Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Earlier investigations involving chronic muscle stimulation have shown that skeletal muscle cells possess a much greater metabolic plasticity than had previously been recognized. We have described more fully the time course for the changes in different enzyme systems in single fibres of rabbit fast-twitch tibialis anterior (TA) muscles after periods of continuous stimulation of up to 10 weeks. After 2-5 wk every fibre shows higher levels of many oxidative enzymes than any control fibre; in some cases these levels are 2-10 times higher (well above any found even in the control soleus, a slow-twitch muscle). Citrate synthase, hexokinase and 3-oxoacid CoA-transferase are representatives of this group of enzymes. Other enzymes, such as malate dehydrogenase and amino acid aminotransferases also increase dramatically, but peak single fibre levels do not reach much above the highest in controls. These differential effects confirm at the single fibre level that chronic stimulation can alter mitochondrial composition. According to their staining reaction for myofibrillar ATPase, TA fibres are approximately 25% type IIA, and 75% type IIB, but by 5 wk these are converted to a mixture of type I, IIA and IIC fibres. At 5 wk, levels of glycolytic and high-energy phosphate transfer enzymes had decreased by 80% or more, and seemed to be adjusted to levels appropriate to their (new) ATPase type. This is in contrast to many enzymes of oxidative metabolism, which increase without synchronization with fibre type change. Determinations of metabolite concentrations in individual fibres from muscles freeze-clamped after varying periods of stimulation gave results which differ strikingly from data for acute stimulation. The findings reinforce our previous view that the high levels of ATP utilization engendered by chronic stimulation of muscle elicit a matching response in ATP production through a series of profound adaptations. Some of these are never encountered under the less extreme conditions of endurance exercise. Such features add to the interest and value of the chronic stimulation model as a means of studying the metabolic plasticity of muscle.
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PMID:Chronic stimulation of mammalian muscle: enzyme and metabolic changes in individual fibres. 252 28

Several functional parameters were studied in a non-synaptic population of brain mitochondria from rats made cirrhotic by chronic treatment with carbon tetrachloride, with and without coma produced by a single injection of ammonium acetate. The following changes were observed in mitochondria from cirrhotic rats, independently of the presence of coma: (a) a large decrease in oxygen consumption with pyruvate-malate as substrate, but not with succinate, in both states 3 and 4; (b) a modified volume oscillation pattern, characterized by a notable diminution in the amplitude of the oscillation; (c) an altered pattern of acyl groups, with a decrease in the proportion of unsaturated with respect to saturated fatty acids. The following parameters were also measured in brain mitochondria from the cirrhotic rats and were found unchanged: (a) malate dehydrogenase and ATPase activities; (b) content of cytochromes; (c) phospholipid composition; (d) total fatty acid content. The possible significance of the changes observed is discussed in terms of the membranal and biochemical alterations that may be involved in the mechanism of hepatic encephalopathy.
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PMID:Functional changes of brain mitochondria during experimental hepatic encephalopathy. 253 14

The changes in histopathology and enzyme histochemistry of thymus induced by a single intraperitoneal injection of sublethal doses of cadmium chloride into Kunming male mice were examined. The swollen endothelium of capillaries was observed, with an obviously decreased activity of ICDH, LDH and ATPase, which seemed to be due to direct inhibition by cadmium at the 4th hour. The necroses of the cortex thymocytes were found at the 8th hour after injection and reached an extreme at the 16-24th hour, while few necroses of the lymphocytes in the medulla. Beginning 4th to 8th hour after exposure, the activity of enzymes was located in mitochondria of the cortex thymocytes, i.e., SDH, ICDH, CCO and ATPase, was decreased gradually. It suggested that thymic cortex had a marked impairment of blood supply and anoxia. Within 2 days after a single injection the cortex of the gland was mainly populated by epithelial reticular cells except a few lymphocytes. It was noted that there were some bigger cells which were characterized by their large size, basophilic cytoplasma, rough chromatin and high mitotic ability and activity of MDH, LDH, G-6-PD increased in these cells. From above observation the author concluded that the cause of cadmium-induced acute thymic atrophy was lymphocyte necroses within thymic cortex. The mechanism of the cortex thymocytes necrosis was possibly secondary to an anoxia of cortex resulting from capillary damage in the cortex. The ability of thymic regeneration is strong after being damaged. The regenerate cells possessed characteristics of morphology and enzyme histochemistry of immature cells, which probably came from the bone marrow.
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PMID:[Changes in histopathology and enzyme histochemistry of thymus in cadmium exposure mice]. 253 4

Oral administration of DEHP, 1000 mg/kg body weight, to rats daily from 6 to 15 day of gestation resulted in retardation of fetal growth and increase in fetal liver weight which contained significant quantities of DEHP. The activities of mitochondrial succinate dehydrogenase, malate dehydrogenase, cytochrome c oxidase and adenosine triphosphatase were decreased in fetal liver. The data indicate that exposure of mothers to DEHP during pregnancy could adversely affect the fetal livers by interfering with bioenergetics of the cell.
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PMID:Biochemical alterations in rat fetal liver following in utero exposure to di(2-ethylhexyl)phthalate (DEHP). 263 47

