Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.3.3.1 (citrate synthase)
 4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The biochemical, histochemical, and structural changes induced by endurance training and long-term exposure to high altitude were studied in the diaphragm muscle of rats exposed to simulated altitude (HA: n = 16; Pb = 62 kPa, 463 Torr; 4000 m) and compared to animals maintained at sea-level (SL: n = 16). Half of the animals in each group were trained (T) by swimming for 12 weeks, the other half were kept sedentary (S). Except for a small decrease in type I fibres in the HA-S group (-7%, P < 0.05), in favour of type IIab and type IIb fibres, neither high-altitude exposure nor endurance training had an overall affect on fibre type distribution. The mean fibre cross-sectional area was found to be unaffected by altitude and/or chronic exercise. Capillary density was shown to be increased by both high-altitude exposure (P < 0.02) and training (P < 0.001), whereas capillary growth, estimated by the capillary/fibre ratio, was unaffected in both cases. Following endurance training, a modest increase in citrate synthase was shown to occur to the same extent in the HA-T and SL-T groups (+15% and +16% respectively, NS). Hexokinase increased following training (P < 0.05) and high-altitude exposure (P < 0.001). In normoxic and hypoxic animals, endurance training enhanced the ratio of the heart-specific lactate dehydrogenase isozyme LDH1 to total LDH activity (+59%, P < 0.01; +92%, P < 0.05 respectively). It may be hypothesized that the increased glucose phosphorylation capacity observed in diaphragm muscle contributes to the reduction of glycogen utilization during exercise.
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PMID:Effects of endurance training at high altitude on diaphragm muscle properties. 148 82

1. Activities of a glycolytic enzyme--lactate dehydrogenase, LDH, and two oxidative enzymes--citrate synthase (CS), a marker for TCA cycle entry, and 3-hydroxyacyl-CoA dehydrogenase (HAD), which indicates the capacity for beta-oxidation of endogenous lipids, were measured in fast (tibialis anterior, TA, and extensor digitorum longus, EDL) and slow (soleus, SOL) muscles of Sprague-Dawley rats with intact and limited blood supply, and following treatment with the xanthine derivative torbafylline (Hoechst, Werk Albert, Wiesbaden). 2. Limitation of blood supply by unilateral ligation of the common iliac artery increased activity of LDH in fast muscles, and activity of CS and HAD in soleus. 3. Torbafylline treatment caused an increased LDH activity in intact fast muscles and decreased it in soleus, although the relative capacity for anaerobic and aerobic metabolism (indicated by the ratio of LDH and CS activities) remained unchanged in all cases. 4. Whilst having little effect on oxidative enzyme activity of fast muscles, torbafylline decreased the activity of CS but increased activity of HAD in soleus, suggesting a greater reliance on lipid metabolism. 5. The effect of arterial ligation on enzyme activity was ameliorated by treatment with torbafylline, possibly due to its effect on the microcirculation.
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PMID:The effect of torbafylline on enzyme activities in fast and slow muscles with limited blood supply. 167 66

1. Morphological, biochemical and metabolic characteristics of hindlimb muscles from summer-active (SA), winter-active (WA) and hibernating (H) golden-mantled ground squirrels (Spermophilus lateralis) were examined to identify alterations resulting from seasonal periods of inactivity. 2. Cross-sectional areas of fibers from the soleus were reduced in both WA and H, although only significantly (P less than 0.05) in WA. Fibers in the EDL exhibited significant reductions in cross-sectional areas in both H and WA groups. Muscle fiber and capillary densities were altered in quantitative agreement with changes in cross-sectional areas. 3. Protein content was reduced 20% (P less than 0.05) in EDL from H and WA groups, but reductions (10%) in the soleus were not statistically significant. RNA content in WA and H groups was significantly decreased in soleus (20%) and EDL (35%) compared with SA, but DNA content was unchanged. 4. In the plantaris, triglyceride content was unchanged, but citrate synthase activity in H (210 +/- 13 mumol min-1 g-1) was significantly greater than in SA (177 +/- 10). In contrast, LDH activity in H was reduced by 25% (P less than 0.05) compared with SA. 5. These results demonstrate atrophic effects associated with seasonal inactivity in hibernating ground squirrels, but suggest the existence of natural mechanisms which limit the response.
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PMID:Morphometric and metabolic indices of disuse in muscles of hibernating ground squirrels. 179 Jun 75

