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:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Intramuscular injections of the title drug in a dose of 5 mg/kg (5% of the LD50) during 10 days produced in the liver and blood serum of white rats a decrease in the activity of glucokinase, succinate dehydrogenase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, glutathione reductase, ATPase and ceruloplasmin. The urea content in total phospholipids rose, whereas the content of triglycerides and hexosamine diminished. Ten and 20 days after the drug was discontinued the majority of these characteristics returned to normal. The activity of glucosophosphate isomerase, transketolase, glucose-6-phosphatase, fructose-1,6-diphosphatase and lactate dehydrogenase as well as the content of total cholesterol, free fatty acids, tyrosine, hydroxyproline, total protein, RNA and DNA remained unchanged.
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PMID:[Effect of decane-1,10-bis[acetoxy-(N, N)-dimethyl-(N)-(diphenylmethoxy-2-ethyl) ammonium] dichloride on metabolism in white rats]. 651 57

The mammalian lens contains an unusually high concentration of glutathione (GSH), the highest level being in the epithelium. GSH is present largely in the reduced state. The high concentration of GSH in a normal lens and the decreased concentration in most types of cataracts have led to many hypotheses on its role in cataract formation. These hypotheses are considered in the light of current evidence. GSH is synthesized and degraded in the lens. Both processes require ATP, derived largely from glycolysis. Carbohydrate metabolism is also involved in the maintenance of GSH in the reduced state. There is a direct link between the rate of formation of oxidized glutathione (GSSG) and the stimulation of the hexose monophosphate shunt through the generation of NADPH. One possible function of GSH in the lens is to maintain the thiol (SH) groups of proteins in the reduced state, thus preventing formation of high molecular weight (HMW) protein aggregates. The formation of HMW proteins in X-ray-induced cataracts through disulphide bond formation and the involvement of SH oxidation in HMW proteins isolated from human cataractous lenses suggest a role for GSH in protecting protein SH groups. GSH in the lens may also protect critical SH groups involved in regulating cation transport and permeability. Studies with mammalian lenses indicate that lowering the lens GSH concentration leads to increased permeability to cations and inactivation of Na+,K+-ATPase. A consequence of the changes in ion distribution is the inhibition of protein synthesis, which may explain the cessation of growth in cataractous lenses. GSH may also protect against oxidative damage to the lens. GSH metabolism is intimately involved in detoxification of H2O2, normally present in the aqueous humour. Lenses with impaired shunt activity or inhibited glutathione reductase are more susceptible to oxidative damage by peroxide. This may contribute to the formation of cataract.
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PMID:Metabolism and function of glutathione in the lens. 656 81

The activities of 13 liver and 6 brain enzymes were studied in 7-12 week old CD2F1 male mice that had been fed ad libitum and standardized either to 12 hours of light (0600-1800) alternating with 12 hours of darkness (1800-0600) (LD12:12); or to a reversed light-dark cycle (darkness 0600-1800; light 1800-0600) (DL12:12). Three separate studies were performed on two different days; in each experiment, subgroups of 14 animals were sacrificed at 3-hour intervals. Livers were assayed for: isocitrate dehydrogenase, glutamate dehydrogenase, lactate dehydrogenase, alcohol dehydrogenase, glutathione reductase, glyoxylate reductase, L-alanine aminotransferase, glutamate oxalacetate transaminase, pyruvate decarboxylase, fructose-1-phosphate aldolase, fructose diphosphate aldolase, fructose 1,6-diphosphatase, and fatty acid synthetase. Brains were assayed for phosphoglucose isomerase, adenosine triphosphatase, creatine phosphokinase, pyruvate kinase, adenylate kinase, and malate dehydrogenase. All 19 enzymes demonstrated a prominent circadian rhythm in at least one experiment. Moreover, each rhythmic variable showed a statistically significant fit to a 24-hour cosine (sine) curve by the method of least squares. In general, peak activities of the liver enzymes analyzed were associated with the beginning of the dark cycle and initiation of the animal's activity, while the group of brain enzymes had peak activities which occurred at the beginning of the animals' rest span and were near the beginning of the light cycle. The phasing of each of the rhythms could be reversed within a two-week span after reversing the environmental light-dark cycle 180 degrees.
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PMID:Circadian organization of thirteen liver and six brain enzymes of the mouse. 731 49

Non-therapeutic toxic dose (250 mg/kg) of acetaminophen (paracetamol), in vivo to albino rats significantly decreased red cell reduced glutathione (GSH) content and activity of (Na+, K+)-ATPase enzyme, whereas osmotic fragility (O.F.) was increased. However, no change was observed in the activity of glutathione reductase (GR) after acetaminophen treatment, while acetaminophen plus vitamin E treated rats showed significant increase in GR activity. Supplementation of vitamin E to the drug treated rats effectively brought the GSH content, (Na+, K+)-ATPase activity and O.F. back to almost normal. The results suggest that acetaminophen toxic dose treatment induces metabolic and membranal alterations making red cells prone to hemolysis, while vitamin E which is an antioxidant shows its ameliorating role to these changes.
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PMID:In vivo effects of acetaminophen on rat RBC and role of vitamin E. 755 83

