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

Activity of dehydrogenases related to pentosephosphate pathway was not distinctly altered in soluble fraction of kidney cortex and medulla after 48 and 72 hrs of starvation. In diabetes the activity of these enzymes in rat kidney, as distinct from liver tissue, was not decreased but it was elevated and within 72 hrs after administration of alloxan the activity of glucose-6-phosphate dehydrogenase was increased 2-fold and the activity of 6-phosphogluconate dehydrogenase was increased by 30% above the normal level. Content of free fatty acids was also increased in kidney cortex of diabetic rats within 72 hrs after administration of alloxan. Alterations in content of free fatty acids were not observed either in kidney of diabetic animals within other studied periods (6 and 14-16 days) of treatment or in the tissue of starved rats. The data obtained suggest that free fatty acids do not participate immediately in controlling effect on dehydrogenases of pentosephosphate pathway in kidney in vivo.
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PMID:[Effect of starvation and diabetes on the activity of glucose-6-phosphate and 6-phosphogluconate dehydrogenases and on the free fatty acid content of rat kidney cortex and medulla]. 66 69

Meal-feeding of a high sucrose diet produces a diurnal cycle (i.e., food response) in glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) levels resulting in an elevated level of these enzymes at approximately 12 hours after the start of a 2-hour meal and a return to base level by 24 hours. The effects of actinomycin D and cycloheximide on the 12-hour increases in G6PD and 6GPD were determined. Cycloheximide completely blocked the increase in G6PD if administered 2 or 4 hours after start of the meal, while actinomycin D completely blocked the increase in G6PD if administered at 2 hours and almost completely at 4 hours after start of the meal. These results were obtained previously with starved rats refed a sucrose diet. The diurnal increases in G6PD and 6PGD in meal-fed rats and the induction of G6PD in starved-refed rats thus appear to be regulated by the same mechanism requires RNA synthesis within 4 hours after start of re-feeding. The response of 6PGD to cycloheximide and to actinomycin D at 2 or 4 hours after start of the meal is essentially the same as that of G6PD. These data suggest that the increases in G6PD and 6PGD (and other enzymes) brought about by carbohydrate refeeding AFTER starvation or by carbohydrate meal-feeding on a diurnal cycle are mediated by a rapid change in RNA synthesis. This appears most compatible with a coordinate control of gene expression through messenger RNA synthesis.
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PMID:Regulation of glucose-6 phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in the meal-fed rat. 117 Feb 87

The effects of one vs. two episodes of starvation-refeeding were studied in young male rats as a function of elapsed time between the two episodes of starvation-refeeding. Starved-refed rats ate more and gained weight faster than ad libitum-fed rats. The difference in weight gains could be attributed to the greater amount of body fat in the starved-refed rats. The responses of four NADP-linked liver dehydrogenases:isocitrate dehydrogenase (ICD)/LS-isocitrate:NADP oxidoreductase (decarboxylating) (EC 1.1.1.42), glucose-6-phosphate dehydrogenase (G6PD)/D-glucose-6-phosphate:NADP oxidoreductase (EC 1.1.1.49); 6-phosphogluconate dehydrogenase (6PGD/6-phospho-D-gluconate:NADP oxidoreductase (decarboxylating) (EC 1.1.1.44); and malic enzyme (ME)/L-malate:NADP oxidoreductase (decarboxylating) (EC 1.1.1.40) were studied. Starvation-refeeding caused an overshoot of G6PD, 6PGD, and ME, but not of ICD. A second episode of starvation caused an even greater enzyme overshoot; this difference persisted for 3 weeks with G6PD and for 2 weeks with 6PGD and ME. No significant differences in blood cholesterol were detected.
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PMID:Long-term effects of starvation-refeeding in the rat. 122 70

