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)

The role of mitochondrial proteins as antigens to antibodies of anti-M7 sera was analysed by flavin fluorescence, one- and two-dimensional Western blots and blue native gel electrophoresis. Flavin fluorescence of succinate dehydrogenase (SucDH, complex II of the respiratory chain) of rat liver inner mitochondrial membranes correlated with the immunoreactivity of a representative anti-M7 myocarditis serum. Antigens of isolated bovine heart mitochondria reacting with antibodies of myocarditis serum on two-dimensional Western blots were identified by MALDI-TOF and NanoESI mass spectrometry as myosin heavy chain beta and as dihydrolipoamide dehydrogenase of the mitochondrial 2-oxoacid dehydrogenase complexes. The SucDH-flavoprotein was not resolved as a discrete protein spot on two-dimensional polyacrylamide gels. However, separation of the rat liver inner mitochondrial membrane complexes by blue native gel electrophoresis followed by Western blotting, and Western blots of purified Escherichia coli SucDH complex revealed that anti-M7 sera contained antibodies directed against the SucDH-flavoprotein subunit.
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PMID:Analysis of mitochondrial antigens reveals inner membrane succinate dehydrogenase flavoprotein subunit as autoantigen to antibodies in anti-M7 sera. 1198 94

The present investigation concerning the histochemical demonstration of DPN diaphorase follows the development of a new reagent, Nitro-BT, which has already been used successfully for the cytochemical localization of the succinic dehydrogenase system. The most consistently favorable results were obtained with the lactate-lactic dehydrogenase system buffered at pH 7.4. Using sections of rat kidney and stomach, it was found that the intensity of stain was optimal after 15 minutes incubation at 37 degrees C., conducted aerobically. By appropriate variations in the substrate mixture it was possible to selectively demonstrate the histochemical distribution of certain DPN-linked dehydrogenases in addition to DPN diaphorase. This was made possible by the special distribution of some of these dehydrogenases which distinguished them from one another. Of the dehydrogenases studied the distribution pattern of beta-hydroxybutyric dehydrogenase was the most singular. In the gastric mucosa beta-hydroxybutyric dehydrogenase was restricted to the cells of the mucous lining epithelium and the gland necks; and in the kidney the enzyme was limited to the cells of the proximal convoluted tubule and thick limbs of Henle's loop. In contrast, lactic dehydrogenase like DPN diaphorase was demonstrable in almost all cytologic elements of both the stomach and the kidney.
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PMID:A histochemical method for the demonstration of diphosphopyridine nucleotide diaphorase. 1350 25

THE ALDEHYDES INTRODUCED IN THIS PAPER AND THE MORE APPROPRIATE CONCENTRATIONS FOR THEIR GENERAL USE AS FIXATIVES ARE: 4 to 6.5 per cent glutaraldehyde, 4 per cent glyoxal, 12.5 per cent hydroxyadipaldehyde, 10 per cent crotonaldehyde, 5 per cent pyruvic aldehyde, 10 per cent acetaldehyde, and 5 per cent methacrolein. These were prepared as cacodylate- or phosphate-buffered solutions (0.1 to 0.2 M, pH 6.5 to 7.6) that, with the exception of glutaraldehyde, contained sucrose (0.22 to 0.55 M). After fixation of from 0.5 hour to 24 hours, the blocks were stored in cold (4 degrees C) buffer (0.1 M) plus sucrose (0.22 M). This material was used for enzyme histochemistry, for electron microscopy (both with and without a second fixation with 1 or 2 per cent osmium tetroxide) after Epon embedding, and for the combination of the two techniques. After fixation in aldehyde, membranous differentiations of the cell were not apparent and the nuclear structure differed from that commonly observed with osmium tetroxide. A postfixation in osmium tetroxide, even after long periods of storage, developed an image that-notable in the case of glutaraldehyde-was largely indistinguishable from that of tissues fixed under optimal conditions with osmium tetroxide alone. Aliesterase, acetylcholinesterase, alkaline phosphatase, acid phosphatase, 5-nucleotidase, adenosine triphosphatase, and DPNH and TPNH diaphorase activities were demonstrable histochemically after most of the fixatives. Cytochrome oxidase, succinic dehydrogenase, and glucose-6-phosphatase were retained after hydroxyaldipaldehyde and, to a lesser extent, after glyoxal fixation. The final product of the activity of several of the above-mentioned enzymes was localized in relation to the fine structure. For this purpose the double fixation procedure was used, selecting in each case the appropriate aldehyde.
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PMID:Cytochemistry and electron microscopy. The preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation. 1397 66

The effect of environmental ion concentration on the enzyme activity of astrocytes was investigated in tissue cultures of rat cerebral cortex. It was found that the oxidative enzymatic activity (succinic dehydrogenase, DPN-diaphorase, and several other enzymes) of astrocytes depended on the concentration of NaCl in the environment. This response was not specific for NaCl, but was also elicited by MgCl(2) and LiCl; the response was less consistent, and often questionable for KCl. However, only NaCl could elicit enzymatic changes in astrocytes at concentrations known to be present in a living organism. Astrocytes were the only cells which responded this way; it appeared that the foot-plates were particularly involved in the response since increase of enzyme activity occurred earlier in the foot-plates than in the perikarya. It was concluded that astrocytes are metabolically involved in the maintenance of the ionic and osmotic environment of the central nervous system, particularly in regard to the active transport of sodium.
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PMID:THE ENZYMATIC RESPONSE OF ASTROCYTES TO VARIOUS IONS IN VITRO. 1410 17