The cytotoxicity of the disulfide n-butyl 2-imidazolyl disulfide (III-2) was determined to be the result of a disruption in the cellular redox state and inhibition of critical membrane enzymes. These events cause perturbations in Ca2+ homeostasis, which may affect the cell signalling machinery and cause the activation of catabolic enzymes. Exposure of EMT6 cells to III-2 resulted in depletion of nonprotein and protein thiols. Under hypoxic conditions, the depletion of reduced glutathione was less than that measured when cells were treated in air, whereas following an exposure to 500 microM III-2 for 2 h the enzymes glutathione S-transferase and glutathione reductase were inhibited to a greater extent under hypoxia. Ca2+ homeostasis was disrupted with an initial shift from the mitochondrial to the cytoplasmic pool. The inhibition of plasma membrane Ca(2+)-ATPase resulted in accumulation of Ca2+ in the cytoplasm. At higher concentrations, further disruption was seen as a net loss of Ca2+ of the cytoplasmic excess with no change in the mitochondrial levels, resulting in lower total cellular Ca2+. Neither the inhibition of Ca(2+)-ATPase nor the disruption of Ca2+ homeostasis were different under hypoxic vs. oxic conditions. Due to these observations, HL60 cells were used to measure whether III-2 stimulated apoptosis. Morphologic changes and DNA laddering were observed following exposure to the disulfide, with lower concentrations required to stimulate the cellular changes under hypoxia. These events may be the result of the disruption in Ca2+ homeostasis due to thiolation or alteration in redox status of the cells.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Disulfide cytotoxicity under hypoxia. 762 Feb 24

Cationic antiseptics--catamine AB, polysept (polymeric derivative of chlorhexidine) as well as cationic protein protamine exhibited a pronounced cytotoxic effect on human skin and lung fibroblasts in cell culture. Their effect was accompanied by augmentation of lipid peroxidation products and by inhibition of DT-diaphorase, LDH, ATPase and glutathione reductase. Introduction of alpha-tocopherol into the cultural medium normalized the rate of lipid peroxidation but did not remove the inhibitory effect on activity of oxidoreductase studied. Blood serum proteins immunoglobulins and albumin diminished significantly the cytotoxic effect of cationic preparations contributing to restoration of all the parameters studied to control values; this phenomenon appears to occur due to nonspecific membrane protective and antioxidation effects of the blood serum proteins.
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PMID:[Some biochemical indicators of the cytotoxic response of human fibroblasts cultured with natural and synthetic polycations]. 779 94

This study was designed to assess Cyclosporin A (CsA) nephrotoxicity in the rabbit-possibly a more sensitive species than the rat-and to explore the mechanism of this toxicity with special attention to glutathione metabolism disturbances and cytochrome P-450 level in the kidney. CsA given for three days at a daily dose of 50 mg/kg (s.c.) induced nephrotoxicity as assessed by histological abnormalities and by a significant increase in blood urea nitrogen and urinary enzyme activities: N-acetyl-beta-D-glucosaminidase and L-gamma-glutamyl-transferase. This observed renal injury was of the same order as that obtained in the rat. In addition, there was a significant increase in oxidized glutathione content (40%) while reduced glutathione level remained unchanged. Concurrently, there was a significant decrease in renal cortex glutathione reductase (49%) and to a lesser extent in glutathione peroxidase activities (16%) whereas that of glutathione-S-transferase was not modified. A significant increase in renal cortex cytochrome P-450 (3-fold versus controls) was also observed. The mechanism of CsA nephrotoxicity is to be related to a cytochrome P-450 induction. This event could induce the observed impairments in renal glutathione metabolism and Na+K(+)-ATPase activity, via a possible increase in eicosanoid metabolism.
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PMID:Effects of cyclosporin on kidney glutathione metabolism and cytochrome P-450 in the rabbit: possible implication of eicosanoid metabolism. 782 Dec 32