Fibers of the garter snake transversus abdominis muscle fall into three classes according to contraction speed: faster and slower twitch and tonic. To determine the relationship between these physiologically determined classes and established mammalian fiber types, individual fibers were assayed for key enzymes representing the major energy-generating pathways in vertebrate muscle. Five such enzymes were examined: lactate dehydrogenase, malate dehydrogenase, adenylokinase, fumarate hydratase, and beta-hydroxyacyl-CoA dehydrogenase. The muscle contained three principal metabolic fiber types. Fast-contracting twitch fibers had low-oxidative but high-glycolytic capacity and therefore resembled mammalian-type fast-twitch glycolytic (FG) fibers. Slower twitch fibers were high oxidative-high glycolytic, similar to mammalian-type fast-twitch, oxidative, glycolytic (FOG) fibers. Tonic fibers were high oxidative-low glycolytic; this metabolic profile is characteristic of type slow-twitch oxidative (SO) fibers in mammals. Activity of the enzyme adenylokinase, which in mammals correlates with contraction speed and myosin adenosine triphosphatase (ATPase) activity, separated these reptilian fibers into three groups that are similar but not identical to those delineated by oxidative and glycolytic enzymes. Adenylokinase and beta-hydroxyacyl-CoA dehydrogenase showed the widest range of activities in snake muscle and, therefore, the greatest ability to discriminate fiber types.
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PMID:Metabolic fiber types of snake transversus abdominis muscle. 273 94

It has been proposed that cellular ageing may be caused by loss of mitochondrial function due to the action of free radicals. To investigate this hypothesis, antigenic structures of the mitochondrial inner membrane/matrix and of the outer mitochondrial membrane of human diploid fibroblasts were monitored by immunoblotting at four stages during cellular lifespan in vitro. At the same time, specific activities of the enzymes oligomycin-sensitive ATPase (O-S ATPase), malate dehydrogenase (MDH) and glutamate dehydrogenase (GDH) were assayed to assess the functional capacity of cellular oxidative phosphorylation and of the tricarboxylic acid cycle. No changes were found with ageing in inner mitochondrial membrane-associated matrix components, or in the activities of O-S ATPase and MDH. However GDH activity increased significantly with ageing in vitro, possibly indicating greater amino acid utilization for energy production in older cells. There was loss of an outer mitochondrial membrane antigen, of approximate molecular weight 60 kilodaltons (kDa), in the oldest cells tested, which may influence outer membrane transport capacity late in the cellular lifespan. Overall, the results fail to provide support for the hypothesis that ageing primarily results from free radical-induced impairment of mitochondrial function.
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PMID:Mitochondrial antigenic structure and enzyme activity in ageing human diploid fibroblasts. 278 45

Cell-free extracts of two strictly anaerobic mollicutes, Anaeroplasma intermedium 5LA and Asteroleplasma anaerobium 161T, were tested for enzymic activities of intracellular carbohydrate metabolism. Asteroleplasma anaerobium was also tested for enzymes of purine and pyrimidine metabolism. Both organisms had enzymic activities associated with the nonoxidative portion of the pentose phosphate pathway, and with the Embden-Meyerhoff-Parnas pathway. The 6-phosphofructokinase (PFK) of Asteroleplasma anaerobium was ATP-dependent, whereas the PFK of Anaeroplasma intermedium was PPi-dependent. The two anaerobic mollicutes also differed with respect to the enzymes that converted phosphoenolpyruvate (PEP) to pyruvate; Anaeroplasma intermedium had pyruvate kinase activity, but Asteroleplasma anaerobium had pyruvate, orthophosphate dikinase activity (PPi-dependent). Both organisms had lactate dehydrogenase activity which was activated by fructose 1,6-bisphosphate (Fru-1,6-P2). Anaeroplasma intermedium had activity for PEP carboxykinase (activated by Fru-1,6-P2), but Asteroleplasma anaerobium did not. PEP carboxytransphosphorylase activity was not detected in either organism. Anaeroplasma intermedium had malate dehydrogenase and isocitrate dehydrogenase activities, but it had no activities for the three other tricarboxylic acid cycle enzymes examined; Asteroleplasma anaerobium had malate dehydrogenase activity only. Asteroleplasma anaerobium had enzymic activities for the interconversion of purine nucleobases, (deoxy)ribonucleosides, and (deoxy)ribomononucleotides, including PPi-dependent nucleoside kinase, reported heretofore only in some other mollicutes. Asteroleplasma anaerobium could synthesize dTDP by the thymine salvage pathway if deoxyribose 1-phosphate was provided, and it had dUTPase, ATPase, and dCMP kinase activities. It lacked (deoxy)cytidine deaminase, dCMP deaminase, and deoxycytidine kinase activities.
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PMID:Enzymic activities of carbohydrate, purine, and pyrimidine metabolism in the Anaeroplasmataceae (class Mollicutes). 281 26

