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)

Antibodies specific for the Mr 65,000 (flavoprotein) and the Mr 28,000 subunits of the succinic dehydrogenase (SDH) of Bacillus subtilis were obtained. By using these antibodies it was shown that both subunits accumulated in the cytoplasm during 5-aminolevulinic acid starvation of a 5-aminolevulinic acid auxotroph. In the cytoplasm the subunits were not associated since they precipitated essentially independently of each other with subunit-specific antibody. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis the cytoplasmic subunits migrated identically with the corresponding subunits from the purified membrane-bound SDH complex. Cytoplasmic subunits were pulse-labeled with L-[35S]methionine during 5-aminolevulinic acid starvation. The labeled subunits bound to the membrane when heme synthesis was resumed and also when protein synthesis was blocked by chloramphenicol before readdition of 5-aminolevulinic acid. The experiments thus demonstrated a precursor relationship between cytoplasmic subunits and the subunits of the membrane-bound SDH complex. All SDH-negative mutants isolated so far carry mutations in the citF locus. None of the mutants was found to have either the Mr 65,000 or the Mr 28,000 SDH subunits in the membrane. Four citF mutants, however, contained both subunits in the cytoplasm. Three of these mutants lacked spectrally detectable cytochrome b558. The respective mutations mapped at one end of the citF locus. These results strongly support our previous suggestion that cytochrome b558 is (part of) a membrane binding site for SDH in B. subtilis.
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PMID:Biosynthesis and membrane binding of succinate dehydrogenase in Bacillus subtilis. 677 71

Hamster brown adipocytes were incubated for up to 24 h with or without norepinephrine (NE) in Dulbecco's modified Eagle's medium supplemented with bovine serum albumin, calf serum, and antibiotics. Brown fat cells were viable for 24 h as defined by their ability to respond to NE by a 10-fold increase in oxygen consumption. However, prolonged exposure of the cells to NE led to a decline in NE-stimulated rates of O2 consumption, which was not the result of loss of cell thermogenic capacity. Brown fat cells incubated for 24 h with or without NE showed no significant change in succinate dehydrogenase activity or uncoupling protein (UCP) content. However, cell recovery after 24 h was significantly reduced in the absence of NE. In brown adipocytes isolated from rat, NE increased [35S]methionine incorporation into cell proteins and UCP. In contrast, [35S]methionine incorporation in hamster brown adipocyte proteins and UCP was greater than in rat brown fat cells and was not increased by NE. These results indicate that although NE may be required for cell survival, it does not stimulate protein and UCP synthesis in hamster brown fat cells.
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PMID:Norepinephrine does not stimulate protein and UCP synthesis in brown adipocytes of golden Syrian hamsters. 834 73

The objective of this work was to evaluate whether insulin, like norepinephrine (NE), exerts direct growth effects in brown adipocytes, as assessed by changes in rates of protein labeling with [35S]methionine. Mouse brown adipocytes isolated by tissue collagenase digestion were incubated for up to 24 h with or without NE in Dulbecco's modified Eagle's medium with albumin, calf serum, and antibiotics. There was a 40% cell loss and a 50% decrease in cell content of succinate dehydrogenase (SDH) activity over 24 h. Both cell recovery and SDH content significantly improved in the presence of NE. In addition, NE increased [35S]methionine incorporation into proteins in both cytosolic and mitochondrial compartments. These effects of NE were inhibited by propranolol. Both insulin and insulin-like growth factor-1 (IGF-1) receptors were detected in brown adipocytes, with insulin receptors in much greater concentration. Increased protein labeling was observed when brown adipocytes were incubated for 4 h with 0.2-5 nM insulin in the absence of serum. This effect was small (30% stimulation) compared with the 200-350% increase observed with NE, and 5 nM IGF-1 had no effect. These results indicate direct trophic actions of both NE and insulin in mouse brown adipocytes, with the effects of NE an order of magnitude greater than those of insulin.
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PMID:Comparison of trophic effects of norepinephrine, insulin, and IGF-1 in mouse brown adipocytes. 876 96

