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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Glucose and fructose were studied in eight healthy volunteers who fasted twice for 4 days. Before and after the fasts each subject received a 4-hr glucose or fructose infusion providing 0.5 g/kg/hr. Glucose infusion during starvation resulted in a mean maximal plasma glucose rise of 401 +/- 21 mg/100 ml (+/- SEM) as compared to 119 +/- 10 mg/100 ml before starvation. Insulin/glucose ratios were lower than normal in fasted subjects. Fructose infusion during fasting produced a maximal plasma glucose rise of 91 +/- 9 mg/100 ml as opposed to 5+/-1 mg/100 ml before starvation. During fructose infusion in the fasted state, plasma fructose levels were higher than control and the rise in blood lactate and pyruvate was delayed, but finally lactate concentrations were above control values. The antiketotic effects of intravenous glucose and fructose were similar during fasting but fructose was significantly less potent in reducing free fatty acid levels. After starvation, urinary carbohydrate losses during glucose infusion were 5 times higher than those observed during fructose infusion. Thus, fructose utillization was less impaired during fasting than was glucose utilization, although fasting induced abnormalities in both glucose and fructose metabolism.
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PMID:Comparison of glucose and fructose tolerance before and after starvation. 90 56

Extracts of Acetobacter xylinum catalyze the phosphorylation of glycerol and dihydroxyacetone (DHA) by adenosine 5'-triphosphate (ATP) to form, respectively, L-alpha-glycerophosphate and DHA phosphate. The ability to promote phosphorylation of glycerol and DHA was higher in glycerol-grown cells than in glucose- or succinate-grown cells. The activity of glycerol kinase in extracts is compatible with the overall rate of glycerol oxidation in vivo. The glycerol-DHA kinase has been purified 210-fold from extracts, and its molecular weight was determined to be 50,000 by gel filtration. The glycerol kinase to DHA kinase activity ratio remained essentially constant at 1.6 at all stages of purification. The optimal pH for both reactions was 8.4 to 9.2. Reaction rates with the purified enzyme were hyperbolic functions of glycerol, DHA, and ATP. The Km for glycerol is 0.5 mM and that for DHA is 5 mM; both are independent of the ATP concentration. The Km for ATP in both kinase reactions is 0.5 mM and is independent of glycerol and DHA concentrations. Glycerol and DHA are competitive substrates with Ki values equal to their respective Km values as substrates. D-Glyceraldehyde and l-Glyceraldehyde were not phosphorylated and did not inhibit the enzyme. Among the nucleotide triphosphates tested, only ATP was active as the phosphoryl group donor. Fructose diphosphate (FDP) inhibited both kinase activities competitively with respect to ATP (Ki= 0.02 mM) and noncompetitively with respect to glycerol and DHA. Adenosine 5'-diphosphate (ADP) and adenosine 5'-monophosphate (AMP) inhibited both enzymic activities competitively with respect to ATP (Ki (ADP) = 0.4 mM; Ki (AMP) =0.25 mM). A. xylinum cells with a high FDP content did not grow on glycerol. Depletion of cellular FDP by starvation enabled rapid growth on glycerol. It is concluded that a single enzyme from A. xylinum is responsible for the phosphorylation of both glycerol and DHA. This as well as the sensitivity of the enzyme to inhibition by FDP and AMP suggest that it has a regulatory role in glycerol metabolism.
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PMID:Phosphorylation of glycerol and dihydroxyacetone in Acetobacter xylinum and its possible regulatory role. 95 17

1. Adult, female Xenopus laevis were subjected to 12 months of starvation. 2. Starvation resulted in a continuous reduction in the activity of both hepatic and renal glucose-6-phosphate dehydrogenase. 3. Fructose-1,6-diphosphatase was significantly reduced at months 10 and 12 in the liver, and at months 4, 10, and 12 in the kidney. 4. Pyruvate kinase activity of muscle and liver decreased during the experimental period whereas the renal enzyme remained essentially unchanged. 5. Both hepatic and renal glutamate-pyruvate transaminase (GPT) and hepatic glutamate-oxaloacetate transaminase (GOT) showed a reduction of activity after 2 and 4 months of starvation followed by an increase in GPT but not in GOT.
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PMID:Long-term starvation in Xenopus laevis Daudin--III. Effects on enzymes in several tissues. 255 3

