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:1.3.99.3 (acyl-CoA dehydrogenase)
1,425 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activities (Vmax) of hexokinase, glycogen phosphorylase, glucose-6-phosphate dehydrogenase, phosphofructokinase, lactate dehydrogenase, citrate synthase, cytochrome c oxidase, and 3-OH-acyl-CoA dehydrogenase in human skeletal muscles were compared with the in vitro utilization of glucose and palmitic acid assessed under optimal conditions. Statistically significant correlations between substrate fluxes and enzyme activities were found suggesting that the substrate incorporation rate in vitro in some way reflects the capacity of metabolic pathways. The incorporation rate of leucine into muscle proteins was also statistically significantly correlated to the RNA concentration in the muscle tissue. Glycolytic and glycogenolytic enzymes correlated significantly to each other and correlations were also found between aerobic enzymes supporting the validity of constant proportions between certain key enzymes in human skeletal muscles.
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PMID:Incorporation rate of glucose carbon, palmitate carbon and leucine carbon into metabolites in relation to enzyme activities and RNA levels in human skeletal muscles. 17 28

Muscle biopsies were taken from the middle gluteal muscle in 163 healthy Thoroughbreds aged one to six years. The horses were separated according to sex and divided into four different age groups (one, two, three and four to six years). Muscle biopsies were analysed for fibre type (I, IIA and IIB), and the enzyme activities of citrate synthase, 3-OH-acyl-CoA dehydrogenase, lactate dehydrogenase and hexokinase were measured. The percentage of Type I fibres of all horses increased with age, irrespective of sex (from 9 to 16 per cent). The percentage of Type IIA fibres varied with age and sex, increasing in stallions from 34 to 53 per cent and in mares from 27 to 45 per cent, respectively. Correspondingly, the proportion of Type IIB fibres decreased with age and differed between sexes (stallions from 56 to 29 per cent and mares from 65 to 40 per cent) Muscle oxidative capacity increased with age as indicated by significant increases in the activities of citrate synthase (from 32 to 67 mmol/kg/min) and 3-OH-acyl-CoA dehydrogenase (from 20 to 34 mmol/kg/min). The activity of hexokinase increased with age (from 2.4 to 4.8 mmol/kg/min), whereas the activity of lactate dehydrogenase decreased (from 1,754 to 1,444 mmol/kg/min). No differences were seen between stallions and mares in enzyme activities. This study shows that age is one factor influencing enzyme activities, the percentage of Type I fibres and the Type IIA/IIB ratio in M. gluteus medius of Thoroughbreds, and that stallions have a higher Type IIA/IIB ratio compared with mares.
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PMID:Muscle characteristics in Thoroughbreds of different ages and sexes. 188 91

Five Standardbred trotters were trained on a treadmill 3 times/wk for 12 wk by intervals of draft-loaded exercise. The draft load was 34 kp and the velocity approximately 7 m/s. Muscle biopsies were taken from the gluteus medius and longissimus muscles before training and after 2, 4, 8, and 12 wk of training and from the brachiocephalicus muscle before and after training. Both the percentage and the area of type IIa fibers increased and the percentage of type IIb fibers decreased in the gluteus medius muscle during the first 2 wk of training, and then no further significant difference was noted. The percentage of type I fibers increased in the brachiocephalicus muscle, and the area of type IIb fibers increased in the longissimus muscle. The citrate synthase activity increased in the gluteus muscle only, and the increase was seen during the first 2 wk. No significant differences were seen in 3-hydroxy-acyl-CoA dehydrogenase and lactate dehydrogenase activities in the muscles during the entire training period. Less glycogen was utilized in the gluteus muscle and less blood lactate accumulated when the horses performed an unloaded submaximal exercise test after compared with before training. It can be concluded that rapid changes are induced in the gluteus medius muscle when horses are trained pulling a light-draft resistance at a submaximal trotting speed.
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PMID:Effects of a draft-loaded interval-training program on skeletal muscle in the horse. 279 58