A novel method for quantifying the fatty change of the graft liver by characterizing the optical property of the tissue was introduced. A wide range of lipid content in the rat liver was obtained by using different feeding regimens, with lipotropic chow (choline/methionine deficient or low chow). The liver was removed and flushed with Krebs-Ringer buffer solution with 3% albumin, and the optical properties of the liver, i.e., absorption and reduced scattering coefficients (mu(a) and mu(s)'), were measured by time-resolved spectroscopy. The fatty liver showed lower mu(a) and higher mu(s)' than the normal liver. Lower mu(a) and lower succinate dehydrogenase activity of the fatty liver suggested that the decrease in mu(a) might indicate a decrease in the mitochondrial content. The value of mu(s)' was positively correlated with the lipid content of the liver, which indicates that fat droplets inside the hepatocyte act as dominant scatterers. To subtract the contribution of the mitochondrial compartment to mu(s)', the ratio of mu(s)' to mu(a) (mu(s)':mu(a)) was useful for the assessment of the lipid content of the liver. These findings were also relevant with prediction of light scattering by the Mie theory. It was concluded that mu(a) and mu(s)' of the graft liver, measured by time-resolved spectroscopy, can be useful parameters for quantifying the fatty change of the graft liver.
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PMID:Optical determination of fatty change of the graft liver with near-infrared time-resolved spectroscopy. 883 Aug 30

Decreased glutamine availability is proposed as a mechanism for changes in immune function with intense exhaustive exercise. Less is known about the immunomodulatory effects of regular nonexhaustive exercise. To determine the effects of low intensity regular exercise and dietary glutamine supplementation on plasma glutamine concentrations, lymphocyte metabolism, and immune function, male (278 +/- 5 g) and female (182 +/- 1 g) Sprague-Dawley Buffalo rats were fed nutritionally complete casein-based semi-purified diets +/- 2% w/w glutamine. Rats were trained (21 d), as confirmed by higher (P < 0.05) succinate dehydrogenase activity in soleus muscle, to swim 2 or 4 h.d-1 or remained sedentary. Exercise lowered plasma concentrations of tryptophan, glutamate, methionine, alanine, threonine, aspartate, asparagine, and ornithine and increased the lysine concentration (P < 0.05). Neither diet nor exercise altered plasma glutamine concentrations, lymphocyte phenotypes in spleen, or the in vitro rates of splenocyte energy metabolism (production of glucose and glutamine metabolites or ATP concentrations in the incubation media). Compared with nonsupplemented rats, splenic cytolytic activity (lysis of 51Cr labeled YAC-1 cells) was reduced (P < 0.05) in the glutamine-supplemented exercising group. Under these conditions, glutamine supplementation does not appear to provide any added benefit to the exercise-trained animal.
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PMID:Dietary L-glutamine does not improve lymphocyte metabolism or function in exercise-trained rats. 910 29

In isolated pea (Pisum sativum L.) mitochondria incorporation of 35S-methionine into newly synthesised proteins was influenced by the presence of site-specific inhibitors of the respiratory electron-transport chain. These effects were not produced by changes in the rate of respiratory electron transport itself nor by changes in ATP concentration. Protein synthesis was inhibited by inhibitors of ubiquinone reduction but not by inhibitors of ubiquinol oxidation. By the use of additional inhibitors at specific sites of the respiratory chain, different oxidation-reduction states were obtained for the different complexes in the electron-transport chain. It was found that electron transport through succinate:ubiquinone oxidoreductase (respiratory complex II) was specifically required for protein synthesis, even when all the other conditions for protein synthesis were satisfied. We suggest that a subunit of complex II, or a component closely associated with complex II, is involved in a regulatory system that couples electron transport to protein synthesis.
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PMID:Protein synthesis by isolated pea mitochondria is dependent on the activity of respiratory complex II. 961 82

The aim of this study was to evaluate the effect of 5-, 15-, and 60-min enflurane anesthesia on the levels of Met-enkephalin, Leu-enkephalin and neuropeptide Y in discrete areas of the rabbit brain. We also evaluated the effect of enflurane anesthesia on energetic, transport and catabolic processes by measuring the activities of succinate dehydrogenase, magnesium-dependent adenosine triphosphatase and acid phosphatase in the rabbit striatum and hypothalamus. Induction of anesthesia (5 min) decreased Met-enkephalin levels in the hypothalamus and striatum, and increased them in the hippocampus and mesencephalon. Induction of anesthesia increased Leu-enkephalin levels in all brain areas studied, except for the striatum, and increased neuropeptide Y content in the hippocampus. 15- and 60-min enflurane anesthesia increased Met-enkephalin content in the hypothalamus and hippocampus. After 15- and 60-min anesthesia, and after cessation of anesthesia, Leu-enkephalin levels were increased in the hypothalamus and mesencephalon, and were decreased in the striatum and hippocampus. In the striatum, neuropeptide Y content was significantly decreased during anesthesia and after cessation of anesthesia. Histochemical analysis revealed that enflurane enhanced ATP production, catabolic processes, and the rates of exchange and transport of energetic substrates in the striatum and hypothalamus. In conclusion, enflurane affects the levels of Met, Leu-enkephalins and NPY in a manner depending on the duration of anesthesia and the brain structure. Compared with isoflurane , which was studied in our previous study enflurane produces stronger alterations in the activities of enzymatic marker in the rabbit brain. This suggests that enflurane may be less safe than isoflurane.
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PMID:Effect of enflurane on selected neuropeptides and marker enzymes in rabbit brain. 1009 16

