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 present study was undertaken to examine the effect of 10 days of detraining levels of GLUT-4 protein expression and citrate synthase (CS) activity in the vastus lateralis of trained men. During the course of normal training, seven endurance-trained (T) men and eight age- and weight-matched active but untrained (UT) men underwent an oral glucose tolerance test (OGTT) after an overnight fast. Muscle samples were obtained from the vastus lateralis by needle biopsy for measurement of GLUT-4 protein and CS activity. The tests were repeated on six of the T subjects after 10 days of detraining (DT men). The area under the insulin response curve during OGTT was lower in T men than in DT and UT men (22.4 +/- 2.8, 32.1 +/- 5.9, and 39.9 +/- 4.7 x 10(-3) pmol.l-1.min-1, respectively; P < 0.05). There were no differences between groups in the glucose responses to OGTT. GLUT-4 protein levels and CS activity were higher in T men than in DT and UT men (GLUT-4: 4.37 +/- 0.40, 2.92 +/- 0.53, and 1.71 +/- 0.22 arbitrary standard units and CS: 47.12 +/- 4.75, 33.63 +/- 3.98, and 24.51 +/- 2.97 mumol.min-1.g-1, respectively; both P < 0.05). Muscle GLUT-4 protein content was correlated with CS activity in all three groups (r = 0.64, 0.68, and 0.96 for UT, T, and DT men, respectively). These results suggest that muscle GLUT-4 protein content and oxidative capacity undergo parallel adaptations after detraining in previously well-trained men.
J Appl Physiol (1985) 1994 Sep
PMID:Effect of detraining on GLUT-4 protein in human skeletal muscle. 783 61

The present study examined the relationship between total skeletal muscle GLUT-4 protein level and glucose uptake during exercise. Eight active non-endurance-trained men cycled at 72 +/- 1% peak pulmonary oxygen consumption for 40 min, with rates of glucose appearance and disappearance (Rd) determined by utilizing a primed continuous infusion of [3-3H]glucose commencing 2 h before exercise. Muscle glycogen content and utilization, citrate synthase activity, and total GLUT-4 protein were measured on muscle biopsy samples obtained from the vastus lateralis. A direct relationship existed between preexercise muscle glycogen content and glycogen utilization during exercise (r = 0.76, P < 0.05). Citrate synthase activity and glucose Rd at the end of exercise averaged 21.9 +/- 3.0 mumol.min-1.g-1 and 27.3 +/- 2.5 mumol.kg-1.min-1, respectively. There was a direct correlation between citrate synthase activity and GLUT-4 protein (r = 0.78, P < 0.05); however, at the end of exercise, glucose Rd was inversely related to both GLUT-4 (r = -0.89, P < 0.01) and citrate synthase activity (r = -0.72, P < 0.05). Plasma insulin, which decreased during exercise, was not related to glucose Rd. In conclusion, glucose uptake during 40 min of exercise at 72% peak pulmonary oxygen consumption was inversely related to the total muscle GLUT-4 protein level. This suggests that factors other than the total GLUT-4 protein level are important in the regulation of glucose uptake during exercise.
J Appl Physiol (1985) 1994 Sep
PMID:Skeletal muscle GLUT-4 and glucose uptake during exercise in humans. 783 67

