Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.3.5.1 (succinate dehydrogenase)
 8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A correlated morphological and cytochemical approach was employed to study frog hepatocytes in different periods of their annual cycle, including the natural hibernating period. There were considerable changes in the distribution and organization of hepatic glycogen in different phases of the annual cycle, and distribution of organelles as well. The most striking findings were glycogen storage during the prehibernation and hibernation phases, followed by drastic glycogen depletion. Cytochemical staining of a number of enzymes (succinate dehydrogenase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, paranitrophenyl phosphatase, acid phosphatase, and glucose-6-phosphatase) involved in a variety of metabolic pathways, showed various cytoplasmic localizations and differences in intensity of the reaction products as a function of seasonality. Morphological and cytochemical data were interpreted as evidencing different functional requirements during seasonal changes in the frog.
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PMID:Frog hepatocyte modifications induced by seasonal variations: a morphological and cytochemical study. 156 23

Neutrophil myeloperoxidase, hydrogen peroxide, and chloride constitute a potent antimicrobial system with multiple effects on microbial cytoplasmic membranes. Among these is inhibition of succinate-dependent respiration mediated, principally, through inactivation of succinate dehydrogenase. Succinate-dependent respiration is inhibited at rates that correlate with loss of microbial viability, suggesting that loss of respiration might contribute to the microbicidal event. Because respiration in Escherichia coli can be mediated by dehydrogenases other than succinate dehydrogenase, the effects of the myeloperoxidase system on other membrane dehydrogenases were evaluated by histochemical activity stains of electrophoretically separated membrane proteins. Two bands of succinate dehydrogenase activity proved the most susceptible to inactivation with complete loss of staining activity within 20 min, under the conditions employed. A group with intermediate susceptibility, consisting of lactate, malate, glycerol-3-phosphate, and dihydroorotate dehydrogenases as well as three bands of glucose-6-phosphate dehydrogenase, was almost completely inactivated within 30 min. The relatively resistant group, including the dehydrogenases for glutamate, NADH, and NADPH and the remaining bands of glucose-6-phosphate dehydrogenase, retained substantial amounts of diaphorase activity for up to 60 min of incubation with the myeloperoxidase system. The differential effects of myeloperoxidase on dehydrogenase inactivation could not be correlated with published enzyme contents of flavin or iron-sulfur centers, potential targets of myeloperoxidase-derived oxidants. Despite the relative resistance of NADH dehydrogenase/diaphorase activity to myeloperoxidase-mediated inactivation, electron transport particles prepared from E. coli incubated for 20 min with the myeloperoxidase system lost 55% of their NADH oxidase activity.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Differential inactivation of Escherichia coli membrane dehydrogenases by a myeloperoxidase-mediated antimicrobial system. 169 36

An optimal and practical method for high resolution separation and visualization of soluble and membrane-binding isoenzymes is described. By use of this method, non-specific esterase, lactate dehydrogenase and acid phosphatase from different tissues of mice can be separated into more than 50, 30 and 20 components, respectively. Cholinesterase, glucose-6-phosphate dehydrogenase, acid phosphatase, succinate dehydrogenase, lactate dehydrogenase and non-specific esterase isolated from the lumbar spinal cord of chick embryos at different ages can be separated into about 15, 12, 9, 6, 14 and 20 components, respectively. In addition, an attempt has been made to evaluate quantitatively by densitometry differences in enzyme activity among different regions of the same tissue (e.g. spinal cord). The findings revealed that there are differences in isoenzyme components between the dorsal and ventral regions of the spinal cord. Collectively, the combination of direct tissue isoelectric focusing and fast enzyme visualization reveals a greater number of isoenzyme components than can be demonstrated by other means. This method is an extremely useful procedure for understanding and analyzing the nature and topographic localization of isoenzyme components.
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PMID:Histo-electrophoretic analysis of the microheterogeneity and region-specificity of isozymes. 175 87

