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)

A light microscopy study on the localization of enzyme activity within atherosclerotic human intracranial arteries was performed on autopsy material obtained within 4 hours of death. The data suggests that the atherosclerotic process first goes through a proliferative phase and then a degenerative phase culminating in the formation of a plaque. In the proliferative phase, smooth muscle cell proliferation has formed a thickened intima. Tetrazolium reductase, adenosine triphosphatase (ATPase) and adenosine monophosphatase (AMPase) activities are present in these cells, while all dehydrogenases and acid phosphatase activities were weak or not present. As the degenerative phase commences, an area of necrosis, lipid and macrophage accumulation is formed on the lumen side of the elastica. This area increases in size until a plaque is formed. Unsaturated polar and nonpolar lipid, cholesterol, alpha-glycerophosphate dehydrogenase, acid phosphatase, and AMPase activities are associated with these areas and in foam cells, which are often found in the thickened intima of the proliferative phase. Tetrazolium reductase and ATPase activities decrease in the thickened intima as the area of necrosis increases in size, while dehydrogenase activity, except that for alpha-glycerophosphate, remains low or not present. Patterns of enzyme alterations for various stages of the disease process in intracranial arteries, the aorta and coronary arteries suggest a similar, if not identical, progression of the atherosclerotic process, irrespective of known differences in the prevalence of atherosclerosis.
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PMID:A histoenzymatic study of human intracranial atherosclerosis. 426 Jul 21

An analysis is presented of the similarities and differences in receptor-effector relationships in the actions of aldosterone and triiodothyronine on the kidney. Both agents augment tubular reabsorption of sodium at different sites in the nephron. Aldosterone acts primarily distally and triiodothyronine, primarily proximally. In both cases, the respective hormone-receptor complexes associate with target cell chromatin and modulate the abundance of specific coding by mRNAs for regulatory proteins. The quantitative relationships between nuclear-receptor occupancy and responses were analyzed by fractional plots in a bounded domain. When applied to the toad bladder, this analysis revealed a parabolic dependence of the increase in transepithelial Na+ transport on the abundance of nuclear of the increase in transepithelial Na+ transport on the abundance of nuclear aldosterone-receptor complexes. In contrast, four independent response parameters (QO2, QO2(t), Na-K-ATPase, alpha-glycerophosphate dehydrogenase) exhibited a hyperbolic dependence on nuclear abundance of T3 in the rat kidney. The observed cosaturation of nuclear occupancy and responses in both systems, for both hormones, implies that the respective high-affinity binding sites are authentic receptors. Further information is needed on the molecular bases of the nonlinear response-occupancy relationships in hormone action on the kidney.
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PMID:Receptors and effectors in hormone action on the kidney. 617 41

Leg muscles of adult rats were stimulated chronically at a low-frequency, and the histochemical reactions of various enzymes (succinic dehydrogenase, mitochondrial alpha-glycerophosphate dehydrogenase, phosphorylase, alkali-ATPase and acid-ATPase), capillary density, resistance to fatigue, and contractile properties were studied. Following stimulation, the histochemical properties of muscle fibres in the fast extensor digitorum longus (EDL) and tibialis anterior (TA) muscles became similar to those of the majority of fibres in the slow soleus muscle. In the soleus muscle, the histochemical properties of the few fast type fibres became similar to the majority of 'slow' fibres so that its fibre composition was homogeneously 'slow'. The stimulated fast muscles also had higher capillary density and were more resistant to fatigue than normal. Despite the prolonged stimulation, the twitch duration of the fast muscles was little changed. This result differs from the findings obtained previously for the rabbit and cat, which show that slowing of contraction can be achieved by low-frequency activity of similar duration. Thus it may be that there is a species difference regarding the readiness with which the transformation of fast to slow muscles can be brought about.
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PMID:Effects of low-frequency electrical stimulation on fast and slow muscles of the rat. 621 64