To evaluate the effects of physical training on mitochondrial gene expression and mitochondrial biogenesis in slow-twitch muscle, adult female Sprague-Dawley rats were trained for 3, 6, and 12 wk by running on a motor-driven treadmill (speed of 25 m/min and duration of 90 min/day, 5 days/wk), and the activities of citrate synthase, ubiquinol-cytochrome-c oxidoreductase, cytochrome oxidase, mitochondrial cytochrome b mRNA (by Northern blot analysis), and mitochondrial DNA (by slot-blot and Southern blot analyses) were measured in rat soleus muscle. A DNA probe for detection of mitochondrial mRNA and DNA was prepared from a 1,500-bp fragment of human mitochondrial DNA that included the coding region of the cytochrome b gene. Training for 3, 6, and 12 wk significantly increased the activities of citrate synthase (31, 28, and 47%, respectively), ubiquinol-cytochrome-c oxidoreductase (61, 63, and 77%, respectively), and cytochrome oxidase (25, 26, and 32%, respectively) in muscle. The concentration of cytochrome b mRNA in the muscle was proportionally elevated with the enzyme activities. On the other hand, the mitochondrial DNA concentration in the muscle was not altered by training for 3 or 6 wk but increased significantly after training for 12 wk (35% in the slot-blot analysis and 31% in the Southern blot analysis). These results suggest that an increase in the oxidative capacity of slow-twitch muscle by the relatively short-term training is regulated at the pretranslational step in mitochondrial protein synthesis but that the increase by the long-term training involves mitochondrial replication.
Am J Physiol 1994 Sep
PMID:Enzymatic and genetic adaptation of soleus muscle mitochondria to physical training in rats. 794 19

It is not known precisely how marine mammals are able to maintain muscle function during active swimming in breath-hold dives, when ventilation stops and heart rate falls. Examination of muscle biochemistry and histochemistry can provide information on the relative importance of different metabolic pathways, the contractile potential of the muscle fibres, the oxygen storage capacity of the muscle and the capillary distribution in these animals. In this study, samples of locomotory muscle were taken from wild grey seals (Halichoerus grypus), harbour seals (Phoca vitulina) and Antarctic fur seals (Arctocephalus gazella); Wistar rat muscle was analysed for comparative purposes. Activities of citrate synthase and beta-hydroxyacyl CoA dehydrogenase were higher in the harbour seal muscle than in the grey seal muscle, suggesting that harbour seals have a greater aerobic capacity. Both phocid muscles had a greater reliance on fatty acid oxidation than the fur seal or rat muscles. The myoglobin data demonstrate that the grey seals have the highest oxygen storage capacity of the three pinniped species, which correlates with their greater diving ability. Myoglobin levels were higher in all three pinniped species than in the Wistar rat. The fibre type compositions suggest that the muscles from the fur seals have higher glycolytic capacities than those of the phocid seals [fur seal pectoralis, 7% slow-twitch oxidative fibres (SO), 25% fast-twitch oxidative glycolytic fibres (FOG), 68% fast-twitch glycolytic fibres (FG); grey seal 57% SO, 5% FOG, 38% FG; area per cents]. However, the pectoralis muscle of the fur seal, although the most glycolytic of the pinniped muscles studied, has the highest capillary density, which indicates a high capacity for fuel distribution. These results show that, while pinniped muscle has an increased oxygen storage potential compared with the muscle of a typical terrestrial mammal, there are no distinct adaptations for diving in the enzyme pathways or fibre type distributions of the pinniped muscle. However, the muscle characteristics of each species can be related to its diving behaviour and foraging strategy.
J Exp Biol 1994 Sep
PMID:The metabolic characteristics of the locomotory muscles of grey seals (Halichoerus grypus), harbour seals (Phoca vitulina) and Antarctic fur seals (Arctocephalus gazella). 796 4

1. Treatment of isolated rat liver mitochondria with methyl methacrylate (MM) produced membrane disruption as evidenced by the release of citrate synthase, and changes in the ultrastructure of mitochondria. 2. At concentration 0.1%, MM uncoupled oxidative phosphorylation as evidenced by stimulation of state 4 respiration supported either by pyruvate plus malate or succinate (+rotenone) and ATP-ase activity in intact mitochondria. 3. At concentration 1% MM stimulated ATP-ase activity in intact mitochondria and succinate (+ rotenone) oxidation at state 4 and was without effect on this substrate oxidation at state 3. 4. MM inhibited pyruvate plus malate oxidation either at state 3 or in the presence of uncoupling agents. 5. MM inhibited the NADH oxidase of electron transport particles at a concentration which failed to inhibit either succinic oxidase or the NADH-ferricyanide reductase activity. 6. The data presented suggest that in the isolated mitochondria MM inhibits NADH oxidation in the vicinity of the rotenone sensitive site of complex I. 7. The general conclusion is that MM may block an electron transport and to uncouple oxidative phosphorylation in rat liver mitochondria. The overall in vitro effect would be to prevent ATP synthesis which could result in cell death under in vivo conditions.
Int J Biochem 1994 Sep
PMID:Effect of methyl methacrylate on mitochondrial function and structure. 798 36