Metabolic differences of the cardiac muscle in children with normoxaemic and hypoxaemic congenital heart disease were analyzed by means of representative enzymes of the energy metabolism in 95 specimens in 80 children with congenital heart disease. Tissue specimens from the right atria and ventricles were obtained during surgical operations. It was revealed that the myocardial metabolism of patients with congenital heart disease was markedly influenced by hypoxaemia: the aerobic capacity was significantly reduced in the atria as well as in the ventricles. Changes in the atrial musculature were, however, more marked: in addition to citrate synthase - similarly as in the ventricles - in the atria also activities of enzymes associated with lactate metabolism (LDH) and with glycolysis (TPDH, GPDH) were reduced. Patients with an atrial septal defect had a significantly lower activity of the enzyme involved in the fatty acid breakdown (HOADH) than patients with a ventricular septal defect. The described new adaptive mechanism is of practical importance for the treatment of congenital heart disease and other conditions associated with prolonged hypoxaemia.
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PMID:[Adaptation of cardiac energy metabolism in children with congenital heart defects]. 280 25

This paper presents a study of the metabolic and contractile types of 34 samples from 30 muscles in five crossbred Pietrain-Large White pigs 6 to 7 months old. The activity of the following enzymes was measured: glyceraldehyde-3-phosphate dehydrogenase (GAPDH), lactate dehydrogenase using high (LDH-h) or low (LDH-b) pyruvate concentrations in the reaction medium, citrate synthase (CS), and myofibrillar Ca-Mg activated ATPase. Haeminic iron and ultimate pH (pHu) were measured on the same samples. The results showed a negative, rather linear relationship between GAPDH, LDH and ATPase activities on the one hand and CS and haeminic iron on the other. Rather high correlations (r = 0.7 to 0.8) were observed between metabolic and contractile criteria and pHu; the red (slow) muscles had the highest pHu.
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PMID:[Enzyme metabolic and contractile activities of 30 pig muscles. Relation with the final ph attained after death]. 293 86

The ultrastructure of skeletal muscle and activity of some enzymes of energy metabolism were studied to assess the effect of a deficiency of dietary energy and subsequent nutritional rehabilitation in 24 young, growing, healthy rhesus monkeys. Electron microscopy of muscles on energy-deficient animals showed thinning of myofibrils with widening of interfibrillar space and enlargement and accumulation of mitochondria at subsarcolemmal level. There was an apparent significant reduction in the fiber size. Muscle samples from each animal were analyzed for enzymes representative of glycolysis (phosphofructokinase [PFK] and lactate dehydrogenase [LDH], citric-acid cycle (isocitric dehydrogenase [ICDH] and citrate synthase [CS] and regeneration of ATP (creatine kinase [CK]. PFK and LDH activities were significantly augmented in energy-deficient animals. The increase in LDH activity resulted from a large increase in MU (skeletal muscle) LDH subunit. The activities of CS and ICDH were reduced. No alteration of CK in muscle and serum was observed. The morphological structure and enzyme activities returned to normal after nutritional rehabilitation.
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PMID:Ultrastructure and activity of some enzymes of energy metabolism of skeletal muscle in experimental energy deficiency. 310 25

To determine whether respiratory muscles undergo alterations in enzyme activities of energy metabolism as a result of increased mechanical activity, adult male Wistar rats were subjected to a prolonged endurance training program. Analysis off maximal enzyme activity patterns in the diaphragm following 15 weeks of extreme training (final running duration: 210 min per day, 27 m.min-1 at 15 degrees grade, indicated significant reductions in the marker enzymes of the citric acid cycle (citrate synthase), glycolysis (pyruvate kinase, PK; lactate dehydrogenase, LDH), ketone body utilization (3-keto acid: CoA transferase) and transamination (glutamate pyruvate transaminase, GPT). No changes were found for the enzymes of glycogenolysis (phosphorylase, PHOSPH), glycolysis (glyceraldehyde phosphate dehydrogenase, GAPDH), glucose phosphorylation (hexokinase, HK) and beta-oxidation (3-hydroxyacyl: CoA dehydrogenase, HAD) following training. In contrast, in the external intercostal muscle, increases in the range of 57-77% were noted for the enzymes CS and HAD, whereas in the internal intercostal muscles no training induced alteration was evident for these enzymes. For both the intercostal muscles, a consistent trend was noted towards a reduction in all of the glycolytic enzymes investigated, however, significantly lower values were recorded for only PK and LDH in the internal intercostals. GPT was increased in the internal intercostal muscles. These findings indicate that the response pattern observed in the enzyme activities studied following training are to some degree specific to the respiratory muscle investigated.
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PMID:Differential response of enzyme activities in rat diaphragm and intercostal muscles to exercise training. 337 43

