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)

Biopsies from m. quadriceps femoris from the operated leg of nine patients were taken before, and 6 weeks after, knee surgery. During the whole postoperative period the operated leg was immobilized with the knee in 40-50 degrees of flexion. Myoglobin (MYO) and the enzymes citrate synthase (CS), creatine kinase (CK) and its isozymes MB (CK-MB) and mitochondrial CK (CK-MIT), aspartate aminotransferase (ASAT), phosphofructokinase (PFK) and lactate dehydrogenase (LD) were determined on the biopsies. Citrate synthase, ASAT, CK, CK-MB, CK-MIT and LD activities were decreased (12-30%) after the postoperative leg immobilization period. Phosphofructokinase did not change, while MYO content was increased (16%). In conclusion, a different control of the synthesis of oxidative enzymes and MYO is suggested, as the induced changes following immobilization were in opposite directions. The function of the increased MYO content may be to facilitate the oxygen extraction.
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PMID:Increase in myoglobin content and decrease in oxidative enzyme activities by leg muscle immobilization in man. 297 30

The effect of physical training on the in vitro activities of key enzymes that provide quantitative information on the maximum capacities of anaerobic and aerobic metabolism has been investigated in the gluteal muscle of the horse. Training had no effect on the activities of 6-phosphofructokinase or creatine kinase, suggesting that there was no effect on the capacity of anaerobic metabolism in this muscle. However, the activities of hexokinase and citrate synthase were increased, indicating that training increased the capacity of aerobic metabolism. For comparative purposes, muscle fibre composition and enzyme activities were also determined in a group of foals and a group of broodmares.
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PMID:Activities of key enzymes of aerobic and anaerobic metabolism in middle gluteal muscle from trained and untrained horses. 299 78

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

The glycolytic and aerobic oxidative capacity in skeletal muscle was investigated to reveal if the decrease seen in muscle protein synthesis is accompanied by a fall in the enzymatic capacity to oxidize substrates. Six patients undergoing elective abdominal surgery were investigated by percutaneous muscle biopsies taken before surgery and on the first and third postoperative days. Protein synthesis as assessed by the polyribosome concentration was 40% lower on the third day postoperatively than before surgery (p less than 0.01). The glycolytic and oxidative capacity was evaluated by determining the activity of eight key enzymes in the intracellular oxidative metabolism, namely total creatine kinase (CK), the isozymes CK-MB and mitochondrial CK, lactate dehydrogenase, citrate synthase, aspartate aminotransferase, and phosphofructokinase, and also the concentration of myoglobin. None of these parameters were affected in the immediate postoperative period independently of the provision of nutritional support. It was concluded that the decrease in protein synthesis is not accompanied by a concomitant decline in the enzymatic oxidative capacity in skeletal muscle in the period immediately following elective surgery.
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PMID:Enzymatic capacity and protein synthesis in human muscle postoperatively. 314 5

Tibialis anterior (TA) muscle of mouse, rat, guinea pig, and rabbit was indirectly stimulated for 10 h/day at 10 Hz up to 28 days. Changes in the activity levels of hexokinase (HK), phosphofructokinase (PFK), glyceraldehydephosphate dehydrogenase (GAPDH), lactate dehydrogenase (LDH), creatine kinase (CK), citrate synthase (CS), malate dehydrogenase (MDH), 3-hydroxyacyl-CoA dehydrogenase (HADH), and beta-hydroxybutyrate dehydrogenase (HBDH) were compared. Although the direction of changes in the enzyme activity pattern was in accordance with previous findings on rabbit TA, the magnitude of the responses varied markedly between the mammals under study. Mouse TA was almost unaffected. A major effect of chronic stimulation in rat, guinea pig and rabbit was an increase in enzyme activities of aerobic-oxidative metabolism. According to intrinsic differences of the muscles under study, the increases varied among the species and appeared to be inversely related to the basal levels of these enzymes in the unstimulated muscles. Conversely, glycolytic enzyme activities (PFK, GAPDH, LDH) markedly decreased in rat, guinea pig, and rabbit, and were only slightly reduced in mouse. Changes in HK and HBDH activities displayed the largest variations in the induced change between species. These results indicate species-specific patterns of metabolic adaptation to increased contractile activity.
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PMID:Species-specific effects of chronic nerve stimulation upon tibialis anterior muscle in mouse, rat, guinea pig, and rabbit. 317 88