The maximum activities of some key enzymes of metabolism were studied in lungs of fed and 48-h-starved rats. The maximum activity of hexokinase in the lung is similar to that of other tissues of the body, but lower than that of phosphorylase and 6-phosphofructokinase. High activities of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were found in lung tissue, suggesting the importance of the pentose phosphate pathway in the lung. The activities of hexokinase and 6-phosphofructokinase were decreased whereas that of phosphorylase increased in response to starvation. Of the enzymes of the tricarboxylic acid cycle whose activities were measured, that of oxoglutarate dehydrogenase was the lowest, yet its activity (approximately 4.2 nmol/min per mg protein at 37 degrees C) was considerably greater than the flux through the cycle (0.46 nmol/min per mg protein at 37 degrees C; calculated from oxygen consumption by incubated lung slices). The activities of both oxoglutarate dehydrogenase and citrate synthase were decreased by starvation. The activities of 3-oxoacid CoA-transferase and acetoacetyl-CoA thiolase were low in lung tissue compared to those of other tissues (eg kidney, brain) and that of 3-hydroxybutyrate dehydrogenase was very low. The activity of carnitine palmitoyl transferase is higher in the lung, suggesting that fatty acids (and possibly acetoacetate) could provide acetyl-CoA as substrate for the tricarboxylic acid cycle. Very low rates of utilization of 3-hydroxybutyrate were observed during incubation of lung slices, but that of oleate was 1.2 nmol/h per mg of protein.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Metabolism of glucose, glutamine, long-chain fatty acids and ketone bodies by lungs of the rat. 176

Both starvation and refeeding and exercise and detraining are procedures that result in lowered lipid stores followed by their refilling. Rats subjected to these procedures were evaluated for their ability to produce hepatic biosynthetic reducing equivalents. Five-week-old male Osborne-Mendel rats were exercised on a motorized treadmill for 6 wk (final speed 27 m/min, 60 min/day, 6 day/wk) or kept sedentary. Exercised and sedentary rats were starved for 48 h or fed ad libitum. After treatments, some rats in each group were killed. Remaining exercised animals were detrained or detrained and refed. Remaining sedentary rats were refed. Activities of hepatic glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and malic enzyme were evaluated. Plasma glucose, triglyceride, insulin, liver triglyceride, and body composition were determined. Results indicate that changes in lipids stores associated with starvation and refeeding and exercise and detraining are not associated with similar changes in enzyme activity. Starvation resulted in lowered plasma glucose, triglyceride, and insulin. Starvation and all exercise treatments resulted in lowered carcass fat. Exercised rats who were starved for 48 h and then detrained and refed for 72 h had the greatest liver weights and percent liver triglycerides. This was not associated with similar changes in enzyme activity. Increased liver lipid and decreased carcass fat may indicate a redistribution of lipid stores in these animals.
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PMID:Effects of exercise, detraining, starvation, and refeeding on lipogenic capacity of Osborne-Mendel rat. 335 13

The objective of these studies was to determine how alterations in dietary carbohydrate affect hepatic glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH) and malic enzyme (ME) activities in adult female rats. Rats were either starved 2 d and then refed a nonpurified diet or a purified 65% carbohydrate diet (glucose, sucrose, fructose or cornstarch) for 3 d, or switched from nonpurified to purified diets for 3 d. Liver G6PDH, 6PGDH and ME activities were determined. In males, enzyme activities were 8- to 12-fold and 3-fold higher when starved and refed purified diets and nonpurified diets, respectively, whereas in females, activities were 2- to 3-fold higher only when refed purified diets. Both genders had higher enzyme activities when shifted to purified diets. Females responded less dramatically than males. Of the higher enzyme activities observed during starvation-refeeding studies, in females 58-65% of the change is a function of switching rats from nonpurified to purified diets. In contrast, in males only 24-40% of the higher activities could be attributed to diet shifting. Results of these studies indicate that the effects of dietary carbohydrates on hepatic G6PDH, 6PGDH and ME activities are gender dependent.
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PMID:Gender-linked differences in dietary induction of hepatic glucose-6 phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and malic enzyme in the rat. 376 Oct 10

