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 hindlimbs of rats were immobilized, in plaster casts, for varying durations, and the time course for atrophy of muscle and of selected proteins in these muscles was determined. In those muscles whose lengths were at less than resting length during the fixation procedures, exponential decay to a new apparent steady state after atrophy was shown by wet and dry muscle weights and by the amounts of biuret protein, cytochrome c, and citrate synthase. The time taken to decrease to one-half of the final decrease at the new apparent steady state level was about 4-6 days for the above parameters which decayed exponentially. In contrast, the myoglobin concentration increased during atrophy and the amount of myoglobin remain unchanged during atrophy. When fixation procedures on limbs were such that muscles were stretched to lengths greater than resting length, then the onset of atrophy was delayed; indeed, in some cases muscles hypertrophied when fixed in the stretched position.
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PMID:Time course of muscular atrophy during immobilization of hindlimbs in rats. 19 96

To assess the effects of fasting on recovery of function and exogenous glucose metabolism after 15 minutes of total ischemia, we perfused isolated working rat hearts from fed and fasted animals. Hearts were perfused in a recirculating system with bicarbonate buffer containing glucose (10 mM). Mechanical performance, release of marker proteins for ischemic membrane damage (lactate dehydrogenase, myoglobin, citrate synthase), and the concentrations of lactate and glucose in the perfusion medium were measured serially. Tissue metabolites were also measured. Fasting raised the myocardial glycogen content by 25%. Cardiac performance of perfused hearts from fed and fasted animals was the same during the preischemic and the post-ischemic period. The time of return of function to preischemic values was significantly less in hearts from fasted rats (2.3 versus 7.8 minutes, p less than 0.025). The release of cytosolic and mitochondrial marker proteins was significantly lower in hearts from fasted rats than in hearts from fed rats. Glucose metabolic rates during control and reperfusion were unchanged for hearts from fasted rats, but decreased for hearts from fed rats during reperfusion. The adenine nucleotide content at the end of ischemia was higher in hearts from fasted animals than in hearts from fed animals. We conclude that increasing glycogen levels prior to ischemia improves recovery of function, lessens membrane damage, and prevents loss of adenine nucleotides.
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PMID:Fasting in vivo delays myocardial cell damage after brief periods of ischemia in the isolated working rat heart. 200 7

Bilateral biopsies from the erector spinae muscles were taken during surgery from 10 females and two males (mean age 14, range 13-17 years) with thoracal scoliosis for 6 years (range 2-11 years). The biopsies were analysed for myoglobin (MYO), citrate synthase (CS) and creatine kinase MB (CK-MB). The severity of scioliosis was estimated by Cobb's angle, the greater the angle the more severe the disease. The convex/concave side ratio (CVX/CCV) was for CS 1.3 +/- 0.4 (P less than 0.01), CK 0.9 +/- 0.1 (P less than 0.05), CK-MB 1.6 +/- 0.4 (P less than 0.01) and for MYO 1.1 +/- 0.2 (P greater than 0.05). No significant correlations were found between the CVX/CCV for CS, CK or CK-MB on the one hand and the Cobb's angle on the other. The CVX/CCV for MYO was, however, directly related to the angle (r = 0.80, P less than 0.01). For the lower range of angles (less than or equal to 59 degrees) the CVX/CCV for MYO was below unity (0.88, P greater than 0.05) and for the larger angles (greater than 59 degrees) above unity (1.23, P less than 0.05). In conclusion, a dissociation in the adaptive response of m. erector spinae in scoliosis between mitochondrial enzyme and myoglobin content was demonstrated.
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PMID:Myoglobin and enzyme adaptations in erector spinae muscles in thoracal scoliosis. 208 81

To compare two situations with similar magnitudes of mitochondrial substrate flux but different blood oxygen contents, one-legged training was employed. Ten healthy subjects trained one leg under normobaric conditions and the other under hypobaric conditions. At each session the subjects trained each leg for 30 min. The absolute work intensity was the same for both legs and was chosen to correspond to 65% of the average (right and left) pretraining one-legged maximal work capacity. There were three to four training sessions per week for 4 wk. Muscle biopsies from each leg were taken before and after training and analyzed for fiber types, capillaries, myoglobin, and oxidative and glycolytic enzymes. The most striking finding was a greater increase of citrate synthase activity under hypobaric conditions than under normobaric conditions. In addition, the myoglobin content increased in the leg trained under hypobaric conditions, whereas it tended to decrease in the normobarically trained leg. Because both legs were trained at the same intensity, the oxygen turnover and the substrate flux through the carboxylic acid cycle and the respiratory chain must have been of similar magnitude. Thus a difference in substrate flux is less likely to have caused the differences in enzyme activities and myoglobin content between training under normobaric and hypobaric conditions. Instead, the stimulus seems to be related to the blood oxygen content or tension.
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PMID:Is hypoxia a stimulus for synthesis of oxidative enzymes and myoglobin? 238 18