Crossed immunoelectrophoresis was used to analyze the components of membrane vesicles of anaerobically grown Escherichia coli. The number of precipitation lines in the crossed immunoelectrophoresis patterns of membrane vesicles isolated from E. coli grown anaerobically on glucose plus nitrate and on glycerol plus fumarate were 83 and 70, respectively. Zymogram staining techniques were used to identify immunoprecipitates corresponding to nitrate reductase, formate dehydrogenase, fumarate reductase, and glycerol-3-phosphate dehydrogenase in crossed immunoelectrophoresis reference patterns. The identification of fumarate reductase by its succinate oxidizing activity was confirmed with purified enzyme and with mutants lacking or overproducing this enzyme. In addition, precipitation lines were found for hydrogenase, cytochrome oxidase, the membrane-bound ATPase, and the dehydrogenases for succinate, malate, dihydroorotate, D-lactate, 6-phosphogluconate, and NADH. Adsorption experiments with intact and solubilized membrane vesicles showed that fumarate reductase, hydrogenase, glycerol-3-phosphate dehydrogenase, nitrate reductase, and ATPase are located at the inner surface of the cytoplasmic membrane; on the other hand, the results suggest that formate dehydrogenase is a transmembrane protein.
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PMID:Identification and localization of enzymes of the fumarate reductase and nitrate respiration systems of escherichia coli by crossed immunoelectrophoresis. 621 54

The behavior of several enzymes was studied during rat heart development (4 days before birth to adult stage). Hexokinase has its highest activity during the fetal period; it decreases at birth and remains with low activity in the adult. The alpha-glycerophosphate dehydrogenase and alpha-glycerophosphate oxidase profiles are similar up to the 15th day of development. From there onwards, both profiles diverge, the cytoplasmic activity increasing 3-fold, while the mitochondrial activity remains unchanged. The developmental profiles of the malate dehydrogenases are almost parallel. The development of citrate synthase and succinate dehydrogenase results in a 2- to 4-fold increase in their activities. However, ATPase increases dramatically (20-fold) over the same period. With respect to the enzymes of the adenine nucleotide metabolism, adenylate kinase is fully expressed throughout all ages examined, showing no variation during development. AMP deaminase and creatine kinase increase during development, the cytoplasmic creatine kinase reaching a high level at birth whereas the increases of the mitochondrial enzymes take place gradually during development.
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PMID:Development of enzymes of energy metabolism in rat heart. 623 Jan 12

Thyroid status was altered by use of a low-iodine-perchlorate (PC) regimen and either reversal with NaI or injections of L-3,5,3'-triiodothyronine (T3). The PC regimen decreased renal and hepatic oxygen consumption (QO2), alpha-glycerophosphate dehydrogenase (alpha-GPDH), and Na+-K+-dependent adenosine triphosphatase (Na-K-ATPase) to comparable extents (25 vs. 23%, 26 vs. 39%, and 41 vs. 51%, respectively). Administration of T3 to hypothyroid rats elicited dose-dependent increases in hepatic and renal cortical QO2, ouabain-sensitive oxygen consumption (QO2(t)), alpha-GPDH, and Na-K-ATPase activities. The half-maximal increases in all of the response parameters in both kidney and liver were obtained at dosages of 6-32 micrograms T3/100 g body wt. The equivalences in the renal cortical vs. hepatic responses were indicated by correlation coefficients of approximately 0.97. Kidney and liver nuclei also showed similar high-affinity binding of 125I-T3-K1/2 = 29 vs. 18 micrograms T3/100 g body wt, and Nmax = 1.8 vs. 2.1 ng T3/mg DNA. The patterns of the responses plotted as a function of T3 occupancy of the high-affinity nuclear binding sites were indistinguishable in kidney and liver. These results imply similar modes of action of T3, probably initiated at the nuclear level, in both kidney and liver.
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PMID:Nuclear binding of T3 and effects of QO2, Na-K-ATPase, and alpha-GPDH in liver and kidney. 625 44

The absence of the thyroid stimulation of hepatic [Na+ + K+]ATPase in obese (ob/ob) mice has been investigated. A wide range of tri-iodothyronine (T3) concentrations failed to enhance the hepatic [Na+ + K+]ATPase of ob/ob mice made hypothyroid by methimazole treatment but glycerophosphate dehydrogenase activity was maximally stimulated at low doses of T3. Adrenalectomy increased the basal activity of [Na+ + K+]ATPase to levels found in lean control mice and restored the response of this enzyme to T3. Body weight gain was unaffected by the induction of hypothyroidism in either lean or ob/ob mice. It is concluded that the adrenal steroids play an important role in the expression of [Na+ + K+]ATPase activity in the ob/ob mouse.
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PMID:Effects of thyroid hormone and adrenalectomy on [Na+ + K+]ATPase in the ob/ob mouse. 627 59