Adult female Sprague-Dawley rats were either prefed ground nonpurified diet, starved 48 h, then refed a purified carbohydrate diet for 72 h or shifted from ground nonpurified diet directly to a purified carbohydrate diet for 72 h. Diets were formulated to contain 65% carbohydrate either as the disaccharides maltose or sucrose or as their respective monosaccharide equivalents glucose and invert sugar (glucose: fructose, 1:1). Alternations in hepatic glucose 6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH) and malic enzyme (ME) activities, relative liver size and food efficiency were determined. Rats starved and refed invert sugar had higher levels of G6PDH and ME than those red glucose, indicating a positive fructose effect. The greatest changes in hepatic enzyme activities were observed in rats consuming diets containing sucrose. Positive fructose and disaccharide effects were obtained with sucrose for all enzymes studied in both dietary shift and starve-refeed studies. No disaccharide effect was observed with maltose. In conclusion, females did not display a generalized disaccharide effect with either dietary shifting or starvation refeeding.
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PMID:Absence of a generalized disaccharide effect in adult female rats. 376 Oct 11

Responses of the hepatic lipogenic enzymes, glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH), and malic enzyme (ME) to starvation refeeding and diet shifting were determined in lean and obese female Zucker rats. Rats were either fed nonpurified diet, starved 48 hr, and then refed nonpurified diet or one of the refined carbohydrate diets containing either glucose, fructose, cornstarch, or sucrose for 72 hr, or shifted from nonpurified diet directly to one of the refined carbohydrate diets for 72 hr. Initial activities were greater in obese than lean rats for all three enzymes studied. Similar to other strains of female rats, lean Zucker rats failed to demonstrate a starve-refeed response when refed nonpurified diet. Obese female littermates showed a statistically significant increase in enzymes when refed a nonpurified diet. Both lean and obese female Zucker rats demonstrated increases in enzyme activities above controls when starved and refed any of the refined carbohydrate diets. The greatest responses were observed when female rats were starved and refed sucrose; activities increased 2.6- to 3.5-fold in lean and 3.0- to 4.3-fold in obese Zuckers. In lean females 50-70% of the starve-refeed response observed with G6PDH and ME can be accounted for by simply shifting from a nonpurified diet to the respective refined carbohydrate diet, whereas in obese females only 33-55% of the increase could be attributed to diet shifting. Plasma testosterone/estrogen ratios were consistently 1.5 times higher in obese than in lean female rats. This phenotypic difference may potentiate the heightened starve-refeed overshoot response observed in obese rats.
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PMID:Dietary induction of hepatic glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and malic enzyme in lean and obese female Zucker rats. 382 5

Insulin treatment of virgin female rats increased the hepatic activity of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase to levels 3.4 and 1.5 fold higher than controls. The increase in glucose 6-phosphate dehydrogenase activity was attributed to increased activity of all three dimer species. Thus dimer bands, 1, 2 and 3 of insulin-treated animals were 5, 3 and 2-fold higher respectively than controls. The activity of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase decreased with fasting to 55% and 72% respectively of controls. The decrease in glucose 6-phosphate dehydrogenase activity reflected a lower activity of dimer bands 2 and 3 only, which were 62% and 39% of control activity respectively after three days fasting. A shift towards band 1 was observed under both conditions of starvation as well as under conditions of insulin treatment.
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PMID:Regulation of the multiple molecular forms of rat liver glucose 6-phosphate dehydrogenase by insulin and dietary restriction. 388 6

Glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and malic enzyme are enzymes involved in NADPH synthesis. Their specific activities and glucose utilization by isolated cell systems have been measured in adipose tissue and mammary gland from mid-lactating rats during starvation/refeeding transition. Starvation for 24 h produced a 75-90% decrease in the specific activities of these NADPH producing systems in mammary gland. Acinis isolated from the gland of starved rats had a lower production of CO2, fatty acids and triacylglycerols from (1-14C)glucose and (6-14C)-glucose than did gland from control rats. The activities of these enzymes in adipose tissue were very low and did not undergo any measurable alteration with starvation. The ability of adipocytes from well fed lactating rats to synthesize fatty acids from (1-14C)glucose was completely blocked. However, starvation is accompanied by a marked decrease in glucose incorporation into triacylglycerols. All the variations observed "in vivo" and "in vitro" in mammary gland returned almost to normal values by refeeding the starved lactating rats.
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PMID:Influence of starvation/refeeding transition on lipogenesis and NADPH producing systems in adipose tissue, mammary gland and liver at mid-lactation. 404 Jan 11


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