Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Activities of enzymes involved in fructose metabolism were measured in samples of human kidney cortex and medulla. The enzymes are ketohexokinase, aldolase, NAD- and NADP-dependent alcohol dehydrogenase, aldehyde dehydrogenase, triokinase and glycerate kinase; hexose biphosphatase and sorbitol dehydrogenase were also investigated. With the exception of glycerate kinase, all enzymes involved in fructose metabolism were found in the human cortex and medulla. The enzyme levels in the medulla were low in comparison with the cortex.
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PMID:Enzymes of fructose metabolism in human kidney. 16 31

In this research on metabolic effects of a high fructose diet, we studied the duration of these effects by measuring the specific activity of 8 enzymes stimulated by such a diet, on days, 0, 3, 6, 9, 15, after the return to a normal diet. In the intestinal mucosa, ketohexokinase, aldolase, triokinase, fructose-diphosphatase, and glucose-6-phosphatase specific activities were still entirely or partially stimulated on the 15th day after return to the standard diet. The stimulation of glucose-6-phosphatase and pyruvate kinase specific activities stopped quickly. In the liver, with the exception of fructose-diphosphatase, the return to basic values was much quicker than in intestine. In 7 enzymes out of 8 it was realized in 9 days or less. When a high fructose diet gives way to a normal one, return to basic values comes so much the quicker as activation has needed longer to appear.
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PMID:Dietary regulation of fructose metabolism in the intestine and in the liver of the rat. Duration of the effects of a high fructose diet after the return to the standard diet. 172 50

The effects of D-glyceraldehyde on the hepatocyte contents of various metabolites were examined and compared with the effects of fructose, glycerol and dihydroxyacetone, which all enter the glycolytic/gluconeogenic pathways at the triose phosphate level. D-Glyceraldehyde (10 MM) caused a substantial depletion of hepatocyte ATP, as did equimolar concentrations of fructose and glycerol. D-Glyceraldehyde and fructose each caused a 2-fold increase in fructose 1,6-bisphosphate and the accumulation of millimolar quantities of fructose 1-phosphate in the cells. D-Glyceraldehyde caused an increase in the glycerol 3-phosphate content and a decrease in the dihydroxyacetone phosphate content, whereas dihydroxyacetone increased the content of both metabolites. The increase in the [glycerol 3-phosphate]/[dihydroxyacetone phosphate] ratio caused by D-glyceraldehyde was not accompanied by a change in the cytoplasmic [NAD+]/[NADH] ratio, as indicated by the unchanged [lactate]/[pyruvate] ratio. The accumulation of fructose 1-phosphate from D-glyceraldehyde and dihydroxyacetone phosphate in the hepatocyte can account for the depletion of the intracellular content of the latter. Presumably ATP is depleted as the result of the accumulation of millimolar amounts of a phosphorylated intermediate, as is the case with fructose and glycerol. It is suggested that the accumulation of fructose 1-phosphate during hepatic fructose metabolism is the result of a temporary increase in the D-glyceraldehyde concentration because of the high rate of fructose phosphorylation compared with triokinase activity. The equilibrium constant of aldolase favours the formation and thus the accumulation of fructose 1-phosphate.
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PMID:Metabolic effects of D-glyceraldehyde in isolated hepatocytes. 382 66

The longitudinal localization of nine enzymes of the carbohydrate metabolism was studied in rats fed standard or high fructose diets, two months after a reciprocal jejuno-ileal transposition. In the ileal segment transposed to jejunal location, an adaptive increase of mucosal mass was observed, but the functional characteristics of enterocytes remained the same in the case of triokinase, aldolase, triose phosphate isomerase, glucose-6-phosphate isomerase and glucose-6-phosphatase activities. In the case of ketohexokinase and hexokinase activities, the functional properties of cells tended to resemble that of jejunum, as revealed by a significant increase in the specific enzyme activity. In the jejunum transposed to the place of the ileum, the fundamental properties of enterocytes and the functional capacity of the gut were maintained except in the case of fructose-1.6-bis phosphatase and of glucose-6-phosphatase. The high fructose diet did not facilitate the re-establishment of the gradient in its normal, aboral, direction. Indeed except for glucose-6-phosphatase, the enzymes of the jejunum transposed to the place of the ileum kept a high sensitivity and the enzymes of transposed ileum a low sensitivity to dietary fructose. Our conclusion is that the response to the diet depends more on the original position of the intestinal segment than on the local nutritional conditions and therefore that the basal activity of the majority of the intracellular enzymes implicated in carbohydrate metabolism and also their regulatory systems, are an intrinsic characteristic of the intestinal cells.
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PMID:[Intestinal adaptation and enzymatic changes following reciprocal jejunoileal transposition in rats. Effects of a high-fructose diet]. 397 35

