Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Endurance exercise training has been found to enhance the functional capacity of the myocardium in several animal models. The sub-cellular phenomena accompanying the augmented function are yet to be explained. The present study sought to determine if the myosin ATPase activity of cardiac muscle increased as a result of endurance conditioning. Five beagles trained by running on a motor driven treadmill (T) and five control (NT) animals were studied. Follwoing 10 weeks of training the T group had a significantly (P less than .05) lower heart rate than the NT while performing the same submaximal exercise and the gastrocnemius cytochrome oxidase activity was significantly greater (P less than .005) in the T than in the NT. These two measurements established that the exercised animals were physically trained. Myosin was isolated from the left ventricular myocardium and activated in a medium containing K-EDTA. No significant (P less than .05) difference in maximum myosin ATPase activity was observed between the NT and T groups in cardiac muscle. It was concluded that cardiac muscle myosin ATPase activity was not affected by 10 weeks of endurance conditioning induced by treadmill running in dogs.
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PMID:Effect of endurance training on myocardial myosin adenosine triphosphatase activity of the dog. 16 Apr 87

The goal was to describe the metabolic profile of ganglionic and cortical arteries and arterioles in aging normotensive male rats. Five enzymes indicative of key metabolic pathways in the vessel walls were semiquantitatively evaluated using bright-field histochemical microscopy. Lactate dehydrogenase showed significant reactivity which increased with vessel diameter in cortical and ganglionic vessels in all age groups tested. Succinate dehydrogenase and cytochrome oxidase showed little reactivity in both cortical and ganglionic vessels, suggesting a reduced role for aerobic metabolic pathways. Myosin ATPase reactivity was high in cortical and ganglionic vessels. Only this enzyme showed an increased reactivity that was correlated with the age and diameter of the vessel. Glucose-6-phosphate dehydrogenase reactivity was more pronounced in cortical than ganglionic vessels, suggesting that the hexose-monophosphate-shunt may be more active in the cortical vessels. There were no regional differences in enzyme reactivity throughout the caudatoputamen. In conclusion, both the cortical and ganglionic vessels are metabolically active, with significant anaerobic glycolysis, and reduced, but observable capacity for aerobic metabolism. The decreased myosin ATPase reactivity and the low level of glucose-6-phosphate dehydrogenase reactivity in the ganglionic arterioles of senescent rats may contribute to the susceptibility of these vessels to cerebrovascular accidents.
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PMID:A histochemical study of cerebral cortical vessels and ganglionic vessels of the caudatoputamen in aging normotensive rats. 315 35

Coronary arteries and arterioles in the left ventricle from the primate Macaca fascicularis were histochemically examined to evaluate their metabolic profiles. Succinate dehydrogenase and cytochrome oxidase activities were assessed to evaluate aerobic metabolic capacity, while myosin ATPase activity was determined as an index of ATP utilization for contraction. Anaerobic capacity was evaluated from lactate dehydrogenase and glycogen reactivity. Glucose-6-phosphate dehydrogenase was examined to determine capacity of the hexose-monophosphate-shunt, while the amounts of deoxyribonucleicc and ribonuclei acids were assessed as possible indicators of protein synthesis. Succinate dehydrogenase and cytochrome oxidase demonstrated slight reactivity in both coronary arteries and arterioles indicating a low capacity for aerobic metabolism. Myosin ATPase showed strong activity in arteries and even stronger reactivity in arterioles, suggesting that arteriolar smooth muscle is more capable of utilizing ATP. Glucose-6-phosphate dehydrogenase activity was extremely low in both arteries and arterioles, while deoxyribonucleic and ribonucleic acids demonstrated only slight to moderate reactivity in both arteries and arterioles, indicating that under normal conditions the coronary vasculature appears quite stable with little cell proliferation.
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PMID:A histochemical evaluation of metabolism in the coronary vasculature of the primate. 617 63

A histochemical study of the metabolism of rat renal arteries and arterioles. Rat renal arteries and arterioles were examined histochemically to determine their metabolic profiles. Succinate, malate and NAD-isocitrate dehydrogenase, cytochrome oxidase and ubiquinone were assessed to determine aerobic metabolism. Glucose-6-phosphate dehydrogenase and DPN diaphorase were evaluated to determine hexose-monophosphate-shunt activity. Anaerobic metabolism was evaluated via lactate dehydrogenase, and the substrate, glycogen. Gomori's lipase, beta-hydroxybutyrate dehydrogenase and amounts of neutral fat and free fatty acids were assessed as indicators of lipid utilization. Myosin ATPase activity was evaluated as an index of ATP utilization for contraction. Deoxyribonucleic and ribonucleic acids were appraised as indicators of protein synthesis. In general, the oxidative enzymes and myosin ATPase demonstrate considerable activity in renal arteries and arterioles which suggests aerobic metabolism and ATP usage. Renal arteries and arterioles also appear capable of anaerobic metabolism as indicated by strong lactate dehydrogenase reactivity and by the presence of slight to moderate quantities of glycogen, while high levels of glucose-6-phosphate dehydrogenase and moderate amounts of deoxyribonucleic acid suggest a potential for beta-hydroxybutyrate dehydrogenase, minimal lipase activity, and the absence of fatty acids with substantial amounts of neutral fat, indicate limited lipid catabolism.
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PMID:A histochemical study of the metabolism of rat renal arteries and arterioles. 620 11

The intent of this study was to determine whether endurance exercise training regulates increases in metabolic enzymes, which parallel modulations of myogenin and MyoD in skeletal muscle of rats. Adult Sprague-Dawley rats were endurance trained (TR) 5 days weekly for 8 wk on a motorized treadmill. They were killed 48 h after their last bout of exercise. Sedentary control (Con) rats were killed at the same time as TR animals. Myogenin, MyoD, citrate synthase (CS), cytochrome-c oxidase (COX) subunits II and VI, lactate dehydrogenase (LDH), and myosin light chain mRNA contents were determined in soleus muscles by using RT-PCR. Myogenin mRNA content was also estimated by using dot-blot hybridization. Protein expression levels of myogenin and MyoD were measured by Western blots. CS enzymatic activity was also measured. RT-PCR measurements showed that the mRNA contents of myogenin, CS, COX II, COX VI, and LDH were 25, 20, 17, 16, and 18% greater, respectively, in TR animals compared with Con animals (P < 0.05). The ratio of myogenin to MyoD mRNA content estimated by RT-PCR in TR animals was 28% higher than that in Con animals (P < 0.05). Myosin light chain expression was similar in Con and TR muscles. Results from dot-blot hybridization to a riboprobe further confirmed the increase in myogenin mRNA level in TR group. Western blot analysis indicated a 24% greater level of myogenin protein in TR animals compared with Con animals (P < 0.01). The soleus muscles from TR animals had a 25% greater CS enzymatic activity than the Con animals (P < 0.01). Moreover, myogenin mRNA and protein contents were positively correlated to CS activity and mRNA contents of CS, COX II, and COX VI (P < 0.05). These data are consistent with the hypothesis that myogenin is in the pathway for exercise-induced changes in mitochondrial enzymes.
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PMID:Myogenin and oxidative enzyme gene expression levels are elevated in rat soleus muscles after endurance training. 1503 61