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:1.3.5.1 (succinate dehydrogenase)
8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adult male Sprague-Dawley rats (> or = 180 days old) develop an obesity-exacerbated insulin resistance in contrast with female animals of the same strain. Given the fact the maintenance of muscle mass requires an adequate supply of insulin and active insulin receptors, we postulated that gender differences might exist in both protein content and metabolic properties of skeletal and cardiac muscle in adult Sprague-Dawley rats. Therefore, to test this hypothesis, we examined activities of bioenergetic enzymes and total protein content in the diaphragm, the heart and the plantaris muscle in 12-month-old male and female animals. Mean (+/- SD) body weights of male animals were significantly (P < 0.05) greater than female animals (598 +/- 8 vs. 362 +/- 19 g) and the diaphragm weight/body weight ratio was significantly lower in males compared to females (2.36 +/- 0.05 vs. 3.02 +/- 0.13 mg/g). The activities of isocitrate dehydrogenase (NADP-specific) and succinate dehydrogenase were significantly lower (P < 0.05) in male animals compared to females in both the crural and costal regions of the diaphragm, the heart, and the plantaris muscle. In contrast, no gender differences (P > 0.05) existed in lactate dehydrogenase activity in any of the muscles studied. Finally, muscle protein concentration was significantly higher in female animals when compared to males (P < 0.05) in all muscles studied except the heart. These data support the hypothesis that gender differences exist for adult Sprague-Dawley rats in general and specific protein content of the diaphragm, locomotor muscles, and the heart.
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PMID:Gender differences in diaphragmatic metabolic properties of the adult Sprague-Dawley rat. 797 31

NADP(+)-specific isocitrate dehydrogenase (ICDH-NADP: EC 1 x 1 x 1 x 42) is primarily a mitochondrial matrix enzyme in both mammalian skeletal muscle and heart and has markedly higher activity levels than the NAD(+)-specific isozyme. To date, it is unknown whether ICDH-NADP activity is inducible with in vivo exercise training in locomotor or respiratory skeletal muscle. Therefore, the purpose of this investigation was to quantify alterations in ICDH-NADP activity in respiratory muscles (costal and crural diaphragm) and locomotor muscles (medial gastrocnemius, plantaris and soleus) following 8 weeks of treadmill endurance training. Ten of the animals had been assigned randomly to an exercise group (TR) and had completed 8 weeks of progressive (5 days week-1: 45 min day-1) treadmill endurance training while the remaining 10 animals comprised a sedentary control (C). Mean ICDH-NADP activities in Tr were significantly higher (P < 0.05) when compared with C in the medial gastrocnemius (61.3%), plantaris (42.9%) soleus (21.4%). Mean costal diaphragm ICDH-NADP activity noted in trained animals when compared to the sedentary control group was not significantly higher (10.8% greater for TR; P = 0.14). No mean differences (P = 0.58) were noted in the crural diaphragm. The results indicate that ICDH-NADP is inducible with endurance training in locomotor skeletal muscle. A coefficient of determination of 0.624 (i.e. 62.4% of the variance could be explained) for ICDH-NADP was calculated, with the oxidative enzyme marker succinate dehydrogenase (P < 0.05) indicating a positive, moderate relationship.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Inducibility of NADP-specific isocitrate dehydrogenase with endurance training in skeletal muscle. 826 7

An enzymohistochemical and immunohistochemical study of the efferent ducts was performed in normal adult men. The epithelium consists of two types of columnar cells: principal cells (PCs) and ciliated cells (CCs), and is surrounded by a lamina propria (LP) with cells arranged circularly (LPCs). Enzymohistochemical study revealed more intense activity of succinic dehydrogenase, NADP, and ATPase in the CCs than in the PCs. The LPCs also showed an intense reaction for NADP and ATPase. Acid phosphatase activity was only intense in the apical cytoplasm of PCs. Immunohistochemical study revealed that antibodies to oestradiol receptor-related protein (ER-D5) immunostained the PCs and CCs intensely and the LPCs weakly. AE1/AE3 antibodies (which stain keratins nos. 1-8 and 14, 15 and 19) immunostained the PCs intensely, but was negative in both CCs and LPCs. Antibodies to keratin Ks.4.62 (which stain keratin no. 19) immunostained PCs and CCs but not LPCs. Epithelial membrane antigen antibodies (EMA) immunostained the adluminal surface and apical cytoplasm of PCs. Anti-vimentin antibodies immunostained the cytoplasm of PCs and CCs weakly as well as isolated cells in the LP. Antibodies to desmin immunostained most LPCs. Antibodies to collagen IV immunostained the basal lamina and many extracellular spaces in the LP, mainly around the LPCs. The differences between the enzymohistochemical and immunohistochemical patterns of the efferent ducts and those of the epididymis may help to explain functional differences along the epididymis.
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PMID:Enzymohistochemical and immunohistochemical study of the human efferent ducts. 827 25