A morphometric analysis was performed on horse muscle tissue to quantify mitochondrial distribution relative to capillaries. Samples of M. vastus medialis, M. semitendinosus, M. masseter and M. cutaneus thoracicus were preserved in a glutaraldehyde fixative for electron microscopy, or frozen for biochemical and histochemical analysis. These four muscles varied from highly oxidative in type, consisting nearly completely of type I fibres, in masseter, to highly glycolytic, primarily type IIb fibres, in cutaneus. In all four muscles, mitochondria were found in highest volume density near capillaries at the fibre border, with a sharp decline in volume density towards the fibre centre. This distribution was independent of myoglobin concentration, muscle fibre type and the activities of three key metabolic enzymes, citrate synthase, 3-OH-acyl-CoA dehydrogenase and lactate dehydrogenase.
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PMID:The similarity of mitochondrial distribution in equine skeletal muscles of differing oxidative capacity. 320 68

Seven middle-aged men with manifest type II diabetes mellitus underwent an endurance training programme for 10-15 weeks. The maximal aerobic capacity, as well as the endurance capacity, was improved by 10% (p less than 0.05). The intramuscular glycogen store increased by more than 80% (p less than 0.05) from 350 mumol/g dw (dry weight), and the activities of citrate synthase and 3-hydroxy-acyl-CoA dehydrogenase increased by more than 50% (p less than 0.05) and 30% (p less than 0.05). The activity of glycogen synthase was decreased by approximately 20% (p less than 0.05), whereas lactate dehydrogenase remained unchanged. Capillaries/fibre and fibre area increased by more than 50% (p less than 0.05) and 30% (p less than 0.05) leaving the area of supply constant. Training did not influence fasting blood lipids and glucose, glycosylated hemoglobin, oral glucose tolerance, and insulin response to an oral glucose load measured 72 hours post-exercise. It is concluded that patients with manifest type II diabetes, as normoglycaemic individuals, adapt to physical training. However, no persistent effect on glucohomeostasis and lipaemia is produced by short-term training in the diabetic patients.
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PMID:Skeletal muscle adaptations to physical training in type II (non-insulin-dependent) diabetes mellitus. 336 17

Men with regular physical training habits voluntarily increased their dietary fat intake from 43 to 54% of energy (E%) for four weeks. This was followed by a low-fat (29 E%), high-carbohydrate diet for another four weeks. During the high-fat diet period, the muscle lipoprotein lipase activity (LPLA) increased from 59 +/- 8 to 106 +/- 12 mU/g (mean +/- SE) (P less than 0.05). After the high-carbohydrate diet, LPLA was 57 +/- 16 mU/g, and unchanged relative to the pre-trial value. The triglyceride content in m. vastus lateralis increased from 30 +/- 4 to 47 +/- 9 mmol/kg d.w. (P less than 0.05; mean +/- SE) following the high-fat diet and to 41 +/- 8 following the high-carbohydrate diet. Neither of the diets affected the serum triglyceride and insulin concentrations, nor glucose, glycerol, beta-hydroxybutyrate, citrate and lactate levels in the blood. Nor did they alter enzyme activities in muscle used as markers for the oxidative (citrate synthase, beta-hydroxy-acyl CoA dehydrogenase) and glycolytic (glyceraldehyde phosphate dehydrogenase, lactate dehydrogenase) capacity. It is concluded that one month's adaptation to a high-fat diet results in increased muscle-LPL activity indicating a higher capacity for uptake of fatty acids from circulating serum triglycerides into the muscle cell in association with a greater capacity for triglyceride storage in the muscle. Under these conditions serum triglycerides were not decreased despite the increased muscle LPLA, and serum insulin variations could not explain the change in muscle LPLA.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Lipoprotein lipase activity and intramuscular triglyceride stores after long-term high-fat and high-carbohydrate diets in physically trained men. 354 51

Muscle biopsy samples were collected from the middle gluteal muscle of seven horses undergoing a nine-month endurance training programme. Samples were collected before the programme began and again after three, six and nine months of training. A fifth sample was collected three months after training ceased. Serial muscle sections were reacted histochemically for myosin adenosine triphosphatase after either acid (pH 4.3 and 4.6) or alkaline (pH 10.3) pre-incubation, and muscle fibres identified as type I, IIA, IIB or IIC. The oxidative capacity of individual fibres was assessed, using the reduced nicotinamide dinucleotide tetrazolium reductase stain, and the number of intermyofibrillar capillaries adjacent to each fibre was counted after staining, using the alpha-amylase periodic acid Schiff technique. Biochemical analyses involved the fluorometric measurement of the enzymes citrate synthase, 3-hydroxy acyl CoA dehydrogenase and lactate dehydrogenase as markers of end terminal oxidative, beta oxidative and glycolytic potential, respectively. There was an increase in the percentage of type IIB fibres having high nicotinamide dinucleotide tetrazolium reductase staining after three months training. This increase persisted throughout the period of training and during the period without training. There was an increase in the number of capillaries adjacent to type IIB fibres after six and nine months training. These had returned to near pre-training numbers after three months without training. There were increases in the activities of citrate synthase and 3-hydroxy acyl CoA dehydrogenase after three months training. The activities of both enzymes continued to rise throughout training and the highest activities were attained after nine months.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of a nine-month endurance training programme on muscle composition in the horse. 367 37