The objective of this study was to determine the effect of the beta-adrenergic agonist cimaterol (CIM) on fiber characteristics, capillary supply, and metabolic enzyme activities in muscles of young Friesian bulls. Four pairs of monozygotic twins in each of three live weight groups (WG) were used (initial average live weight [LW]: 162, 299, and 407 kg, respectively). Within each pair, one twin was fed .06 mg of CIM.kg LW-1.d-1 for 90 d. The other twin served as control (C). Needle biopsies were obtained from the longissimus (LM) and semitendinosus (ST) muscles at d 82 to 84 of treatment, and muscle fibers were identified as slow-twitch (Type I) or fast-twitch (Type IIA or Type IIB) by the myosin ATPase stain. In LM, the proportion of Type I (C: 24.0%, CIM: 20.4%; P < .07) and Type IIA fibers (C: 24.2%, CIM: 8.6%; P < .001) decreased, whereas the proportion of Type IIB fibers increased (C: 51.7%, CIM: 71.1%; P < .001). Cimaterol increased the cross-sectional area of Type I (P < .02) and Type IIB fibers (P < .001), with no change in Type IIA fibers. Overall, the mean fiber area increased (C: 2,363 microns 2, CIM: 3,934 microns 2; P < .001). The number of capillaries per fiber did not change, but the number of capillaries per square millimeter decreased (P < .001) after CIM treatment. Cimaterol changed metabolic enzyme activities toward lower oxidative capacity of the muscle (lactate dehydrogenase: +22%, hydroxyacyl-CoA dehydrogenase: -33%, and citrate synthetase: -34%; all P < .001) and reduced the glycogen content by 25% (P < .01).(ABSTRACT TRUNCATED AT 250 WORDS)
J Anim Sci 1994 Sep
PMID:The effect of cimaterol on muscle fiber characteristics, capillary supply, and metabolic potentials of longissimus and semitendinosus muscles from young Friesian bulls. 800 49

A general role for chaperonin ring structures in mediating folding of newly translated proteins has been suggested. Here we have directly examined the role of the E. coli chaperonin GroEL in the bacterial cytoplasm by production of temperature-sensitive lethal mutations in this essential gene. After shift to nonpermissive temperature, the rate of general translation in the mutant cells was reduced, but, more specifically, a defined group of cytoplasmic proteins--including citrate synthase, ketoglutarate dehydrogenase, and polynucleotide phosphorylase--were translated but failed to reach native form. Similarly, a monomeric test protein, maltose-binding protein, devoid of its signal domain, was translated but failed to fold to its native conformation. We conclude that GroEL indeed is a machine at the distal end of the pathway of transfer of genetic information, assisting a large and specific set of newly translated cytoplasmic proteins to reach their native tertiary structures.
Cell 1993 Sep 10
PMID:Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. 810 2

The rates of muscle glucose uptake of trained (TR) and untrained (UT) obese Zucker rats were assessed by hindlimb perfusion under basal conditions (no insulin) in the presence of a maximally stimulating concentration of insulin (10 mU/ml) and after muscle contraction elicited by electrical stimulation of the sciatic nerve. Perfusate contained 28 mM glucose and 7.5 microCi/mmol of 2-deoxy-D-[3H]glucose. Muscle GLUT-4 concentration was determined by Western blot analysis and expressed as a percentage of a heart standard. The rates of insulin-stimulated glucose uptake were significantly higher in the plantaris, red gastrocnemius (RG), and white gastrocnemius (WG), but not the soleus or extensor digatorum longus (EDL) of TR compared with UT rats. After muscle contraction the rates of glucose uptake in the TR rats were significantly higher in the soleus, plantaris, and RG. TR rats had significantly higher GLUT-4 protein concentration and citrate synthase activity than the UT rats in the soleus, plantaris, RG, and WG. Basal plasma membrane GLUT-4 protein concentration of TR rats was 144% above UT rats (P < 0.01). Stimulation by insulin and contraction resulted in a significant increase in plasma membrane GLUT-4 protein concentration in UT rats only. However, plasma membrane GLUT-4 protein concentration in insulin- and contraction-stimulated TR rats remained 53% and 30% greater than that of UT rats, respectively (P < 0.05). Exercise training did not alter basal, insulin-, or contraction-stimulated GLUT-4 functional activity.(ABSTRACT TRUNCATED AT 250 WORDS)
Am J Physiol 1993 Sep
PMID:Effects of exercise training on muscle GLUT-4 protein content and translocation in obese Zucker rats. 821 51

