Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.1.1.37 (malate dehydrogenase)
4,591 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Regional glucose uptake in perfused hearts, and the activities of several glycolytic enzymes contributing to the glucose metabolism in perfused and nonperfused hearts were studied in male and female rats after 8-9 weeks of swimming training. The left ventricular glucose uptake showed a transmural gradient in the sedentary animals, the subendocardial uptake being 30% and 12% higher than that of the subepicardial layer in the males and females, respectively. Swimming exercise abolished the left ventricular glucose uptake gradient in male rats, and in female rats an opposite gradient was found, the subepicardial uptake being 23% higher than the subendocardial uptake. The activities of phosphofructokinase and 3-phosphoglyceraldehyde dehydrogenase also showed transmural gradients in the left ventricles. Training did not abolish these gradients. Training-induced changes in the activities of phosphofructokinase, 3-phosphoglyceraldehyde dehydrogenase, pyruvate kinase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, citrate synthase, and malate dehydrogenase were found in certain sites of the myocardium. Perfusion of isolated hearts for 50 min with insulin-containing Krebs-Ringer buffer especially affected the activities of phosphofructokinase, lactate dehydrogenase, and citrate synthase, increasing these activities in the left ventricles and decreasing them in the atria. These results indicate that there are regional differences between male and female rats in the cardiac glucose uptake rate after swimming training.
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PMID:Effect of chronic exercise on glucose uptake and activities of glycolytic enzymes measured regionally in rat heart. 273 May 24

The maximum rate (Vmax) of some mitochondrial enzymatic activities related to energy transduction (citrate synthase, malate dehydrogenase, NADH-cytochrome c reductase (as total activity), cytochrome oxidase) and amino acid metabolism (glutamate dehydrogenase) were evaluated in non-synaptic (free) and synaptic mitochondria from rat brain hippocampus. Three types of mitochondria were isolated from rats subjected to single i.p. treatments with piracetam (300 mg.kg-1) or with clonidine (750 micrograms.kg-1). With respect to the enzymatic pattern of three types of non-synaptic and synaptic mitochondria, in hippocampus a different maximum rate of both NADH-cytochrome c reductase and cytochrome oxidase was observed, these activities in particular being lowest in the "synaptic heavy" mitochondrial subfraction than in the "synaptic light" one; in addition, other enzyme activities are different in the "free" as compared to both the "light" and "heavy" mitochondria. This confirms that in various types of brain mitochondria a different metabolic machinery exists. Acute treatment with piracetam decreased citrate synthase, glutamate dehydrogenase, NADH-cytochrome c reductase and cytochrome oxidase activities only in the "heavy" mitochondria obtained from synaptosomes. Acute treatment with clonidine decreased the citrate synthase, NADH-cytochrome c reductase and cytochrome oxidase activities only in the same type of mitochondria, i.e. synaptic "heavy" mitochondria. However, this drug increased the same enzymatic activities in "free" mitochondria, some of them being increased or decreased in "light" intrasynaptic ones. Therefore in vivo administration of piracetam mainly affects some specific enzyme activities (suggesting a specific molecular trigger mode of action) of the intrasynaptic mitochondria (suggesting a specific subcellular trigger site of action), the effect on enzyme activities by clonidine being more complex.
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PMID:Action of piracetam and clonidine on different mitochondrial populations from hippocampus. 277 15

Tissue specimens from the right atrium and ventricle of the same heart were obtained during surgery in 45 children operated on account of congenital heart disease (tetralogy of Fallot and ventricular septal defect). Significant differences were found in the enzyme activities between the atrial and ventricular musculature. The activities of enzymes associated with aerobic metabolism (citrate synthase, malate dehydrogenase, with lactate metabolism) lactate dehydrogenase (and the fatty acid oxidation) hydroxyacyl-SoA-dehydrogenase) were significantly higher in the ventricular musculature. Hexokinase, the enzyme responsible for glucose phosphorylation was on the other hand, significantly higher in the atria. From this ensues that the right ventricle can utilize and oxidize to a full extent all main nutrients (fatty acids, glucose and lactate), while the right atrium utilizes above all glucose. These atrio-ventricular differences do not depend on the type of the congenital heart disease and it may be assumed that they exist also in healthy subjects.
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PMID:[Differences in the activity of enzymes associated with energy metabolism in the heart atria and ventricles in children]. 280 28