Biopsy samples were obtained from the middle gluteal muscle of 10 Thoroughbred horses undergoing a commercial race-training program. Samples were obtained before the program began and again after 6 and 12 weeks of training. All horses had raced at least once by the 12th week of training. Serial sections of muscle were examined histochemically for myosin adenosinetriphosphatase after either acid (pH 4.3 and 4.6) or alkaline (pH 10.3) preincubation, and then muscle fibers were identified as types I, IIA, IIB, or IIC. The oxidative capacity of individual fibers was assessed, using the reduced nicotinamide dinucleotide tetrazolium-reductase stain, and the number of intermyofibrillar capillaries adjacent to each fiber were counted after staining, using the alpha-amylase-periodic acid-Schiff technique. Biochemical analyses involved the fluorometric measurement of 3 enzymes--citrate synthase, 3-hydroxy-acyl coenzyme A dehydrogenase, and lactate dehydrogenase--as markers of end terminal oxidative, beta-oxidative, and glycolytic potentials, respectively. Changes in fiber-type percentages did not occur in response to training. There was a significant (P less than 0.01) increase in the percentage of type IIB fibers, having high nicotinamide dinucleotide-tetrazolium reductase staining after 12 weeks of training. Alterations in the number of capillaries adjacent to each fiber type did not occur during the training period. There were increases in the activities of both citrate synthase and 3-hydroxy-acyl coenzyme A dehydrogenase after 6 weeks (P less than 0.05) and 12 weeks (P less than 0.001) of training. Alterations in the activity of lactate dehydrogenase did not occur in response to training.
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PMID:Effects of training on muscle composition in horses. 394 89

In 12 patients with paramyotonia congenita, percutaneous needle biopsies from the brachial biceps muscle were performed. Muscle fibre area, distribution of muscle fibre types I, II-A and II-B and capillarization were not different from healthy controls. Signs of myopathy with central nuclei in the muscle cells were noted in 9 of the patients. 4 of these patients also had small areas with degeneration and, in one, vacuoles were observed. Quantitative determination of muscle glycogen, water and protein content were within normal range as were enzyme activities for hexokinase, lactate dehydrogenase, citrate synthetase and 3-hydroxy-acyl-CoA dehydrogenase.
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PMID:Skeletal muscle in paramyotonia congenita: biochemistry, histochemistry and morphology. 397 54

Chronic indirect stimulation (10 Hz) was performed on rabbit tibialis anterior muscle. Long-term stimulation (52-140 days) produced a transformation of the fast tibialis anterior into a slow red muscle as judged from the histochemistry of myofibrillar actomyosin ATPase, the pattern of myosin light chains and the thorough rearrangement of the enzyme activity pattern of energy metabolism. Activity levels of citrate synthetase (CS), malate dehydrogenase (MDH), succinate dehydrogenase (SDH), 3-hydroxy-acyl-CoA dehydrogenase (HAD), and lactate dehydrogenase (LDH) were determined quantitatively by either microbiochemical assays (CS, MDH, HAD and LDH) on microdissected, single fibres or by kinetic microphotometry on cross-sectioned fibres (SDH). The activity profiles of these enzymes displayed pronounced scattering in the fibre population of the unstimulated muscle. Despite a several fold increase in the activities of CS, MDH, SDH and HAD and a pronounced decrease in LDH, chronic stimulation failed to abolish the metabolic heterogeneity of the fibre population. It is possible that chronic indirect stimulation cannot produce uniformity of fibres because of continuing diverse natural activity of the motor units.
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PMID:Effects of chronic stimulation on the metabolic heterogeneity of the fibre population in rabbit tibialis anterior muscle. 674 46


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