6-PhosphateBiologyIn Vitro TechniquesBiochemistrychemistry.chemical_compoundInternal medicinemedicineFructosediphosphatesAnimalsInsulinGlycolysisInsulin-Like Growth Factor IPhosphorylationGlycogen synthaseMolecular BiologyGlycogenInsulinMusclesGlucose transporterGlucosephosphatesFructoseBiological TransportRats Inbred StrainsCell BiologyRatsKineticsEndocrinologyGlucosechemistryFructolysisbiology.proteinGlycolysisOxidation-ReductionGlycogenResearch Article
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Photoaffinity Labeling and Photoaffinity Cross-Linking of Phosphofructokinase-1 from Saccharomyces cerevisiae by 8-Azidoadeninenucleotides

2001

Phosphofructokinase-1 from Saccharomyces cerevisiae is composed of four alpha- and four beta-subunits, each of them carrying catalytic and regulatory bindings sites for MgATP. In this paper, various photoaffinity labels, such as 8-azidoadenosine 5'-triphosphate, 8-azido-1,N6-ethenoadenosine 5'-triphosphate, and 8-N3-3'(2')-O-biotinyl-8-azidoadenosine 5'-triphosphate have been used to study their interaction with the enzyme in the dark and during irradiation. All nucleotidetriphosphates function as phosphate donor forming fructose 1,6-bisphosphate from fructose 6-phosphate. However, the kinetic analysis revealed distinctly differences between them. Photolabeling causes a decrease in enzyme a…

LightPhosphofructokinase-1Blotting WesternSaccharomyces cerevisiaeBiophysicsPhotoaffinity LabelsSaccharomyces cerevisiaePhotoaffinity LabelsBiochemistryAdenosine TriphosphateFructosediphosphatesChymotrypsinMagnesiumPhosphofructokinase 1Molecular Biologychemistry.chemical_classificationGel electrophoresisBinding SitesAffinity labelingbiologyPhotoaffinity labelingFructosephosphatesDarknessbiology.organism_classificationEnzyme assayKineticsProtein SubunitsCross-Linking ReagentsEnzymechemistryBiochemistrybiology.proteinElectrophoresis Polyacrylamide GelArchives of Biochemistry and Biophysics
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