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:2.3.3.1 (citrate synthase)
4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The adaptation of enzyme activities, notably in the oxidative metabolism, and of prerequisites for tissue transport of oxygen in the claudication leg was evaluated by comparing muscle biopsies from the gastrocnemius muscle of the claudication and the symptom-free leg of seven patients with unilateral claudication. The claudication leg had higher activities of a marker enzyme for mitochondrial oxidative capacity, citrate synthase (CS), as well as of the MB and the mitochondrial isoenzyme of creatine kinase (CK), which are considered to be involved in the transfer of high energy phosphate from the mitochondria to the resynthesis of ATP in the cytoplasm. The difference between claudication and healthy leg in activities of these CK isoenzymes were well correlated with the corresponding side difference in CS activity. No significant differences between claudication and healthy leg were found in distribution of muscle fibre types or fibre dimension, capillary density or myoglobin content, nor was there any side difference in phosphofructokinase or lactate dehydrogenase. Side differences tended to be greater in those patients with the most advanced obstructive arterial disease as estimated from non-invasive pressure measurements. It is concluded that in reasonably physically-active patients, the mode of ischaemia to which the claudication leg is subjected leads to a metabolic adaptation characterized by increased activities of enzymes involved in the oxidative metabolism, but no significant adaptation of either the conditions for local oxygen transport, as estimated by myoglobin content, and capillary density, or capacity for anaerobic metabolism.
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PMID:Calf muscle adaptation in intermittent claudication. Side-differences in muscle metabolic characteristics in patients with unilateral arterial disease. 296 71

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 contribution of the liver to the increased metabolic efficiency of the obese rat (fa/fa) was examined. Oxygen consumption of isolated hepatocytes and isolated mitochondria, and hepatic activities of mitochondrial enzymes were measured. Hepatocyte oxygen consumption was similar in the obese and nonobese rats for all substrates tested. Mitochondrial respiration also was similar in both phenotypes for all substrates tested. Activities of citrate synthase, succinate dehydrogenase, and cytochrome oxidase were similar for obese and nonobese rats. Taken together, these data show that in vitro hepatic oxygen consumption and oxidative capacity are similar in obese and nonobese rats. Rates of mitochondrial respiration with palmitoylcarnitine further show that the capacity for hepatic lipid oxidation is similar in obese and nonobese rats. Therefore, the increased metabolic efficiency of the obese rat probably cannot be attributed to an intrinsic decreased hepatic oxidative capacity. Further, there is no defect in hepatic lipid oxidative capacity in the young obese rat.
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PMID:Oxygen consumption and oxidative capacity of hepatocytes from young male obese and nonobese Zucker rats. 302 May 65

1. The effects of artificial swim training on maximal oxygen consumption and heart rate, as well as on the capillarity and oxidative capacity of locomotory muscles, have been studied in the tufted duck, Aythya fuligula. 2. The artificial training programme resulted in a 27% increase in maximal oxygen consumption, mainly as a result of an increase in muscle capillarity (20% increase in capillary/fibre ratio). In addition, activity of an oxidative enzyme, citrate synthase, increased (by 42%) and there was a significant transformation of fibre types in the lateral gastrocnemius muscle. 3. Altering the duration and nature of the training stimulus, for example flying and diving, can bring about different degrees of muscular adaptation, particularly in oxidative capacity.
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PMID:Effect of training on maximal oxygen uptake and aerobic capacity of locomotory muscles in tufted ducks, Aythya fuligula. 2679 34