A study was made of the role of prolactin (PRL) in the regulation of thyroid function in intact animals and in those exposed to stress (swimming was used as physical exercise). A single daily dose of 125 micrograms of PRL per 100 g of body mass was injected subcutaneously in 0.5 ml of saline solution during a week to male rats (control: intact rats; injection of 0.5 ml of saline solution subcutaneously). Redox enzymes; succinate dehydrogenase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, NAD.H2 and NADP.H2, ATPase and monoamine oxidase, total protein, RNA and glycogen in glandular cells were investigated histochemically 24 h after the last injection of PRL or saline, 30 min., 1, 2, 3, 5 and 7 hours after swimming or right after complete fatigue (in the presence of experimental hyperprolactinemia). A conclusion has been made that one of the most important mechanisms of the adaptive effect of PRL is its ability to suppress thyroid function, thus decreasing the metabolism level, which results in reduction of oxygen consumption and improves body tolerance to stress.
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PMID:[Metabolism of thyroid gland cells as affected by prolactin and emotional-physical stress]. 178 Feb 95

Approximately in 80% of cow oocytes (n = 632) ended cytoplasmatic and nucleus maturation to the state of metaphase II in the conditions of 24 hours in vitro cultivation. In 300 oocytes cytochemically we have determined the activity of enzymes--the succinate dehydrogenase (SDH, EC 1.3.99.1.), alpha-glycerophosphate dehydrogenase (GPDH, EC 1.1.1.8.) and glucose-6-phosphate dehydrogenase (G6PDH, EC 1.1.1.49.). The reaction intensity of the observed dehydrogenases increased in cow oocytes which were cultivated in vitro for 24 hours. Dehydrogenases are located in the mitochondria which are laid out regularly in the cytoplasm of oocytes. Part of oocytes showed polarization in the lay out of reaction and part of oocytes gave extramitochondrial reaction.
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PMID:[Cytoplasmic maturation of cow oocytes cultured in vitro and their dehydrogenase activity]. 178 95

A study is performed on the long-term effect of the chloracetanilide herbicide "Acetochlor" in doses 21.0; 10.6: 5.5 and 2.6 mg/kg-1 in conditions of 6-month oral application and 2-month rehabilitation period on the metabolite processes and the balance of the connective-tissue components in the myocardium and aorta of male white rats. A complex of biochemical and histological methods are performed (activity of succinate dehidrogenase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, adenosin triphosphatase, cytochrome oxidase, fructoso-1,6-diphosphatase, level of the thiol groups, soluble globular, elastine, collagen fractions, insoluble collagen and elastine, general and sulphated glucosamino glycanes). The dose 21.0 mg/kg-1 leads to blocking of the thyol groups, inactivation of succinate dehydrogenase, cytochrome oxidase, adenosin triphosphatase, fructose-1,6-diphosphatase, glucose-6-phosphate dehydrogenase, activation of lactate dehydrogenase, decrease of the soluble globular, elastine, and collagen fractions and increase of the glucoseaminoglycanes in the heart muscle and aorta. The changes established in the heart muscle at 10,6 mg/kg-1 certify for stronger sensitivity of the organ of the aorta wall. The presence of single changes in the examined indices, their complete dying out after the rehabilitation period and absence of structural changes in the myocardium and aorta permit the dose of 5.5 mg/kg-1 to be accepted as not effective in the conditions of chronic experiment concerning the cardiovascular system.
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PMID:[The effect of the acetanilide herbicide Acetochlor on the cardiovascular system of white rats]. 179 94

Alpha-glycerophosphate dehydrogenase (alpha-GPD) and succinate dehydrogenase (SD) activities were investigated in lymphocytes from peripheral blood of normal rats and rats bearing the Walker 256 carcinosarcoma. Computer analysis using an original algorithm revealed a hierarchy of biorhythmic patterns of dehydrogenase activities. In all rats, mean SD activity was higher than mean alpha-GPD activity. In rats without tumor, SD and alpha-GPD activities were both higher than in rats with the Walker tumor. Biorhythm spectra for both dehydrogenases were very similar in rats with or without tumor, but tumor implantation resulted in a change of the phase relationship between alpha-GPD and SD.
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PMID:Chronobiological analysis of peripheral lymphocyte dehydrogenase activities in rats with Walker 256 carcinosarcoma. 180 27

