Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0392674 (exhaustion)
 13,658 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phenothiazines are used as antipsychotic drugs and as reagents to determine microamounts of hemoglobin in biological fluids and tissues. Several agents cause the oxidation of phenothiazines to chromophoric cation radicals, whose stability may be related with their biological action. Enzymes and proteins with peroxidase activity catalyze the oxidation by H2O2 of phenothiazines to their corresponding cation radicals, which suffer a nonenzymatic breakdown. The instability of these cation radicals makes the determination of their respective molar absorptivities very difficult. These properties, however, have been determined for a few phenothiazine cation radicals by cumbersome or unreliable procedures. In this paper a new method is proposed and applied to six different phenothiazines oxidized with H2O2/peroxidase. The method involves the stoichiometric exhaustion of H2O2, under assay conditions which yield a fast enzymatic formation of phenothiazine cation radicals and which slow down their nonenzymatic breakdown. This method may be useful for quantitative studies on the enzymatic activity and the reaction mechanism of the oxidation of a number of phenothiazines catalyzed by different types of peroxidase, as well as by proteins with peroxidase activity, such as hemoglobin.
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PMID:Determination of the molar absorptivities of phenothiazine cation radicals generated by oxidation with hydrogen peroxide/peroxidase. 151 48

The changes in the glutathione-dependent and superoxide dismutase (SOD) enzymatic activity in the rat lungs and liver tissues have been studied after the administration of plague murine toxin (LD100). It has been found out the early toxic effect in 1h in the lungs: 35% SOD and glutathione peroxidase (tributyl hydroperoxide) (GP) decrease, 87% glutathione reductase (GR) increase along with two-hold ascent of ratio GR/Glutathione-S-transferase (GT), GR/GPs. The fundamental ratio GR/GT.GPs rises in 1h 3.7 times and then falls below standard rate (5h). This is the evidence of the lungs antioxidant system potential power exhaustion. It has been established that in the liver, 4 times SOD activity increases in 2h after the toxin injection, and 1.5 times GP (tributyL) hydroperoxide) activity ascends in 1h. The ratio increase (150% for SOD/GP-H2O2 in 2h, 114% for GR/GP (tributyl hydroperoxide) and 61% for GR/GT in 5h) indicates the stable unbalance of this system. The pathogenetic significance of detoxication system disturbances in the lungs and liver tissues under the murine toxin influence is discussed.
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PMID:[Glutathione and superoxide dismutase redox system in the development of toxic-infectious shock caused by Yersinia pestis toxin]. 233 51

Myxoedematous endemic cretinism is prevalent in African goitre endemies. It has been related to a thyroid 'exhaustion' atrophy occurring near birth. It is proposed that this might result from the low resistance of a fragile tissue to enhanced H2O2 generation under intense thyroid stimulation by thyrotropin. In support of this hypothesis, low selenium and glutathione peroxidase serum levels have been found in the African endemic area of the Idjwi Island (Kivu, Zaire). Serum selenium and plasma glutathione peroxidase were lower in the area of high endemicity of goitre and cretinism (Northern part of the Island). However, only the former difference is statistically significant. These data thus suggest a role of oligoelements and oxygen toxicity in the pathogenesis of endemic cretinism.
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PMID:Selenium deficiency as a possible factor in the pathogenesis of myxoedematous endemic cretinism. 357 81

Rat aortic rings stop producing prostacyclin upon prolonged washing in buffer. This 'exhaustion' is caused by inhibition of cyclo-oxygenase, since these rings still convert cyclic endoperoxides but not arachidonic acid into prostacyclin, and most probably is due to high concentrations of peroxides: it can be accelerated by H2O2 or by interrupting the glutathione cycle, while it is delayed by reduced glutathione. Incubation of exhausted rings in human plasma or in a plasma filtrate restores to some extent prostacyclin formation. This filtrate, in particular from uraemic subjects, also inhibits the H2O2 initiated oxidation of guaiacol by ram seminal vesicle microsomes or horseradish peroxidase. The prostacyclin regulating plasma factor has been partially purified and identified as a stable and very polar molecule of mol. wt. 300-400, able to reactivate prostacyclin generation by exhausted rings. We suggest that one or more low mol. wt. plasma components prolong vascular prostacyclin formation by acting as reducing cofactor for cyclo-oxygenase peroxidase. The main physiological role of this plasma activity is probably to protect the vascular prostacyclin forming system from exhaustion during persistent irritation.
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PMID:Partial isolation and function of the prostacyclin regulating plasma factor. 393 Jan 27