Succinate dehydrogenase (SDH) deficiency represents a minor cause of Leigh syndrome (LS). Noticeably, the first mutation in a nuclear-encoded respiratory chain component, a mutation in the 5p15 copy of the flavoprotein (Fp) subunit gene of the SDH, was reported 4 years ago in two siblings with LS and SDH deficiency. We now report a new patient with LS and SDH deficiency. Because two copies of the Fp gene are present in the human genome, we first determined the complete structure of these two copies. This allowed us to identify a 1 bp deletion creating a frameshift in the 3q29 copy, confirming that this second copy was a pseudogene. We also sequenced the promoter region of the 5p 15 gene and, in addition, screened for mutations in the patient. Sequencing of the Fp SDH cDNA in the patient only allowed us to identify a heterozygous C to T transition, changing an alanine to a valine in one allele. This transition was found to be heterozygous in the patient's father but was absent from 150 controls. Transfection of the corresponding mutant cDNA into human Fp-deficient cells failed to restore normal SDH activity, confirming the deleterious effect of this mutation. The second allele, inherited from the mother, carried an A to C substitution changing the methionine translation initiation codon to a leucine. This mutant transcript represented only 10% of total Fp transcript suggesting instability of this transcript. So far, profound deficiencies in complex II activity resulting from mutations in the Fp gene of the SDH present only as LS, a striking observation in view of the ubiquitous expression of this typical housekeeping gene in humans.
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PMID:Compound heterozygous mutations in the flavoprotein gene of the respiratory chain complex II in a patient with Leigh syndrome. 1074 66

Shoots of germinating rice (Oryza sativa L.) seedlings are able to grow under anoxia and to withstand long periods of anoxic treatment. Mitochondria were purified from aerobically germinated and anaerobically treated rice shoots by differential and isopycnic centrifugation and were found to consist of two subpopulations. The mitochondrial subpopulation of higher density was used for further characterization. Ultrastructural studies showed anaerobic mitochondria to be significantly different from aerobic mitochondria, with a matrix of lower density and more developed cristae. Aerobic and anaerobic mitochondria also differed in their specific activities for fumarase and succinate dehydrogenase, which were significantly lower after the anoxic treatment. In vivo labeling of seedlings with l-[(35)S]methionine and subsequent isolation of the mitochondria indicated that anoxia induced a drastic decrease, but not a total inactivation, of the synthesis of mitochondrial proteins. In organello protein synthesis showed that anaerobic mitochondria were able to synthesize most of the polypeptides synthesized by aerobic mitochondria, although only in the presence of exogenous ATP, as would occur under anoxia. Anaerobic mitochondria, but not aerobic mitochondria, could carry out protein synthesis without a functional respiratory chain. Thus, mitochondrial protein synthesis was found to be potentially functional in the rice shoot under anoxia.
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PMID:Effects of anoxia on mitochondrial biogenesis in rice shoots: modification of in organello translation characteristics. 1666 55

The mechanism for fumarate reduction by the soluble fumarate reductase from Shewanella frigidimarina involves hydride transfer from FAD and proton transfer from the active-site acid, Arg-402. It has been proposed that Arg-402 forms part of a proton transfer pathway that also involves Glu-378 and Arg-381 but, unusually, does not involve any bound water molecules. To gain further insight into the importance of this proton pathway we have perturbed it by substituting Arg-381 by lysine and methionine and Glu-378 by aspartate. Although all the mutant enzymes retain measurable activities, there are orders-of-magnitude decreases in their k(cat) values compared with the wild-type enzyme. Solvent kinetic isotope effects show that proton transfer is rate-limiting in the wild-type and mutant enzymes. Proton inventories indicate that the proton pathway involves multiple exchangeable groups. Fast scan protein-film voltammetric studies on wild-type and R381K enzymes show that the proton transfer pathway delivers one proton per catalytic cycle and is not required for transporting the other proton, which transfers as a hydride from the reduced, protonated FAD. The crystal structures of E378D and R381M mutant enzymes have been determined to 1.7 and 2.1 A resolution, respectively. They allow an examination of the structural changes that disturb proton transport. Taken together, the results indicate that Arg-381, Glu-378, and Arg-402 form a proton pathway that is completely conserved throughout the fumarate reductase/succinate dehydrogenase family of enzymes.
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PMID:A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina. 1669 70


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