We tested the hypothesis that adaptations in peripheral arterial vasoreactivity are induced by exercise training. Male rats were trained to run on a treadmill at 30 m/min (15 degrees incline) for 1 h/day 5 days/wk for 10-12 wk. Efficacy was indicated by a 51% increase (P < 0.05) in citrate synthase activity in soleus muscle of exercise-trained (ET) rats compared with that of sedentary (SED) control rats. Responses to vasoactive compounds were examined in vitro using rings of abdominal aorta. Maximal isometric contractile tension evoked by KCl, norepinephrine (NE), and phenylephrine were not different between groups; sensitivity to phenylephrine was also not different between groups. However, sensitivity was lower for both KCl and NE in vessels from ET animals. Endothelium removal did not influence KCl sensitivity but did abolish the difference in NE sensitivity of vessel segments between ET and SED animals. Maximal vasodilator responses induced by acetylcholine (ACh; NE or prostaglandin F2 alpha preconstriction) were greater in vessel rings from ET rats. However, dilatory responses by sodium nitroprusside (NE or prostaglandin F2 alpha preconstriction) and forskolin (NE preconstriction) were not different between groups, indicating that the augmented ACh-induced dilatory response resulted from an adaptation of the endothelium. Blockade of nitric oxide synthase activity diminished ACh-induced vasodilation by 79 and 100% in SED and ET rats, respectively. These results indicate that training alters vasomotor function in rat abdominal aortas through adaptations of both endothelium and smooth muscle.
J Appl Physiol (1985) 1993 Sep
PMID:Exercise training alters endothelium-dependent vasoreactivity of rat abdominal aorta. 822 51

Muscle biopsies of the vastus lateralis muscle taken before and after 18 weeks of resistance training were compared by preparing frozen cross sections for electron microscopy and using adjacent sections for fiber typing by myosin ATPase activity. Quantitative ultrastructural changes were observed in histochemically-identified muscle fiber types of twelve young women who underwent the training. The percentage of type IIB fibers decreased and IIA fibers increased. The cross-sectional area of all major fiber types increased with training. The absolute volume of myofibrils, intermyofibrillar space, and mitochondria increased with training for most major fiber types (type I, IIA and IIAB), but the relative volume percentages were not significantly changed because of corresponding fiber hypertrophy. Mean mitochondrial size for types I and IIA and myofibril size for types IIC and IIB increased significantly with training. The capillary number per fiber and density did not change with training. Activity levels were measured for selected glycolytic and oxidative enzymes. Cytochrome oxidase and hexokinase increased significantly with training, while creatine kinase, citrate synthase, phosphofructokinase, glyceraldehyde phosphate dehydrogenase and hydroxyacyl CoA dehydrogenase enzymes were not significantly altered. The results suggest that this type of high-repetition resistance training causes the intracellular components of all fiber types to increase proportionally with an increase in fiber size. In addition, the enzyme analysis indicates the muscle as a whole may increase its oxidative phosphorylation capacity in conjunction with the decreased percentage of type IIB fibers.
Pflugers Arch 1993 Sep
PMID:Muscle fiber types of women after resistance training--quantitative ultrastructure and enzyme activity. 825 33


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