Activity of the main enzymes of gluconeogenesis under food thiamine deficiency was studied in tissues of satiated and 48-hour starved rats. Starvation of control rats (with no vitamin B1-deficiency) led to increased activity of glucose 6-phosphatase (G-6-P) in the liver, kidney and small intestinal mucosa, and of phosphoenolpyruvate carboxykinase (PEPCK) in the liver and kidneys. Fructose 1,6-diphosphatase (F-D-P) activity in the control animals was not changed in the liver and kidneys but decreased in the small intestinal mucosa. Starvation of the test animals (with vitamin B1-deficiency) was attended by increased G-6-P and PEPCK activity in the liver and kidneys, and F-D-P activity in the liver. Thiamine deficiency led to lowered G-6-P and F-D-P activities in the liver and kidneys and PEPCK in the liver of the test animals as compared to the control. The data obtained have evidenced disorders in the gluconeogenesis under conditions of vitamin B1-deficiency.
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PMID:[Enzyme activity of gluconeogenesis in dietary thiamine deficiency]. 283 78

The occurrence of fructose 2,6-bisphosphate was detected in Dictyostelium discoideum. The levels of this compound were compared with those of cyclic AMP and several glycolytic intermediates during the early stages of development. Removal of the growth medium and resuspension of the organism in the differentiation medium decreased the content of fructose 2,6-bisphosphate to about 20% within 1 h, remaining low when starvation-induced development was followed for 8 h. The content of cyclic AMP exhibited a transient increase that did not correlate with the change in fructose 2,6-bisphosphate. If after 1 h of development 2% glucose was added to the differentiation medium, fructose 2,6-bisphosphate rapidly rose to similar levels to those found in the vegetative state, while the increase in cyclic AMP was prevented. The contents of hexose 6-phosphates, fructose 1,6-bisphosphate and triose phosphates changed in a way that was parallel to that of fructose 2,6-bisphosphate, and addition of sugar resulted in a large increase in the levels of these metabolites. The content of fructose 2,6-bisphosphate was not significantly modified by the addition of the 8-bromo or dibutyryl derivatives of cyclic AMP to the differentiation medium. These results provide evidence that the changes in fructose 2,6-bisphosphate levels in D. discoideum development are not related to a cyclic-AMP-dependent mechanism but to the availability of substrate. Fructose 2,6-bisphosphate was found to inhibit fructose-1,6-bisphosphatase activity of this organism at nanomolar concentrations, while it does not affect the activity of phosphofructokinase in the micromolar range. The possible physiological implications of these phenomena are discussed.
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PMID:Fructose 2,6-bisphosphate in Dictyostelium discoideum. Independence of cyclic AMP production and inhibition of fructose-1,6-bisphosphatase. 302 83

The provision of small amounts of glucose during fasting is known to spare body protein and to attenuate markedly the metabolic response to starvation. These actions, which are not shared by fat, are generally thought to depend on the ability of exogenous glucose to stimulate insulin secretion. To determine whether fructose, a very weak insulin secretagogue, will also conserve nitrogen and alter the response to fasting, we infused small amounts of fructose, 100 g/d (375 kcal), into 7 obese subjects during a 10-day fast: 4 received fructose days 7 to 10, and 3 received fructose days 1 to 7. Fructose virtually abolished (all P less than 0.05-0.01) the fasting induced: (a) fall in glucose and insulin and rise in glucagon, (b) fall in triiodothyronine, (c) ketosis and acidosis, (d) increased ammonia excretion, (e) hyperuricemia (and hypouricosuria), and (f) fall in plasma alanine and rise in branched chain amino acids. Fructose also significantly reduced urinary sodium loss. Moreover, fructose exerted a prominent protein-sparing action, even though plasma insulin concentrations never exceeded postabsorptive levels. Excretion of total nitrogen was reduced by 40% to 50% during periods of fructose infusion, reflecting significant suppression of both urea and ammonia generation (all P less than 0.05-0.01). Most plasma glucogenic amino acids rose significantly during fructose administration. We conclude that low-dose fructose infusion essentially abolishes the entire hormone-substrate response to fasting, and spares body protein without raising insulin above postabsorptive levels.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Nitrogen conservation in starvation revisited: protein sparing with intravenous fructose. 351 Mar 63