The dithionite ion is catalytically disproportionated by lactoperoxidase with Km = 0.36 mM in 100 mM glycine HCl pH 3.0. The products formed are thiosulfate and hydrogensulfite ions. The rate of reaction is considerably increased at low pH with a pKa at 3-3.5 possibly indicating the involvement of a carboxyl group. The reaction is competitively inhibited by hydrogensulfite, Ki = 5.5 mM in 100 mM glycine HCl pH 3.50. Four different spectral forms of reduced lactoperoxidase appear during the reaction. The first two forms are found during the lag phase of the reaction. The third form, which is interpreted as a ternary complex, exists under the dismutation phase. After exhaustion of the substrate a visible spectrum similar to that of lactoperoxidase H2O2 compound III appears. A mechanistic model for the lactoperoxidase dismutation of the dithionite ion is proposed and discussed.
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PMID:Lactoperoxidase, a dithionite ion dismutase. 674 74

Oxygen release accompanying oxidation of vanadyl by diperoxovanadate was suppressed on addition of NADH. The added NADH was rapidly oxidized, oxygen in the medium was consumed, and the reaction terminated on exhaustion of either NADH or vanadyl. The consumption of oxygen and disappearance of NADH needed small concentrations of diperoxovanadate to initiate and increased with increase in the concentration of vanadyl and NADH or decrease of pH. The products of the reaction were found to be NAD+ from NADH and vanadate oligomers from vanadyl and oxygen. The reaction was insensitive to catalase and was not dependent on H2O2. The reaction was inhibited by superoxide dismutase, cytochrome c, EDTA, Mn2+, histidine, and DMPO, but not by hydroxyl radical scavengers such as ethanol and benzoate. The ESR spectrum of the reaction mixture showed the presence of the 1:2:2:1 quartet signal typical of a DMPO-OH adduct, but this was not modified by ethanol. This oxygen radical species, possibly of .OV type derived from diperoxovanadate, is proposed to have a role in the reactions of oxygen release and NADH oxidation.
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PMID:Requirement of a diperoxovanadate-derived intermediate for the interdependent oxidation of vanadyl and NADH. 784 Jun 32

Addition of NADH decreased the oxygen release that accompanied oxidation of vanadyl by H2O2. The added NADH was oxidized rapidly and oxygen was consumed with a stoichiometry of 1:1 for NADH/O2. Small concentrations of H2O2 were sufficient to trigger this oxygen-consuming NADH oxidation which terminated on exhaustion of either NADH or vanadyl. The oxidation of NADH increased proportionately with concentration of NADH and vanadyl. The oxidation products of vanadyl were found to be a mixture of vanadate oligomers and peroxovanadates. The reaction was sensitive to catalase, SOD, histidine and EDTA. Using ESR spectroscopy with DMPO as the spin trap, an adduct corresponding to DMPO-OH was detected in these phosphate-buffered reaction mixtures. Participation of hydroxyl radicals in NADH oxidation, however, seems doubtful because even high concentrations of ethanol, methanol, mannitol, formate and benzoate, known to scavenge these radicals, did not block the reaction. The results indicate that peroxovanadate intermediates formed during vanadyl oxidation by H2O2 play a key role in the oxidation of NADH.
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PMID:NADH oxidation is stimulated by an intermediate formed during vanadyl-H2O2 interaction. 794 44