The effects of thyroid hormone treatment on brown adipose tissue (BAT) and liver metabolism were assessed by measuring oxygen consumption, sodium-potassium adenosine triphosphatase (Na-K-ATPase), and mitochondrial alpha-glycerophosphate dehydrogenase (alpha-GPD) activities in tissues from triiodothyronine- (T3) and vehicle-injected (for 3 days) newborn and adult rabbits. In the newborns, basal BAT cellular respiration was increased [mean (%/- SE) = 119 +/- 18 vs. 65 +/- 4 microliter O2/10(6) cells-1 . h in controls (P less than 0.005)], whereas hepatic respiration was unchanged. Ouabain had no effect on basal BAT cellular respiration, but suppressed hepatic respiration by 30% in both newborn groups. T3 treatment had no effect on NE- (10(-6) M) stimulated BAT respiration, whereas adult hepatic respiration was increased almost twofold. alpha-GPD activities were increased in both newborn BAT and adult liver but not in newborn liver. Na-K-ATPase activity was significantly increased only in newborn liver. In conclusion, 1) both BAT and liver are thyroid-hormone sensitive in the newborn rabbit, but the responses to T3 treatment are different in the two tissues; 2) the failure to stimulate both hepatic alpha-GPD and respiration in the newborn appears to be a developmental phenomenon characteristic of the rabbit; 3) thyroid hormones have little effect on sodium transport-dependent respiration in either BAT of liver in the newborn rabbit.
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PMID:Thyroid hormone-sensitive brown adipose tissue respiration in the newborn rabbit. 627 13

The effect of 1-3,5,3'-triiodothyronine (T3) and thyroxine (T4) on (Na+ +K+)-ATPase activities was examined in rabbit kidneys because in this tissue almost 80% of the metabolism is connected to active sodium transport. T3-receptor concentrations were estimated as 0.62 and 0.80 pmol/mg per DNA in the cortex and outer medulla, respectively. A dose of 0.5 mg T3/kg body weight for 3 days increased basal metabolic rate by almost 60%, and the mitochondrial 1-alpha-glycerophosphate dehydrogenase activity was increased by 50% in both the cortex and medulla. (Na+ +K+)-ATPase activity in the liver was raised by almost 50%. However, no changes in (Na+ +K+)-ATPase activities or binding sites for [3H]ouabain in either the kidney cortex or medulla could be observed. T4 at 16 mg/kg daily for 14 days was also without effect on renal (Na+ +K+)-ATPase activities. Furthermore, the response to T3 was absent at high sodium excretion rates induced by unilateral nephrectomy and extracellular volume expansion. Thus, despite stimulation of basal metabolic rate and renal 1-alpha-glycerophosphate dehydrogenase activity by T3 and T4, the (Na+ +K+)-ATPase activity in the rabbit kidney is identical in euthyroid and hyperthyroid states. However, thyroid hormones prevent the normal natriuretic response to extracellular volume expansion.
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PMID:Lack of stimulation of renal (Na+ +K+)-ATPase by thyroid hormones in the rabbit. 628 89

Early postnatal changes (4-5 days to 15 days after birth) in the biochemical composition of microsomes were investigated in rabbit skeletal muscles destined to become fast-twitch muscles. During this period, a steady decrease in the microsomal content of cholesterol and of ouabain-sensitive Na + /K + -ATPase activity, as well as a decrease in protein electrophoretic components in the 80 000-70 000 molecular weight range, were observed. These changes are probably due to a diminishing yield of microsomal membranes derived from T-tubules, as the age of the animals increases, and are indicated from a knowledge of the mixed composition of muscle microsomes and previous biochemical data on isolated T-tubules. The content of cytochrome b5, which was found to be high in muscle microsomes of newborn animals, decreased strikingly as the amount of membrane-bound Ca2 + -ATPase protein increased, with a crossing-over point at about 7-10 days after birth. These changes, possibly corresponding to a transition from precursor sarcoplasmic reticulum (SR) to mature SR, were found to be temporally correlated with changes in [3H] alpha-tocopherol binding ability of the microsomes and in the mitochondrial content of glycerol phosphate dehydrogenase. At the same critical periods, coincident with the onset of motile activity, the immunological cross-reactivity of the Ca2 + -ATPase protein of microsomal vesicles, with antibody specific for the Ca2 + -ATPase of adult fast SR, was found to increase markedly, as tested by competitive enzyme-linked immunosorbent assay (ELISA). The immunological data are consistent with data in the literature demonstrating an increase in the concentration of Ca2 + -ATPase molecules in the SR membranes during ontogenic development. Both these data and catalytic data, however, suggest that the Ca2 + -ATPase protein is present in the same form in the SR of immature and of adult fast muscle and, in an antigenically different form, in slow muscle SR.
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PMID:Transitions in membrane composition during postnatal development of rabbit fast muscle. 628 21


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