1. Endosulfan insecticide is a polychlorinated compound used for controlling a variety of insects; it is practically water-insoluble, but readily adheres to clay particles and persists in soil and water for several years. Its mode of action involves repetitive nerve-discharges positively correlated to increase in temperature. This compound is extremely toxic to most fish and can cause massive mortalities. In fish, it causes marked changes in Na and K concentrations, decrease in blood Ca(2+) and Mg levels and inhibits Na, K and Mg-dependent ATPase (in brain). 2. Bioaccumulation of endosulfan is reported for marine animals; however, freshwater animals (e.g., crayfish) accumulate it to some extent, but they lose the compound rapidly during depuration. Endosulfan is generally less toxic to aquatic invertebrates than fish. However, it causes decreases in adenylate energy charge, oxygen consumption, hemolymph amino acids, succinate dehydrogenase, heart-beat (mussel) and altered osmoregulation. 3. Generally, mammals are less susceptible to endosulfan's toxicity than aquatic animals. The majority of studies conducted on laboratory mammals can be summarized. (a) Neurotoxicity: male rats are more sensitive than females to endosulfan, which decreases brain and plasma acetylcholinesterase activity. Endosulfan I (a metabolite) causes a significant change in norepinephrine, 5-HT and GABA. (b) Renal toxicity: inhibition of MFOs activity was noticed in rats; other effects included changes in proximal convoluted tubules and necrosis of the tubular epithelium. (c) Hepatotoxicity: chemically-induced aminopyrine N-demethylase and aniline hydrolase were found in rat liver, and reduction in the glycogen level occurred. (d) Hematologic toxicity: endosulfan exposure resulted in a significant decrease in the level occurred. (d) Hematologic toxicity: endosulfan exposure resulted in a significant decrease in the erythrocyte glutathione reductase, hemoglobin amount, RBC number and mean corpuscular volume. 4. Respiratory toxicity: involved dyspnea, acute emphysema, cyanosis and hemorrhages in teh interalveolar portions of rat's lungs. 5. Biochemical: in rats, endosulfan caused increased glucose-6-phosphate dehydrogenase activity, blood glucose level, phospholipid contents of the microsomal and surfactant system, and profoundly induced the activity of alcohol dehydrogenase and cytosolic glutathione S-transferases. It also decreased significantly Na+, K+ and Mg(2+) ATPases, plasma calcium level and alkaline phosphatase in the intestinal epithelium. 6. Immunologic toxicity: rat serum antibody titer to tetanus toxin, IgG, IgM and gammaglobulins were significantly reduced. 7. Reproductive toxicity: degenerative changes in the seminiferous epithelium, induction of the rate-limiting enzyme in testosterone production (3beta-hydroxysteroid transferase and 17 beta-hydroxysteroid transferase), histological changes in reproductive organs, testicular atrophy and the occurrence of ovarian cysts were noticed in rat. Reduction in the weight of secondary sex organ was also observed.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Bioaccumulative potential and toxicity of endosulfan insecticide to non-target animals. 790 Sep 59

Red cell metabolism (RCM) was examined in 63 patients with severe and complicated meningococcal infection and purulent meningitis of another etiology. There were complex pathobiochemical shifts with changes in glycolysis (in activity of lactate dehydrogenase, piruvatkinase, in the amount of piruvate, lactate and 2,3-DPG), antioxidant status (in the activity of glucose-6-phosphate-dehydrogenase, glutathione reductase), Mg+2, Na+, K(+)-dependent ATPase. Primary depression of red cell metabolism changed for compensatory activation for hypoxia adaptation in clinical improvement. RCM disturbance coincided with emergence of early complications and reached maximum in lethal outcome. Pathogenetic and clinical implications of RCM in meningococcal infection and purulent meningitis are described.
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PMID:[The enzyme activity and pyruvate, lactate and 2,3-DPG levels in the erythrocytes of patients with severe forms of meningococcal infection and suppurative meningitis]. 877 62

The aim of this study was to better characterize rabbit proximal kidney tubule cells cultured on collagen IV-coated porous inserts, as compared to the same cells seeded in standard plastic wells. Total protein contents in confluent monolayers on permeable membranes were about twofold higher than those measured in confluent cultures in plastic wells. Microscopy examinations suggested that such a difference was probably due to a higher cell density and to an impressive development of the apical brush-border membrane. Moreover, measurement of unidirectional transport of p-aminohippuric acid and tetraethylammonium bromide confirmed the high polarization level of cultures on porous inserts. Results of methyl(alpha-D-[U-14C]glyco)pyranoside uptake suggested that cell phenotype was probably influenced by culture conditions. Analysis of different markers as a function of time in culture showed decreases of alkaline phosphatase (AP), gamma-glutamyltranspeptidase (GGT), and Na(+)-K(+)-ATPase activities as well as increases in LDH, ATP, and glutathione levels, similar to those formerly reported for cells cultured in standard plastic plates. However, comparative data from 6-d-old monolayers have shown that AP, GGT, Na(+)-K(+)-ATPase, glutathione reductase (GRED), and selenium-dependent glutathione peroxidase (Se-GPX) activities were 2.8-, 2.6-, 1.6-, 1.2-, and 2.1-fold, respectively, better preserved on precoated permeable membranes. On the other hand, this paper reports for the first time in the literature that GRED and SE-GPX, two phase II detoxification enzymes, were well maintained in cultures of rabbit proximal kidney tubule cells. Our results show that culturing rabbit proximal kidney tubule cells on collagen IV-coated porous membranes was accompanied by an improvement of both morphological and biochemical properties of the cells.
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PMID:Morphological and biochemical characterization of primary culture of rabbit proximal kidney tubule cells grown on collagen-IV coated Millicell-CM. 935 85


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