Quadriceps muscle biopsies from five patients with primary polycythaemia and four patients with non-primary polycythaemia, all with normal respiratory functions, were studied before and after normalization of haemoglobin and erythrocyte volume fraction by haemodilution or venaesectio. Since similar results were obtained from both groups of patients data were pooled. After normalization of the erythrocyte volume fraction myoglobin decreased by 19 +/- 16%, P less than 0.01, the activity of creatine kinase and citrate synthase by 12 +/- 8 and 14 +/- 18%, P less than 0.05, respectively. The decrease in myoglobin content was related to the decrease in haemoglobin concentration (r = 0.77, P less than 0.01). In conclusion, these data suggest that in non-hypoxaemic polycythaemia skeletal muscle shows adaptations indicative of an impaired oxygenation and a metabolic stress, adaptations that are reversed by haemodilution.
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PMID:Decrease in myoglobin and enzyme contents with haemodilution in non-hypoxaemic polycythaemic patients. 239 84

Metabolic adaptations were studied in papillary muscle from 18 patients undergoing open-heart surgery for mitral valve disease. Analyses were made of myoglobin (MG), the enzymes lactate dehydrogenase (LD) with its isoenzymes, glyceraldehyde phosphate dehydrogenase (GAPDH), phosphofructokinase (PFK), citrate synthase (CS) and creatine kinase (CK) with its isoenzymes MB (CK-MB) and mitochondrial CK (CK-MIT). Myocardial function was assessed with left ventricular angiography. Positive and significant correlations were found between enzymes of oxidative metabolism, i.e. CS on the one hand and MG (r = 0.76), LD1 (r = 0.68), CK-MIT (r = 0.86) and CK-MB (r = 0.65) on the other. Indicators of glycolysis--PFK, GAPDH and LD3--varied independently of CS. LD3% was directly related to GAPDH (r = 0.66). In a sub-group of 12 patients with isolated mitral regurgitation due to myxomatous valve degeneration, LD3% rose (r = 0.72) with increasing myocardial derangement which, however, showed no relationship with any other marker. Thus the capacities of oxidative and glycolytic pathways did not co-vary. Volume load appeared not to affect oxidative capacity, while the anaerobic fraction of glycolysis was increased.
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PMID:Key enzymes of myocardial energy metabolism in papillary muscle of patients with mitral valve disease--relation to left ventricular function. 252 75

To evaluate the participation of proteins derived from mitochondrial genes in the adaptive response of skeletal muscle to increased contractile activity, we administered chloramphenicol (CAP; 200-1,000 mg.kg-1.day-1), an inhibitor of translation from mitochondrial ribosomes, to adult rabbits undergoing electrical stimulation of the tibialis anterior muscle of one hind limb. In unmedicated animals, 10 days of electrical stimulation increased maximum velocity (Vmax) of cytochrome oxidase and citrate synthase by 214 +/- 17 and 201 +/- 16% (P less than 0.01). In a dose-dependent manner, CAP abolished activity-induced increases in cytochrome oxidase Vmax, suggesting that augmented mitochondrial protein synthesis is necessary for the adaptive response of enzymes that require protein subunits encoded by mitochondrial genes. However, CAP failed to inhibit activity-induced changes in Vmax of enzymes derived exclusively from nuclear genes (citrate synthase and aldolase). CAP also failed to inhibit activity-induced increases in mRNA transcribed from the nuclear genes encoding beta-F1 ATPase or myoglobin, or from the mitochondrial genes encoding 12S rRNA, 16S rRNA, or cytochrome b. These latter findings suggest that mitochondrial translation products do not participate in pretranslational regulation of these nuclear or mitochondrial genes in response to changes in contractile activity of skeletal muscle.
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PMID:Effects of inhibition of mitochondrial protein synthesis in skeletal muscle. 289 13

Chronic stimulation of rat fast-twitch muscle increased the content of both fatty acid-binding protein (FABP) and myoglobin. The increases in FABP, which reached values close to that of cardiac muscle, exceeded those in myoglobin and those in citrate synthase and 3-hydroxyacyl-CoA dehydrogenase activities.
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PMID:Electrostimulation-induced increases in fatty acid-binding protein and myoglobin in rat fast-twitch muscle and comparison with tissue levels in heart. 292 22

The purpose of this study was to determine if changes in intra-muscular myoglobin concentration accompany histochemical and enzymatic adaptations to supra-maximal exercise training. Subjects were assigned to either a training group (N = 11), who trained 2 to 3 times weekly for 6 wk, or a control group (N = 6). Training progressed from two 15-s and two 30-s "all-out" sprints on a cycle ergometer during week 1 to six 15-s and six 30-s bouts per session during week 6. The Wingate test was performed before and after the 6 wk, but performance variables were not changed in either group. In the training group, peak lactate after the Wingate test was significantly higher after training. No significant changes in enzyme activities, myoglobin concentration, or fiber-type frequency were observed in the control group. In contrast, in the training group, the percent fast twitch oxidative fibers increased, myoglobin decreased, and both citrate synthase and phosphofructokinase activities increased (P less than 0.05). The results suggest that muscle myoglobin concentration is not increased by 6 wk of supra-maximal exercise training and that such training induces cellular adaptations without accompanying performance changes. Alternatively, the Wingate test is not a sensitive test of adaptations to the training.
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PMID:Sprint training effects on muscle myoglobin, enzymes, fiber types, and blood lactate. 295 71

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


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