Iguanid lizards exhibit considerable intraspecific variation in several aspects of their muscle composition. To determine the relationship of this variation to the variation in locomotor performance, running speeds of 20 male desert iguanas (Dipsosaurus dorsalis) of similar mass were measured from video recordings of animals as they sprinted down a 4.9-m runway maintained at 40 degrees C, the preferred body temperature of Dipsosaurus. Mean sprint speed ranged from 2.2 to 4.2 m/s. Selected muscles from these animals were then analyzed histochemically for fiber type size and composition, and the activities of citrate synthase, pyruvate kinase, and creatine kinase were measured. Muscle fiber cross-sectional areas were highly correlated within individuals, in three leg muscles and across all three fiber types, so that individuals could be characterized as possessing large or small fibers relative to the sample mean. Activities of all three enzymes also covaried within individuals so that individual lizards could be characterized as possessing high or low leg muscle catabolic capacity. There existed a significant and inverse relationship between fiber cross-sectional areas and muscle enzyme activities so that individuals with small muscle fibers tended to have higher catabolic capacities. Approximately 25-30% of the variation in mean sprint running speed could be predicted by variation in muscle fiber areas alone. The use of muscle fiber areas and snout vent length as independent variables in a multiple-regression equation explained approximately 50% of the sprint-running variation.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Muscle composition and its relation to sprint running in the lizard Dipsosaurus dorsalis. 341 42

1. Palmitate oxidation rates and activities of creatine kinase, cytochrome c oxidase and citrate synthase were determined in homogenates of three different human muscles and their derived muscle cell cultures. Palmitate oxidation was also assayed in intact cultured cells (myotubes). 2. Biopsies obtained from m. rectus abdominis exhibited a lower palmitate oxidation rate and lower activities of citrate synthase and cytochrome c oxidase than those from m. gluteus and m. quadriceps. In contrast, cell cultures obtained from the three muscles were mutually comparable with regard to these mitochondrial activities. 3. Although cell cultures only reached a low differentiation grade (judged by the total creatine kinase activity and percentage isoenzyme-MM) they are well comparable with the original biopsies with respect to citrate synthase activity and capacity of palmitate oxidation. The activity of cytochrome c oxidase was clearly lower in the cultured cells. 4. Palmitate was more completely oxidized in intact myotubes than in homogenates of myotubes. Apparent Km and Vmax values of palmitate oxidation did not differ significantly in homogenates and intact preparations of myotubes.
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PMID:Palmitate oxidation and some enzymes of energy metabolism in human muscles and cultured muscle cells. 342 77

Individual muscle fibers from patients with Duchenne muscular dystrophy at an early stage in their disease, and from apparently normal boys of similar age, were analyzed for 13 enzymes of energy metabolism. This approach avoided the serious problems with muscle homogenate assays from increases in nonparenchymal components and permitted assessment of disease changes in different fiber types. Some enzymes of glycogenolysis (phosphorylase, phosphoglucomutase, and pyruvate kinase) were decreased in dystrophic fibers of all types. Phosphofructokinase was decreased in presumptive type II fibers. Lactate dehydrogenase was increased in type I fibers and essentially unchanged in type II. Phosphoglucoisomerase was near normal. Two enzymes of glucose metabolism not involved in glycogenolysis, hexokinase and glycogen synthase, were near normal, but a third, fructose bisphosphatase, was sharply reduced. Two enzymes of oxidative metabolism, citrate synthase, and beta-hydroxyacyl CoA dehydrogenase, were unchanged or increased. Two enzymes of high energy phosphate transfer, creatine kinase and adenylokinase, were only marginally affected. The net result is to leave the type II fibers, which normally exert the greatest force, with a severe deficit in the glycogenolytic enzyme machinery to maintain that force.
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PMID:Effect of Duchenne muscular dystrophy on enzymes of energy metabolism in individual muscle fibers. 360 Feb 88

To determine the adaption of myocardial metabolism in mitral regurgitation and mitral stenosis, human papillary muscles obtained during open heart surgery were analysed to measure selective enzyme activities in energy metabolism. All enzyme activities were expressed per unit dry weight muscle, per unit alkali soluble protein, and per unit total creatine and the different results compared. The activities of enzymes concerned with mitochondrial energy production and energy transfer (namely, citrate synthase and mitochondrial creatine kinase) tended to be higher in papillary muscles from hearts with mitral regurgitation than in those with mitral stenosis. The activities of enzymes concerned with cytoplasmic energy production (creatine kinase MM, lactate dehydrogenase, and phosphofructokinase) did not show statistically significant differences between mitral regurgitation and mitral stenosis. The ratio of creatine kinase MB activity to total creatine content showed the greatest difference when papillary muscles from patients with mitral regurgitation and mitral stenosis were compared (31% higher in mitral regurgitation; p less than 0.001). The specific function of creatine kinase MB, which is located in cytoplasm, is not well defined. Creatine kinase MB activity increases with extreme endurance training of human skeletal muscle. Thus the higher creatine kinase MB activity in papillary muscle of mitral regurgitation may represent an adaptation to increased physical demand.
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PMID:Myocardial enzyme activities in patients with mitral regurgitation or mitral stenosis. 365 86

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


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