The activity of 7 mitochondrial enzymes, fumarase, NAD-malate dehydrogenase (MDH), citrate synthase (CS), valine dehydrogenase (VDH), succinate dehydrogenase (SDH), glutamate dehydrogenase (GDH), pyruvate dehydrogenase complex (PDHC) has been measured in platelet preparations from patients affected by Friedreich's ataxia (FA), dominant and non-dominant olivopontocerebellar atrophy (DOPCA, NDOPCA) and normal individuals. Significant decreases of GDH (P less than 0.01), PDHC (P less than 0.01), VDH (P less than 0.05) and SDH (P less than 0.05) activities were observed in FA patients. Significant decreases of GDH (P less than 0.01), PDHC (P less than 0.01), VDH (P less than 0.05), SDH (P less than 0.05) and CS (P less than 0.05) activities were Observed in ND-OPCA patients, whereas in DOPCA patients only GDH activity was significantly (P less than 0.05) decreased. In 8 of 10 patients with FA and in all patients with NDOPCA the activity of one or more of 4 enzymes, i.e. GDH, VDH, SDH, PDHC, was lower than the lowest of control values. Four of 6 patients with DOPCA had GDH activity lower than the lowest of control values. These results indicate that abnormalities of mitochondrial metabolism is a constant element in hereditary ataxia and suggest that the alteration primary leading to the different types of ataxias should be related to mitochondrial oxidative metabolism, at least at a regulatory level.
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PMID:Abnormalities of mitochondrial enzymes in hereditary ataxias. 281 70

A method for a 50-60-fold purification of a cysteine proteinase from trophozoites of Entamoeba histolytica using 35-80% ammonium sulphate fractionation, gel chromatography on Sephadex G-75, and preparative isoelectric focusing is described. The enzyme was examined for its proteolytic potencies towards native enzyme substrates. The amebic proteinase directly inactivates aldolase and glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle as well as glucose-6-phosphate dehydrogenase from yeast. The inactivation of citrate synthase from porcine heart proceeds rather slowly, whereas malate dehydrogenase from porcine heart is not affected by the amebic proteinase under the condition used. With the exception of aldolase all inactivated enzyme substrates have been cleaved by limited proteolyses yielding major cleavage products. The inactivation of aldolase probably functions by the release of a small segment from a terminus being essential for aldolase activity.
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PMID:Cysteine proteinase of Entamoeba histolytica. I. Partial purification and action on different enzymes. 287 Apr 30

Nonselective and beta 1-selective adrenergic antagonists were tested for their effects on enzymatic adaptation to exercise training in rats as follows: trained + placebo (TC); trained + propranolol (TP); trained + atenolol (TA); and corresponding sedentary groups, SC and SP. Trained rats ran 1 h/d at 26.8 m/min, 15% grade, 5 d/wk, 10 wk. Both beta-antagonists were given at doses that decreased exercise heart rates by 25%. Training increased skeletal muscle citrate synthase, cytochrome c oxidase (Cyt-Ox), carnitine palmitoyltransferase (CPT), beta-hydroxyacyl coenzyme A dehydrogenase, mitochondrial malate dehydrogenase (MDH), and alanine aminotransferase (ALT) activities significantly in the TC group, but not in TP. These enzyme activities, except Cyt-Ox and CPT, were also significantly increased in TA. Hepatic phosphoenolpyruvate carboxykinase activity did not alter with training or beta-blockade. Fructose 1,6-bisphosphatase activity was lower in TC than in SC, but unchanged in TP or TA. Hepatic mitochondrial MDH and ALT activities increased with training only in TC. It is concluded that beta 2-adrenergic mechanisms play an essential role in the training-induced enzymatic adaptation in skeletal muscle.
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PMID:Enzymatic adaptation to physical training under beta-blockade in the rat. Evidence of a beta 2-adrenergic mechanism in skeletal muscle. 287 82

Binding experiments indicate that mitochondrial aspartate aminotransferase can associate with the alpha-ketoglutarate dehydrogenase complex and that mitochondrial malate dehydrogenase can associate with this binary complex to form a ternary complex. Formation of this ternary complex enables low levels of the alpha-ketoglutarate dehydrogenase complex, in the presence of the aminotransferase, to reverse inhibition of malate oxidation by glutamate. Thus, glutamate can react with the aminotransferase in this complex without glutamate inhibiting production of oxalacetate by the malate dehydrogenase in the complex. The conversion of glutamate to alpha-ketoglutarate could also be facilitated because in the trienzyme complex, oxalacetate might be directly transferred from malate dehydrogenase to the aminotransferase. In addition, association of malate dehydrogenase with these other two enzymes enhances malate dehydrogenase activity due to a marked decrease in the Km of malate. The potential ability of the aminotransferase to transfer directly alpha-ketoglutarate to the alpha-ketoglutarate dehydrogenase complex in this multienzyme system plus the ability of succinyl-CoA, a product of this transfer, to inhibit citrate synthase could play a role in preventing alpha-ketoglutarate and citrate from accumulating in high levels. This would maintain the catalytic activity of the multienzyme system because alpha-ketoglutarate and citrate allosterically inhibit malate dehydrogenase and dissociate this enzyme from the multienzyme system. In addition, citrate also competitively inhibits fumarase. Consequently, when the levels of alpha-ketoglutarate and citrate are high and the multienzyme system is not required to convert glutamate to alpha-ketoglutarate, it is inactive. However, control by citrate would be expected to be absent in rapidly dividing tumors which characteristically have low mitochondrial levels of citrate.
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PMID:Regulation of malate dehydrogenase activity by glutamate, citrate, alpha-ketoglutarate, and multienzyme interaction. 289 80