Coenzyme Q10 (CoQ10) was studied in papillary muscle from 18 patients (52-67 years, 2 females) subjected to open heart surgery due to mitral valve disease. In addition the enzyme activities of lactate dehydrogenase (LD) with its five isozymes, citrate synthase (CS) and mitochondrial CK (CK-MIT) were determined. Myocardial function was assessed by means of left ventricle (LV) angiography. CoQ10 averaged 0.39 (range 0.26-0.59) micrograms x mg-1 dw. On an individual basis CoQ10 was related to CS activity although not as closely as CK-MIT (r = 0.45, p less than 0.05 versus r = 0.86, p less than 0.001). The ratio (CoQ10) x (CS activity)-1 was calculated to represent mitochondrial quality. The level of LD3 fraction increase was used to mark for the degree of metabolic stress in the heart. LD3 fraction was negatively related to the quality index (r = -0.71, p less than 0.001). Thus, those with a low CoQ10 per unit of CS activity had also a high LD3 isozyme fraction. In a subset of 12 patients with isolated mitral regurgitation due to myxomatous valve degeneration, CoQ10 and the ratio CoQ10 over CS decreased with the degree of LV function impairment (r = -0.58, p less than 0.05 and r = -0.68, p less than 0.05, respectively). The quality index takes into account not only enzyme activity but also the potential for control of free oxygen radicals.
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PMID:Coenzyme Q10 and key enzyme activities in papillary muscle related to left ventricle function in mitral valve disease. 323 Dec 16

Maximal activities of rat skeletal muscle mitochondrial citrate synthase (CS), malate dehydrogenase (MDH), and alanine aminotransferase (ALT), as well as several other mitochondrial enzymes involved in various metabolic functions were significantly suppressed after a single bout of acute or exhaustive treadmill running. This enzymatic "down regulation" was maintained 24 and 48 h post exhaustion, especially in the untrained rats. Neither muscle cytosolic nor hepatic enzymes exhibited down regulation after exercise. Proteolysis was increased with exercise as assessed by the clearance of [3H]leucine previously incorporated into the proteins of the rats. Decreased CS, MDH, and ALT activities correlated with a significant loss of mitochondrial total protein sulfhydryl (r = 0.67, 0.68, 0.59, respectively, P less than 0.001) in untrained rats and both CS and MDH could be partially restored by incubation with dithiothreitol. Endurance-tested untrained and trained rats had significantly higher glutathione peroxidase (GPX) activity in both muscle mitochondria and cytosol which correlated significantly with endurance time (r = 0.70 and 0.74, respectively). It is concluded that enzymatic down regulation is not caused by proteolysis alone; i.e., peroxides and oxygen free radicals produced in prolonged exercise may alter the intramitochondrial redox state by oxidizing free thiols that may be required at active sites of these enzymes. Training may enhance the ability of the muscle to resist the toxic oxygen species by increasing GPX activity.
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PMID:Enzymatic down regulation with exercise in rat skeletal muscle. 336 59

Twelve, highly trained male swimmers were studied before, during, and after 10 successive days of increased training in an attempt to determine the physical effects of training over-load. Their average training distance was increased from 4,266 to 8,970 m.d-1, while swimming intensity was maintained at 94% (SE +/- 2%) of their maximal oxygen uptake, resulting in an average caloric cost during training of 2,293 kcal.d-1 (+/- 74). As a result of the intensified training regimen, the swimmers experienced local muscular fatigue and difficulty in completing the training sessions. Nevertheless, their swimming power, sprinting (s.22.86 m-1), endurance (s.365.8 m-1) performance, aerobic capacity, and muscle (m. deltoid) citrate synthase were unchanged as a consequence of the 10-d training regimen. Four of the 12 swimmers were, however, unable to tolerate the heavier training demands, and were forced to swim at significantly slower (P less than 0.05) speeds during the training sessions. These men were found to have significantly reduced muscle glycogen values, which was the result of their abnormally low carbohydrate intake. The findings of this research suggest that some swimmers may experience chronic muscular fatigue as a result of their failure to ingest sufficient carbohydrate to match the energy demands of heavy training.
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PMID:Effects of repeated days of intensified training on muscle glycogen and swimming performance. 338 3