Succinate dehydrogenase activity was measured in rat pancreatic islet homogenates incubated in the presence of [1,4-14C]succinate, the reaction velocity being judged through the generation of 14CO2 in the auxiliary reactions catalysed by pig heart fumarase and chicken liver NADP-malate dehydrogenase. In the presence of 1.0 mM succinate, the reaction velocity averaged 5.53 +/- 0.44 pmol min-1 microgram-1 islet protein. The Km for succinate was close to 0.4 mM and the enzymic activity was restricted to mitochondria. These kinetic results indicate that, under the present experimental conditions, the activity of succinate dehydrogenase does not vastly exceed that of either NAD-isocitrate dehydrogenase or the 2-ketoglutarate dehydrogenase complex, at least when the latter enzymes are activated by ADP and/or Ca2+. Nevertheless, the activity of succinate dehydrogenase is sufficient to account for the increase in O2 uptake evoked in intact islets by the monomethyl ester of succinic acid. It could become a rate-limiting step of the Krebs cycle in models of B-cell dysfunction.
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PMID:Hexose metabolism in pancreatic islets: succinate dehydrogenase activity in islet homogenates. 840 29

Immunophenotyping of lymphocytes by direct double-color immunofluorescence, investigation of metabolic activity of succinate dehydrogenase, alpha-glycerophosphate dehydrogenase, glucose-6-phosphate dehydrogenase, NAD- and NADP-diaphorases were performed in 77 tuberculous patients and 50 healthy donors. Activation of T-lymphocytes and their regulatory subpopulations is shown to depend on the extension of lung infiltration. At the same time, there were marked disorders in intracellular metabolism of peripheral blood lymphocytes. Close correlation exists between the activity of lymphocytic energy enzymes and the degree of expression on lymphocytes of receptors to interleukin-2, transferrin and HLA-DR-molecules. Cytochemical reactions for evaluation of blood lymphocyte energetic enzymes activity may be used in clinical practice for characterization of activation of T-lymphocytes and their regulatory subpopulations.
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PMID:[The activation processes of T-lymphocytes and their regulatory subpopulations in patients with pulmonary tuberculosis]. 890 85

The effect of various metabolic inhibitors on the rate of oxygen consumption by procyclic culture forms of Trypanosoma congolense utilizing proline as substrate was investigated. Cyanide inhibited the rate of oxygen consumption by 81.0 +/- 6.7%, malonate inhibited the rate by 51.6 +/- 1.6% and Antimycin A by 73.1 +/- 5.9%. A combination of cyanide and malonate inhibited the rate of oxygen consumption by 84.9 +/- 6.7% while a combination of antimycin A and malonate inhibited the rate by 81.6 +/- 7.6%. Rotenone had no effect on the rate of respiration except when the intact cells were first permeabilized by digitonin after which rotenone decreased the rate of respiration by 20-30%. Salicylhydroxamate (SHAM) did not have any effect on the rate of oxygen consumption. Enzymes involved in the catabolism of proline with high activities were: proline dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, fumarase, NADP-linked malic enzyme, alanine aminotransferase and malate dehydrogenase. Activities of 1-pyrroline-5 carboxylate dehydrogenase, glutamate dehydrogenase, aspartate aminotransferase and NAD-linked malic enzyme were detectable but lower. The end products of proline catabolism were alanine and glutamate. Unlike the case in Trypanosoma brucei brucei aspartate was not detected. Possible pathways of proline catabolism in procyclic culture forms of T. congolense and of electron transfer are proposed.
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PMID:Catabolism of proline by procyclic culture forms of Trypanosoma congolense. 1042 13

Studies of respiration on glucose in procyclic Trypanosoma congolense in the presence of rotenone, antimycin, cyanide, salicylhydroxamic acid and malonate have indicated the presence of NADH dehydrogenase, cytochrome b-c1, cytochrome aa3, trypanosome alternate oxidase and NADH fumarate reductase/succinate dehydrogenase pathway that contributes electrons to coenzyme Q of the respiratory chain. The rotenone sensitive NADH dehydrogenase, the trypanosome alternate oxidase, and cytochrome aa3 accounted for 24.5 +/- 6.5, 36.2 +/- 4.2 and 54.1 +/- 5.5% respectively of the total respiration. Activities of lactate dehydrogenase, NAD(+)-linked malic enzyme and pyruvate kinase were less than 6 nanomoles/min/mg protein suggesting that they play a minor role in energy metabolism of the parasite. Phosphoenolpyruvate carboxykinase, pyruvate dehydrogenase, succinate dehydrogenase, NADP(+)-linked malic enzyme, NADH fumarate reductase, malate dehydrogenase, and alpha-ketoglutarate dehydrogenase and glycerol kinase on the other hand had specific activities greater than 60 nanomoles/min/mg protein. These enzyme activities could account for the production of pyruvate, acetate, succinate and glycerol. The results further show that the amount of glycerol produced was 35-48% of the combined total of pyruvate, acetate and succinate produced. It is apparent that some of the glycerol 3-phosphate produced in glycolysis in the presence of salicylhydroxamic acid is dephosphorylated to form glycerol while the rest is oxidised via cytochrome aa3 to form acetate, succinate and pyruvate.
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PMID:Pathways of glucose catabolism in procyclic Trypanosoma congolense. 1084 79