The enzyme activities involved in fructose metabolism were measured in samples of human liver. On the basis of U/g of wet-weight the following results were found: ketohexokinase, 1.23; aldolase (substrate, fructose-1-phosphate), 2.08; aldolase (substrate, fructose-1,6-diphosphate), 3.46; triokinase, 2.07; aldehyde dehydrogenase (substrate, D-glyceraldehyde), 1.04; D-glycerate kinase, 0.13; alcohol dehydrogenase (nicotinamide adenine dinucleotide [NAD]) substrate, D-glyceraldehyde), 3.1; alcohol dehydrogenase (nicotinamide adenine dinucleotide phosphate [NADP]) (substrate, D-glyceraldehyde), 3.6; and glycerol kinase, 0.62. Sorbitol dehydrogenases (25.0 U/g), hexosediphosphatase (4.06 U/g), hexokinase (0.23 U/g), and glucokinase (0.08 U/g) were also measured. Comparing these results with those of the rat liver it becomes clear that the activities of alcohol dehydrogenases (NAD and NADP) in rat liver are higher than those in human liver, and that the values of ketohexokinase, sorbitol dehydrogenases, and hexosediphosphatase in human liver are lower than those values found in rat liver. Human liver contains only traces of glycerate kinase. The rate of fructose uptake from the blood, as described by other investigators, can be based on the activity of ketohexokinase reported in the present paper. In human liver, ketohexokinase is present in a four-fold activity of glucokinase and hexokinase. This result may explain the well-known fact that fructose is metabolized faster than glucose.
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PMID:Enzymes of fructose metabolism in human liver. 438 49

In patients with hereditary fructose intolerance, which is characterized by deficient aldolase activity toward fructose-1-phosphate, fructose induces a renal tubular dysfunction that implicates only the proximal convoluted tubule. Because normal metabolism of fructose by way of fructose-1-phosphate requires fructokinase, aldolase "B," and triokinase, the exclusively cortical location of these enzymes indicates that the medulla is not involved in the metabolic abnormality presumably causal of the renal dysfunction.
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PMID:Renal fructose-metabolizing enzymes: significance in hereditary fructose intolerance. 578 37

The adaptative response of a diet containing 60% fructose on the activity of those enzymes which are involved in the metabolism of fructose was measured in the liver and in the jejunal mucosa of rats over a period of 12 days. Control animals received isocaloric amounts of glucose or starch. Under fructose feeding there was a marked increase in the activity of fructose-1-phosphate aldolase (3-fold), ketohexokinase (2--3-fold), and triokinase (3-fold) in the jejunal mucosa. In the liver, however, a significant increase in enzyme activity could only be seen for triokinase (2--3-fold), whereas the activity of the other enzymes measured were only slightly or not at all altered. The activity of the three enzymes mentioned above were elevated to a maximum within 3 days after feeding the fructose diet. In the following time of observation no major further changes occurred. The results show that fructose feeding in comparison to a glucose or starch containing diet leads to a marked adaptative increase in the activity of those enzymes, which are involved in the breakdown of fructose, only in the jejunal mucosa.
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PMID:Adaptative changes of activity of enzymes involved in fructose metabolism in the liver and jejunal mucosa of rats following fructose feeding. 625 5

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

Male, Sprague-Dawley rats were weaned prematurely (postnatal day 17) to a starch-based diet. At the age of 182 days, half of the rats were fed for 14 days a diet in which sucrose supplied 40% of the energy. Early weaning led to increases in the activities of hepatic glucose-6-phosphate dehydrogenase (G6PD) and malic enzyme (ME). Compared with spontaneously weaned rats, prematurely weaned animals also showed increases in hepatic lipogenesis in vivo and in liver cholesterol levels. However, early weaning did not influence intraperitoneal glucose tolerance, plasma cholesterol concentrations or the activities of hepatic ketohexokinase (KHK), fructose-1-phosphate aldolase (FIPA) and triokinase (TK). Sucrose feeding led to deterioration of glucose tolerance and to enhanced hepatic lipogenesis in vivo. Sucrose-fed rats also showed increases in the total activities of hepatic G6PD, ME, KHK, FIPA and TK. There was a positive interaction in effects on liver size between early weaning and dietary sucrose. In general, however, there were no differences between prematurely and normally weaned rats in their responses to sucrose. The results did not support the idea that dietary adaptations in early life alter the manner in which adult rats respond to dietary stimuli.
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PMID:Effects of premature weaning on the metabolic response to dietary sucrose in adult rats. 707 28

Male, Sprague-Dawley rats were weaned prematurely (post-natal day 17) to a starch-based diet. Compared with normally-weaned rats, prematurely-weaned animals showed increases in the activities of hepatic glucose-6-phosphate dehydrogenase (G6PD) and malic enzyme (ME), and a fall in serum cholesterol level within 1 day. These enzymatic changes occurred sooner and were more pronounced when the diet of prematurely-weaned rats supplied 20% of the energy from sucrose, but the initial fall in serum cholesterol levels was smaller than in animals weaned prematurely to the control diet. Sucrose also led to an early rise in the activity of hepatic triokinase, but did not influence ketohexokinase or fructose-1-phosphate aldolase. Sucrose consumption resulted in an increase in lipogenesis in vivo in the liver and carcass and in serum cholesterol concentration on postnatal day 30, but animals weaned to the control diet were comparable with normally-weaned rats at the time. Early weaning led to elevation in the activities of hepatic G6PD and ME in 122-day-old rats, even though the control diet was fed from the age of 30 days. This response was not altered by the type of carbohydrate fed during the initial weaning period. Sucrose consumption during the weaning period did not exert long-term effects on the activities of hepatic fructolytic enzymes or in serum cholesterol levels.
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PMID:Immediate and late effects of premature weaning of rats to diets containing starch or low levels of sucrose. 728 3


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