With aging, several functions related to the locomotor system will deteriorate. Still, there is a rather well-maintained adaptability for increasing physical activity and for training in the elderly with respect to strength as well as endurance. Part of the observed reduction in muscle function with age could therefore be caused by inactivity. Evidently, however, there is a reduction in muscle mass with age due to loss of motor units. Muscle strength and aerobic power will fall fairly proportionally to the reduction in muscle mass. The muscle changes are, at least up to around the age of 70, more quantitative than qualitative. There is a reduction in the size of the fast-twitch (type II) fibers in the quadriceps, but not in other muscles such as the biceps brachii, presumably due to differences in activity pattern and motor unit recruitment. Aging per se may not reduce oxidative enzymatic capacity in the skeletal muscle. There is maintained potential for increase with endurance training. Thus, as an extreme example in very well trained elderly endurance athletes, high activity of citrate synthase is found and, in connection with that, also low plasma insulin values at baseline as well as after glucose intake. Limitations to aerobic capacity besides the reduced muscle mass are mainly located in the central circulatory and respiratory systems. Comparing the oxygen cost of activities in daily living, such as walking, and the aerobic power of the elderly, suggestions will be given on the choice of training activities.
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PMID:Physical activity and effects of muscle training in the elderly. 340 16

Oxygen consumption was measured before and during infusion of the catecholamine isoproterenol in age-matched spontaneously hypertensive (SHR) and Wistar-Kyoto (WKY) normotensive rats. Mass-independent rates of oxygen consumption of anesthetized 7-week-old rats were similar in the WKY and SHR rats (11.08 +/- 0.74 and 11.33 +/- 0.82 ml O2 min-1 kg-.67, respectively). Catecholamine infusion elicited increased total oxygen consumption in both WKY and SHR animals (15.0 +/- 1.0 and 14.9 +/- 1.2 ml O2 min-1 kg-.67, respectively), and the magnitude of these increases did not significantly differ. To assess whether there were changes in the metabolic state of brown adipose tissue, the major site of catecholamine-induced thermogenesis in rats, enzymes whose activity is proportional to aerobic capacity were assayed in vitro. In both the interscapular and cervical brown fat depots, maximal citrate synthase and maximal HOAD (beta-hydroxyacyl-CoA dehydrogenase) activities were similar in SHR and WKY rats. There were also no significant differences in brown fat protein content, suggesting no differential growth of this tissue in the two rat strains. Our results indicate that the nonshivering thermogenic capacity of the hypertensive SHR rats does not differ from that of the normotensive WKY animals.
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PMID:Nonshivering thermogenesis and brown fat in spontaneously hypertensive rats. 342 Jan 7

An isolated single rat hindlimb muscle preparation was used to examine the influence of exercise training on leucine metabolism during steady-state conditions at rest and during isometric contractions. Treadmill training increased the activity of citrate synthase in the hindlimb muscle by 40-45%. Leucine oxidation, measured as the rate of alpha-decarboxylation, was not different between trained (2.28 +/- 0.15 nmol.min-1.g-1, n = 9) and control (2.57 +/- 0.20, n = 9) muscle at rest. In addition, successive 40-min contraction periods at 15 and 45 tetani/min induced similar increases (50 and 100%, respectively) in leucine oxidation in both groups. However, trained muscle maintained a greater tension output (P less than 0.05) during contractions and exhibited a greater oxygen consumption (VO2) (P less than 0.05) during 45 tetani/min. Thus the rate of leucine oxidation, relative to VO2, was less (P less than 0.05) in the trained group. This response was probably related to differences in intracellular factors modulating branched-chain alpha-keto acid dehydrogenase, the rate-limiting step in leucine oxidation. Although our observed rates of muscle leucine alpha-decarboxylation can reasonably account for the rates of whole-body leucine alpha-decarboxylation of nontrained individuals found during steady-state tracer studies in vivo, this is less reasonably the case for the trained group. This suggests that a greater rate of leucine oxidation by nonmuscle tissues (e.g., liver) may occur in trained compared with nontrained individuals.
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PMID:Effect of endurance training on leucine metabolism in perfused rat skeletal muscle. 342 11


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