1. Measurements of the activities in rat liver of the four key enzymes involved in gluconeogenesis, i.e. pyruvate carboxylase (EC 6.4.1.1), phosphoenolpyruvate carboxykinase (EC 4.1.1.32), fructose 1,6-diphosphatase (EC 3.1.3.11) and glucose 6-phosphatase (EC 3.1.3.9), have been carried out, all four enzymes being measured in the same liver sample. Changes in activities resulting from starvation and diabetes have been studied. Changes in concentration (activity/unit wet weight of tissue) were compared with changes in the hepatic cellular content (activity/unit of DNA). 2. Each enzyme was found to increase in concentration during starvation for up to 3 days, but only glucose 6-phosphatase and phosphoenolpyruvate carboxykinase showed a significant rise in content. Fructose 1,6-diphosphatase appeared to decrease in content somewhat during the early stages of starvation. 3. There was a marked increase in the concentration of all four enzymes in non-starved rats made diabetic with alloxan or streptozotocin, for the most part similar responses being found for the two diabetogenic agents. On starvation, however, the enzyme contents in the diabetic animals tended to fall, often with streptozotocin-treated animals to values no greater than for the normal overnight-starved rat. Deprivation of food during the period after induction of diabetes with streptozotocin lessened the rise in enzyme activity. 4. The results are compared with other published values and factors such as substrate and activator concentrations likely to influence activity in vivo are considered. 5. Lack of correlation of change in fructose 1,6-diphosphatase with the other enzymes questions whether it should be included in any postulation of control of gluconeogenic enzymes by a single gene unit.
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PMID:A comparison of the effects of diabetes induced with either alloxan or streptozotocin and of starvation on the activities in rat liver of the key enzymes of gluconeogenesis. 432 34

The phosphofructokinase stabilizing factor, believed to be a peptide of molecular weight 3,800 (Dunaway G.A. and Segal H.L., 1976, J. Biol. Chem. 251, 2323-2329), shares many chemical and biological properties with fructose 2,6-bisphosphate. It co-migrated with it upon gel filtration in the molecular weight range 300-400 or 3,000-4,000 depending upon the ionic strength of the solution. Fructose 2,6-bisphosphate is the most potent phosphofructokinase stabilizing agent present in the liver of a fed rat. Its disappearance during fasting and diabetes could account for the faster rate of degradation of phosphofructokinase reported to occur under these conditions. The effect of starvation to decrease by 60% the phosphofructokinase content of the liver is, however, for its greatest part, related to a non-specific decrease in liver mass.
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PMID:The role of fructose 2,6-bisphosphate in the long-term control of phosphofructokinase in rat liver. 622 34

We have examined the role of fructose as a substrate for the mammalian lung. Isolated and ventilated rat lungs were perfused for 2 h in the presence of either [U-14C]- or [5-3H]fructose. Fructose utilization, 3H2O production, and lactate and pyruvate production were measured. Insulin had no effect on the production of radiolabeled lactate. The 14C label from [U-14C]fructose was incorporated into the neutral lipids, phospholipids, fatty acid moiety, and deacylated fraction of lung. The apparent Km and maximum velocity of enzyme reaction for fructose utilization were 0.5 mM and 75 nmol X h-1 X g dry wt-1, respectively. Recovery of fructose 1-phosphate and fructose 1,6-diphosphate after perfusion with fructose, as well as detection of fructokinase, aldolase, and triokinase activities in the lung homogenates, suggested that fructose had been metabolized via phosphorylation through fructose 1-phosphate. Activities of fructose-metabolizing enzymes were not altered by the induction of diabetes, hypophysectomy, or starvation. These results suggest that mammalian lungs may utilize fructose to synthesize fatty acids, which in turn are used for phospholipid biosynthesis. The utilization of fructose by lung does not seem to be affected by nutritional or hormonal conditions.
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PMID:Fructose utilization by lung. 632 66

A specific fructose uptake system (Km = 0.4 mM) appeared in Neurospora crassa when glucose-grown mycelia were starved. Fructose uptake had kinetics different from those of intramycelial fructose phosphorylation, and uptake appeared to be carrier mediated. The only sugar which competitively inhibited fructose uptake was L-sorbose (Ki = 9 mM). Glucose, 2-deoxyglucose, mannose, and 3-O-methyl glucose were noncompetitive inhibitors of fructose uptake. Incubation of glucose-grown mycelia with glucose, 2-deoxyglucose, or mannose prevented derepression of the fructose transport system, whereas incubation with 3-O-methyl glucose caused the appearance of five times as much fructose uptake activity as did starvation conditions.
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PMID:Fructose transport in Neurospora crassa. 644 95


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