The synthetic "picket fence" porphyrin, tetra(o-acetamidophenyl)porphine (TAc), as a biological photosensitizer has been evaluated both in vitro and in vivo in mitochondria from the R3230AC mammary tumor. Studies in vitro, consisting of incubation of mitochondria with TAc at a concentration of 4.0 micrograms/ml followed by photolysis, result in the inhibition of cytochrome c oxidase, proton translocating ATPase, succinate dehydrogenase, and malate dehydrogenase. The diminution in activity of the first three enzymes is approximately 2-fold greater than that seen with Photofrin II under the same conditions. Although TAc exists as four isolable atropisomers, no differences among these different forms were observed in their photosensitized inhibition of mitochondrial enzymes. Administration to tumor-bearing rats of TAc i.p. at a dose of 25 mg/kg did result in accumulation of porphyrin within the mitochondria of the R3230AC tumor as determined by subsequent irradiation of isolated mitochondria. The potential utility of TAc and related porphyrins in cancer phototherapy is discussed.
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PMID:Picket-fence porphyrins as potential phototherapeutic agents. 283 16

In vivo administration of L-thyroxine (L-T4) in Anabas testudineus, while significantly stimulated the activities of cytochrome c oxidase and alpha-glycerophosphate dehydrogenase (alpha-GPDH), inhibited glucose-6-phosphate dehydrogenase (G-6-PDH), cytosolic and mitochondrial malate dehydrogenase (cyt. MDH; mit. MDH), and Mg2+ DNP-dependent adenosine triphosphatase (Mg2+ ATPase) activities. The activities of lactate dehydrogenase (LDH), succinate dehydrogenase (SDH), and catalase remained unaltered after L-T4 treatment. Administration of protein synthesis inhibitors such as actinomycin D, while significantly inhibited cytochrome oxidase, alpha-GPDH, catalase, SDH, and Mg2+ ATPase activities, did not change LDH, cyt. MDH, and mit. MDH activities. Chloramphenicol injection significantly stimulated cytochrome oxidase, alpha-GPDH, and G-6-PDH activities. Simultaneous injections of actinomycin D or chloramphenicol with 3,5,3'-triiodo-L-thyronine (L-T3) or L-T4 prevented the effects of thyroid hormones on enzyme activities, when compared to the respective controls.
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PMID:Oxidative metabolism in a teleost, Anabas testudineus Bloch: effect of thyroid hormones on hepatic enzyme activities. 292 Sep 3

The adaptation of human skeletal muscle to endurance training and detraining has been investigated. The following variables were monitored: phenotypic expression of slow and fast isoforms of myofibrillar ATPase, as well as contractile and regulatory proteins, capillary supply and fibre areas, levels of enzymes in the main metabolic pathways and the NADH shuttles. For the latter purpose, several methodological surveys were undertaken. The main findings and conclusions are: Endurance training can induce a transformation of type II (fast-twitch) fibres into myofibrillar ATPase intermediate fibres (IM fibres: types IIC, IIC-IB and IB). Using immunohistochemical techniques, a co-existence of slow and fast isoforms of whole myosin, myosin heavy chains, and myosin lights chains as well as troponin C, T and I components, was demonstrated in the training-induced IM fibres. Furthermore, a co-existence of slow and fast isoforms of myofibrillar ATPase in the IM fibres, can be anticipated from the stainings for myofibrillar ATPase. No neonatal myosin heavy chains could be detected in any of the trained muscle fibres. The IM fibres were intermediate between type I (slow-twitch) and type II also with regard to morphological and metabolic characteristics. Along with other lines of evidence, the occurrence of IM fibres in conjunction with endurance training demonstrates that transformation of fibre type II to type I can occur in response to endurance training. On the basis of findings of a decreased spread of fibre areas among individuals in connection with extensive endurance training, it is suggested that fibre sizes are determined by two conflicting demands: good diffusion conditions and high force development. The existence of a mechanism that can elicit decreases in fibre size, despite extensive use of the fibres, is suggested. The magnitude by which levels of oxidative enzymes and capillary supply are enhanced by endurance training is dependent on both the exercise intensity and the duration. However, if the intensity is below a certain critical point, its inefficiency in stimulating to adaptive changes can not be compensated for by even a very long duration of exercise. The patterns of training-induced increases in CS, MDH and HAD indicate that the levels of these enzymes can be regulated independently. It appears possible that the levels of the malate-aspartate shuttle enzymes can vary in relation to citric acid cycle enzymes depending on the extent to which oxidation of fatty acids contributes to the metabolism. Detraining results in rather rapidly regressing levels of oxidative enzymes and capillary supply.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Plasticity of human skeletal muscle with special reference to effects of physical training on enzyme levels of the NADH shuttles and phenotypic expression of slow and fast myofibrillar proteins. 295 Jul 27


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