Enzyme histochemical profiles of spinal motoneurons in the zebrafish were determined. Five enzymes of glucose metabolism were chosen: glucose-6-phosphate dehydrogenase (G6PDH), hexokinase (HK), phosphofructokinase (PFK), succinate dehydrogenase (SDH) and NADH tetrazolium reductase (NADH-TR). Motoneurons were traced with Fluorogold and classified as those that innervate white muscle fibres (W-MNs) and those that innervate red and intermediate muscle fibres (R/I-MNs). The average enzyme activities per volume of tissue in the somata of both populations differed at most by 25%. Both the average soma volume and the average number of muscle fibres innervated are three times larger for the W-MNs than for the R/I-MNs. This suggests that the total amount of enzyme activity within a neuron soma matches target size. In the R/I-MNs, the activities of SDH and NADH-TR were closely correlated (correlation coefficient, r = 0.99; p less than 0.05) and HK activity correlated well with G6PDH activity (r = 0.94; p less than 0.05), but not with PFK (r = 0.64; p greater than 0.05). In the W-MNs, there was no correlation between SDH and NADH-TR (r = -0.59; p greater than 0.05) or between HK and G6PDH (r = 0.50; p greater than 0.05) and the correlation coefficient between HK and PFK activity was close to zero (r = 0.04; p greater than 0.05). It was concluded that in the R/I-MNs, which are continuously active, firing activity is fuelled by oxidative metabolism. We suggest that in the W-MNs glucose is stored in the form of glycogen and that, despite high levels of NADH-TR present, the energy for intermittent firing activity is provided by glycolysis.
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PMID:Histochemical profiles of motoneurons innervating muscle fibres with different activity patterns in the zebrafish, Brachydanio rerio. 183 17

The metabolic functions of endothelial cells of the rabbit cornea in different storage conditions were studied using quantitative cytochemistry. The corneas were stored for 2 h, and 1, 3, 7, 14 and 21 days in dexol at 4 degrees C and in culture medium at 37 degrees C. It was shown that glycolysis as expressed by the activity of the cytosolic enzymes glyceraldehyde 3-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase and lactic dehydrogenase is well preserved for 1 week in dexol and for 3 days only in the culture medium. Mitochondrial enzymes as shown by succinate dehydrogenase and fatty acid oxidation activity show a similar pattern. Uridine diphosphoglucose dehydrogenase, which plays an important part in proteoglycan synthesis, is markedly decreased in both media, but retains its activity in dexol for a slightly longer time. Keratan and chondroitin sulfate content show a sharp drop in the culture medium at 37 degrees C as compared to dexol. This study demonstrates the superiority of dexol at 4 degrees C over the culture medium at 37 degrees C. Quantitative cytochemistry is a useful tool for studying the metabolism of endothelial cells.
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PMID:Endothelial cells of rabbit cornea in different storage conditions. A quantitative cytochemical study. 187 Aug 47

Dietary products of lipid peroxidation cause hepatic dysfunctions such as reductions in activities of aldehyde dehydrogenase (mitochondrial NAD-dependent), succinate dehydrogenase, phosphoglucomutase, glucokinase, and glucose-6-phosphate dehydrogenase, and a depletion of coenzyme A. Toxic products in the peroxidation are considered to be the aldehydes among the decomposed products from hydroperoxides, because the decomposed products were incorporated into the liver but the other products were not when they were administered orally to rats. There are three current ideas on the causes of the dysfunctions: (a) direct attack of the incorporated aldehydes on the enzymes, (b) injury of the bio-membranes by the aldehydes, and (c) disturbance of the synthetic system for enzymes. In this study, to examine these ideas, a reasonable concentration of the peroxidation products to use in vitro was estimated from the amounts present in the liver after an oral dose of lipid peroxidation products. With respect to idea (a), when the peroxidation products were added to subcellular fractions of hepatocytes, the decomposed products specifically inactivated aldehyde dehydrogenase and glucose-6-phosphate dehydrogenase, and destroyed coenzyme A. For ideas (b) and (c), in which the parenchymal hepatocytes isolated from rat were used, the decomposed products did not seem to injure the bio-membrane, but they inhibited induction of glucokinase by hormones in the hepatocytes. It was concluded that in the hepatic dysfunction caused by the dietary products of lipid peroxidation the incorporated decomposed products in the liver directly inactivated the mitochondrial NAD-dependent aldehyde dehydrogenase and glucose-6-phosphate dehydrogenase, destroyed coenzyme A, and disturbed the synthetic system of glucokinase.
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PMID:Hepatic dysfunction caused by dietary products of lipid peroxidation. 195 95


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