Geobacter sulfurreducens strain PCA oxidized acetate to CO2 via citric acid cycle reactions during growth with acetate plus fumarate in pure culture, and with acetate plus nitrate in coculture with Wolinella succinogenes. Acetate was activated by succinyl-CoA:acetate CoA-transferase and also via acetate kinase plus phosphotransacetylase. Citrate was formed by citrate synthase. Soluble isocitrate and malate dehydrogenases NADP+ and NAD+, respectively. Oxidation of 2-oxoglutarate was measured as benzyl viologen reduction and strictly CoA-dependent; a low activity was also observed with NADP+. Succinate dehydrogenase and fumarate ductase both were membrane-bound. Succinate oxidation was coupled to NADP+ reduction whereas fumarate reduction was coupled to NADPH and NADH Coupling of succinate oxidation to NADP+ or cytochrome(s) reduction required an ATP-dependent reversed electron transport. Net ATP synthesis proceeded exclusively through electron transport phosphorylation. During fumarate reduction, both NADPH and NADH delivered reducing equivalents into the electron transport chain, which contained a menaquinone. Overall, acetate oxidation with fumarate proceeded through an open loop of citric acid cycle reactions, excluding succinate dehydrogenase, with fumarate reductase as the key reaction for electron delivery, whereas acetate oxidation in the syntrophic coculture required the complete citric acid cycle.
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PMID:Oxidation of acetate through reactions of the citric acid cycle by Geobacter sulfurreducens in pure culture and in syntrophic coculture. 1113 Oct 21

1) The oxygen consumption increases during Bufo bufo development in accordance with the two steps which border at the "heart beat" stage. 2) Cytochrome c oxidase activity is not proportional to the oxygen consumption: it is notable and constant in the first step, and it only increases in the second. 3) In the mitochondria of preneural embryos, citrate synthase, NADP+ dependent isocitrate dehydrogenase, and succinate dehydrogenase activities are very low in respect to malate dehydrogenase and glutamate oxaloacetate transaminase activities. The Krebs cycle results lowered at the condensing reaction level with acetyl accumulation when pyruvate is available. The same behavior has been observed in the Xenopus laevis oocytes and differentiated tissues. 4) The presence of a phosphagen system which is different from creatine phosphate and arginine phosphate, supporting ATP level, has been demonstrated in B. bufo embryos. 5) Mitochondria of postneural embryos are able to accomplish a complete Krebs cycle by increasing citrate synthase, and succinate dehydrogenase activities. 6) In all B. bufo development, malate dehydrogenase and glutamate oxaloacetate transaminase constitute a multienzymatic system by which the mitochondria accomplish a decarboxylic amino acid shunt required for the transformation of deutoplasm into protoplasm. This shunt is also operative in the X. laevis oocytes. 7) Through pyruvate production, by oxidative decarboxylation of malate, the NAD(P)+ dependent malic enzyme could carry out a fundamental anaplerotic function in the mitochondria which is specialized in the production of biosynthetic blocks belonging to the embryo in which the carbohydrates metabolism rather than the glycolytic activity is designed for pentose phosphate and glycerol phosphate synthesis for protein and cytomembrane production. 8) Consistent metabolic differences have been highlighted between B. bufo embryos and X. laevis embryos.
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PMID:Physiological differentiation of the mitochondria during Bufo bufo development. 1125 8

Respiration in cyanobacterial thylakoid membranes is interwoven with photosynthetic processes. We have constructed a range of mutants that are impaired in several combinations of respiratory and photosynthetic electron transport complexes and have examined the relative effects on the redox state of the plastoquinone (PQ) pool by using a quinone electrode. Succinate dehydrogenase has a major effect on the PQ redox poise, as mutants lacking this enzyme showed a much more oxidized PQ pool. Mutants lacking type I and II NAD(P)H dehydrogenases also had more oxidized PQ pools. However, in the mutant lacking type I NADPH dehydrogenase, succinate was essentially absent and effective respiratory electron donation to the PQ pool could be established after addition of 1 mM succinate. Therefore, lack of the type I NADPH dehydrogenase had an indirect effect on the PQ pool redox state. The electron donation capacity of succinate dehydrogenase was found to be an order of magnitude larger than that of type I and II NAD(P)H dehydrogenases. The reason for the oxidized PQ pool upon inactivation of type II NADH dehydrogenase may be related to the facts that the NAD pool in the cell is much smaller than that of NADP and that the NAD pool is fully reduced in the mutant without type II NADH dehydrogenase, thus causing regulatory inhibition. The results indicate that succinate dehydrogenase is the main respiratory electron transfer pathway into the PQ pool and that type I and II NAD(P)H dehydrogenases regulate the reduction level of NADP and NAD, which, in turn, affects respiratory electron flow through succinate dehydrogenase.
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PMID:Succinate dehydrogenase and other respiratory pathways in thylakoid membranes of Synechocystis sp. strain PCC 6803: capacity comparisons and physiological function. 1141 66


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