The purpose of this study was to determine whether contractile activity associated with running exercise was a prerequisite for neutrophil infiltration into rat tissues. H2O2-dependent myeloperoxidase (MPO) activity for rat (n = 8) liver, heart, and gastrocnemius muscles was assayed after 58 +/- 11 min of running to voluntary exhaustion (25 m/min; 0% grade). MPO activity values measured with 0.6 mM H2O2 were 0.988 +/- 0.331 (SD) U/g (skeletal muscle), 1.563 +/- 0.303 U/g (heart), and 1.652 +/- 0.510 U/g (liver) for control samples, compared with 1.690 +/- 0.321, 3.128 +/- 1.221, and 2.752 +/- 0.437 U/g, respectively, for the exercise group (P < or = 0.05). Kinetic analysis revealed that maximum velocity for all tissues increased as a result of the exercise (P < 0.05). The Michaelis constant (Km) values at rest for all tissues were similar (range 0.53-0.57 mM H2O2; P > or = 0.05). Exercise did not alter the Km values for cardiac and liver samples; however, for skeletal muscle, the Km was 28% lower than control (P < or = 0.05). The results of this study show that, with prolonged running, MPO activity is elevated in most rat tissues and not exclusively in skeletal muscle. Moreover, the metabolic status of the tissues may be an important factor for neutrophil infiltration with exercise and not exclusively the type of muscle contraction, as previously hypothesized.
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PMID:Heart, liver, and skeletal muscle myeloperoxidase activity during exercise. 892 63

The resistance to divalent metal ions, antibiotics and H2O2 was investigated in Yersinia kristensenii strains 13, 15, 18 by performing subcultivations with CdSO4 (20 and 100 mg/L) in nutrient agar (NA) and M9 medium with thiamine. Metal resistance of all three strains in NA was the same and decreased in the following sequence: Ni > Zn = Co > Cd. The chloramphenicol (Cmp) resistance ranged between 32 and 256 mg/L and the H2O2 sensitivity was very low or even zero. In the presence of thiamine the metal resistance sequence changed to Zn = Cd > Ni, Co, Ni and Co tolerance being 10-20 mg/L. Cmp resistance of all strains increased to 256 mg/L and H2O2 sensitivity also rose. In Cd-treated cultures, the ratio of glucose to thiamine in culture medium affected Cd resistance. At normal content of glucose and thiamine (5 g/L and 5 mg/L), Cd resistance markedly decreased coincident with thiamine exhaustion in these slowly-growing cultures. The Cmp resistance decreased to 16 mg/L, Ni and Co intolerance and H2O2 hypersensitivity appeared. At lowered glucose or thiamine levels (5 g/L and 2.5 mg/L or 2.5 g/L and 5 mg/L) a marginal decrease of Cd resistance took place in response to limited glucose uptake. Low thiamine or low-glucose cultures were resistant to H2O2, and exhibited a small decrease in Cmp resistance and a low Ni, Co tolerance. The adaptation of strain 15 to Cd induced only a small decrease of Cd resistance. Lowered glucose-to-thiamine ratio in culture medium probably induced in Cd-treated cultures a response triggering Cd resistance.
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PMID:The role of thiamine in Yersinia kristensenii resistance to antibiotics and heavy metals. 943 58

The anti-lipoperoxidation of grape seed extracts (GSE) was observed by malondialdehyde (MDA) generated in liver and brain homogeneates spontaneously or induced by CCl4, H2O2, Fe(2+)-ascorbic acid. The exhaustion of glutathione (GSH) in liver homogenate initiated by Fe(2+)-ascorbic acid was also tested. Results showed that GSE significantly inhibited the generation of MDA in rat liver and brain homogenates both spontaneously formed or induced by CCl4, H2O2 and Fe(2+)-ascorbic acid with dose-effect relationships. GSE could also reduce the exhaustion of GSH levels in mice liver. The study indicated that GSE is effective on the inhibition of lipid peroxide and on the protection of liver from injury caused by lipid peroxidation.
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PMID:[Anti-lipoperoxidation of grape seed extracts in vitro]. 1256 67


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