Single fibers of rabbit fast-twitch tibialis anterior (TA) muscles were analyzed after continuous low-frequency stimulation for up to 8 wk. After 2-5 wk, every fiber showed higher levels of citrate synthase, hexokinase, and 3-oxoacid CoA-transferase than any control fiber; in some cases these levels were 2-10 times higher (well above any found even in the control soleus, a slow-twitch muscle). Average levels of malate dehydrogenase and alanine transaminase also rose dramatically, but peak single fiber levels were not much above the highest in controls. These differential effects confirm at the single fiber level that chronic stimulation can alter mitochondrial composition. Lactate dehydrogenase, fructose-bisphosphatase, and adenylate kinase declined to levels far below those of any control TA fiber, and, in the case of fructose-bisphosphatase, to within the activity range of control soleus fibers. According to their staining reaction for myofibrillar ATPase, TA fibers were initially 23% type IIA, and 74% type IIB, but by 5 wk these had been converted to a mixture of type I, IIA, and IIC fibers. At 5 wk, levels of lactate dehydrogenase, adenylate kinase, and malate dehydrogenase were characteristic of their (new) ATPase type, but 3-oxoacid CoA transferase had increased to levels 6-15 times higher than in control fibers of the same type.
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PMID:Chronic stimulation of mammalian muscle: enzyme changes in individual fibers. 302 Sep 91

The sensory projections from the whiskers of mice and other rodents synapse somatotopically in 3 subnuclei in the brainstem trigeminal complex, in the ventrobasal complex of the thalamus and in the somatosensory cortex. Deafferentation of the whiskers in adult animals results in qualitative and quantitative changes in activities of the metabolic enzymes in the somatosensory cortex (e.g. J. Neuro-sci., 1 (1981) 929-935). We determined the time course and extent of changes in the subcortical trigeminal centers of adult mice after deafferentation. The right infraorbital nerve was sectioned in mice under surgical anesthesia; the animals survived for periods up to 26 weeks. The optic nerve was also cut to evaluate the effects of central tract section. Some brains were prepared histochemically for the mitochondrial enzymes cytochrome oxidase (CO) and succinic dehydrogenase (SDH), and some were prepared for microchemical analysis of the enzymes citrate synthase (CS), malate dehydrogenase (MDH) and phosphorylase. All deafferented and intact nuclei were examined in each animal quantitatively. The oxidative enzymes (CO, SDH, CS and MDH) that were analyzed by histochemical and microchemical approaches showed a decrease in activities as early as 3 weeks postdeafferentation, a trend that continued up to 12 weeks in all the subcortical trigeminal stations and lateral geniculate nucleus (LGN) when compared with the intact side. By 25 weeks postlesion, the levels were comparable to the intact side except that in the LGN, the levels remained depressed. The phosphorylase levels increased at around 3 weeks postoperation and remained elevated 25 weeks postlesion. Each case provided results on the effects of deafferentation at a given time point throughout the trigeminal pathway. Direct quantitative correlation of histochemical and microchemical approaches for glycolytic enzymes is consistent with a coordinate regulation of these molecules. The changes in enzyme levels in all nuclei occur simultaneously and to a similar degree. This strongly suggests that neuronal activity plays an important role in regulating metabolic machinery throughout this pathway in adults.
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PMID:Quantitative histochemical and microchemical changes in the adult mouse central nervous system after section of the infraorbital and optic nerves. 303 55

In the present study the effects of chronic administration of dextroamphetamine on energy metabolism in the brain of the rat were examined. The enzymes studied were: hexokinase (soluble and particulate forms), phosphofructokinase, pyruvate kinase, lactate dehydrogenase, citrate synthase, NAD+ and NADP+-dependent isocitrate dehydrogenases, succinate dehydrogenase and malate dehydrogenase. All the activities of the enzymes were assayed in four regions of the brain of the rat (cerebellum, medulla oblongata and pons, cererbral cortex and diencephalon). Rats were injected intaperitoneally once daily with dextroamphetamine for 20 consecutive days. The initial dose was 5 mg/kg/day and the dose was then increased by 1 mg/kg/every 5 days up to a total of 8 mg/kg/day on days 16-20. In the glycolytic enzymes a reduction of the activity of phosphofructokinase was found in the diencephalon and an increase of the activity of pyruvate kinase and lactate dehydrogenase in the diencephalon and medulla oblongata and pons, respectively. Citrate synthase was the only enzyme in the Krebs' cycle affected by chronic administration of dextroamphetamine. The results presented here show that chronic administration of dextroamphetamine produced important changes in some enzymes of glycolysis and the Krebs' cycle in the brain of the rat.
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PMID:Effects of chronic administration of dextroamphetamine on enzymes of energy metabolism in regions of the rat brain. 303 25


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