Lactate dehydrogenase (LDH; EC 1.1.1.27), citrate synthase (CS; EC 4.1.3.7), and beta-hydroxyacyl-CoA-dehydrogenase (beta-OH-acyl-CoA-DH; EC 1.1.1.35) activities were determined in each of the three major cell types of rat uterus, i.e., epithelial, stromal, and smooth muscle, using quantitative microanalytical techniques. Adult ovariectomized rats were treated with 17-beta-estradiol to determine the time course and dose response (0.025-50 micrograms/300-g rat) effect of estrogen on enzyme activity of each type of uterine cell. The use of "oil well" and enzyme-cycling microtechniques to determine the time course and the dose responses of enzyme activity changes required microassays involving 1595 microdissected single cell specimens. Estradiol treatment increased epithelial LDH, CS and beta-OH-acyl-CoA-DH activity but had no effect on these enzymes in the stroma or in smooth muscle cells. The estradiol-stimulated peak enzyme activities on Day 4 in the intervention group are compared with those in the ovariectomized rat controls as follows: LDH, 44.5 +/- 3.5 vs 22.3 +/- 3.9; CS, 3.5 +/- 0.2 vs 1.5 +/- 0.6; beta-OH-acyl-CoA-H, 3.5 +/- 0.32 vs 2.2 +/- 0.2 (mean +/- standard deviation; mol/kg/hr). Stromal cell activities (LDH, 7.4 +/- 1.0; CS, 1.2 +/- 0.2; beta-OH-acyl-CoA-DH, 0.9 +/- 0.1) were significantly lower than epithelial cell levels and were similar to smooth muscle levels. Therefore, even in the ovariectomized animal epithelial cells have markedly higher metabolic activity compared with adjacent cells. The enzyme activities are expressed as moles of substrate reacting per kilogram of dry weight per hour. All three enzymes exhibited a 17-beta-estradiol-induced dose response between 0.025-0.15 micrograms/300-g rat. The three enzymes studied all had similar response patterns to estrogen. The effect of estradiol was restricted to epithelial cells, with enzyme activities increasing to maximal levels after approximately 96 hr of hormone treatment. This study therefore not only confirms the specific and differential metabolic responses of uterine cells to estradiol treatment, but clearly demonstrates that marked metabolic differences exist between epithelial cells and stromal or smooth muscle uterine cells.
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PMID:Rat uterine microbiochemistry: metabolic enzyme activities stimulated by 17-beta-estradiol are localized in epithelial cells. 357 58

We determined representative enzyme activities of glycogenolysis (glycogen phosphorylase) glycolysis (d-glyceraldehyde-3-phosphate dehydrogenase, GAPDH), beta oxidation of free fatty acids (1-3-hydroxyacyl CoA dehydrogenase, HADH), citric acid cycle (citrate synthase, CS), lactate fermentation (lactate dehydrogenase LDH), and creatine phosphate metabolism (creatine kinase, CK) in left ventricular samples of 36 patients to investigate if the metabolic capacities of the energy-supplying pathways are differently affected in different heart diseases. There were 17 patients with mitral valve diseases (MVD), 8 patients with aortic valve diseases (AVD), and 11 patients who suffered from dilative cardiomyopathies (DCM). The main metabolic characteristic on the level of enzymatic organization in patients with DCM was an increased ratio of GAPDH/HADH activities and a decreased ratio of HADH/CS activities compared to the valve-diseased patients. This result indicates that the capacity of glucose oxidation is enhanced at the expense of fatty acid metabolism in patients with DCM. Furthermore, we determined significantly lower myocardial CK activities in this group of patients, most probably reflecting a diminished content of myofibrils. Citrate synthase activity was lowest in patients with AVD. Although we cannot rule out that the impaired left ventricular function is in part responsible for the shift of the capacities of the energy-supplying metabolism in patients with DCM, we favor the assumption that it is a specific feature of this myocardial disease.
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PMID:Comparative analysis of myocardial enzyme activities of the energy-supplying metabolism in patients with dilative cardiomyopathies and valve diseases. 370 46

In three groups of healthy young subjects (n = 33; mean ages 6.4, 13.5, 17.1 years), muscle enzyme activities (creatine kinase, hexose phosphate isomerase, aldolase, pyruvate kinase, lactate dehydrogenase, citrate synthase, fumarase) of the vastus lateralis muscle were investigated to show age-dependent variations. A significant age-dependent increase in aldolase (P less than 0.05) and pyruvate kinase (P less than 0.01) activity and a decrease in fumarase activity (P less than 0.01) were computed. In relation to the age-dependent variation, maximum LDH activities could be measured at an age of 12-14 years; significantly decreased activities of the glycolytic enzymes could only be found in the youngest group.
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PMID:Skeletal muscle enzyme activities in healthy young subjects. 375 6


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