We have studied the functional steps by which Saccharomyces cerevisiae mitochondria can synthesize FAD from cytosolic riboflavin (Rf). Riboflavin uptake into mitochondria took place via a mechanism that is consistent with the existence of (at least two) carrier systems. FAD was synthesized inside mitochondria by a mitochondrial FAD synthetase (EC 2.7.7.2), and it was exported into the cytosol via an export system that was inhibited by lumiflavin, and which was different from the riboflavin uptake system. To understand the role of the putative mitochondrial FAD carrier, Flx1p, in this pathway, an flx1Delta mutant strain was constructed. Coupled mitochondria isolated from flx1Delta mutant cells were compared with wild-type mitochondria with respect to the capability to take up Rf, to synthesize FAD from it, and to export FAD into the extramitochondrial phase. Mitochondria isolated from flx1Delta mutant cells specifically lost the ability to export FAD, but did not lose the ability to take up Rf, FAD, or FMN and to synthesize FAD from Rf. Hence, Flx1p is proposed to be the mitochondrial FAD export carrier. Moreover, deletion of the FLX1 gene resulted in a specific reduction of the activities of mitochondrial lipoamide dehydrogenase and succinate dehydrogenase, which are FAD-binding enzymes. For the flavoprotein subunit of succinate dehydrogenase we could demonstrate that this was not due to a changed level of mitochondrial FAD or to a change in the degree of flavinylation of the protein. Instead, the amount of the flavoprotein subunit of succinate dehydrogenase was strongly reduced, indicating an additional regulatory role for Flx1p in protein synthesis or degradation.
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PMID:Riboflavin uptake and FAD synthesis in Saccharomyces cerevisiae mitochondria: involvement of the Flx1p carrier in FAD export. 1455 54

The photoreducible cytochrome (Cyt) b from Dictyostelium discoideum was purified by differential precipitation with ammonium sulfate and chromatography over Sephadex G-100, diethylaminoethyl-cellulose, and calcium phosphate. The purified Cyt is composed of a single subunit of 15,000 daltons including a noncovalently bound protohaem, and exhibits in the reduced form alpha absorption bands at 555.5 and 560 nm at room temperature and 551 and 558.5 nm at 77 K. This Cyt is similar in some respects to Cyt b(557.5) from complex II of beef heart mitochondria, and to Cyt b(555) from the microsomal fraction of mung bean seedlings. Photoreduction by blue light of the purified Cyt b requires the addition of flavin; flavoprotein isolated from D. discoideum was the most active of four flavoproteins tested in catalyzing the photoreduction while diaphorase and l-amino-acid oxidase were inactive.
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PMID:Purification and Characterization of the Photoreducible b-type Cytochrome from Dictyostelium discoideum. 1666 Apr 35

Survivors of massive inhalation of combustion smoke endure critical injuries, including lasting neurological complications. We have previously reported that acute inhalation of combustion smoke disrupts the nitric oxide homeostasis in the rat brain. In this study, we extend our findings and report that a 30-minute exposure of awake rats to ambient wood combustion smoke induces protein nitration in the rat hippocampus and that mitochondrial proteins are a sensitive nitration target in this setting. Mitochondria are central to energy metabolism and cellular signaling and are critical to proper cell function. Here, analyses of the mitochondrial proteome showed elevated protein nitration in the course of a 24-hour recovery following exposure to smoke. Mass spectrometry identification of several significantly nitrated mitochondrial proteins revealed diverse functions and involvement in central aspects of mitochondrial physiology. The nitrated proteins include the ubiquitous mitochondrial creatine kinase, F1-ATP synthase alpha subunit, dihydrolipoamide dehydrogenase (E3), succinate dehydrogenase Fp subunit, and voltage-dependent anion channel (VDAC1) protein. Furthermore, acute exposure to combustion smoke significantly compromised the respiratory capacity of hippocampal mitochondria. Importantly, elevated protein nitration and reduced mitochondrial respiration in the hippocampus persisted beyond the time required for restoration of normal oxygen and carboxyhemoglobin blood levels after the cessation of exposure to smoke. Thus, the time frame for intensification of the various smoke-induced effects differs between blood and brain tissues. Taken together, our findings suggest that nitration of essential mitochondrial proteins may contribute to the reduction in mitochondrial respiratory capacity and underlie, in part, the brain pathophysiology after acute inhalation of combustion smoke.
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PMID:Impaired mitochondrial respiration and protein nitration in the rat hippocampus after acute inhalation of combustion smoke. 1913 81

The aim of the present investigation was to detect the regularities of postnatal development of "motor end-plate-muscle fiber (MF)-vascular network" system in different calf muscles of intact albino rats. Gastrocnemius, plantaris and soleus muscles were studied in 72 albino rats aged from 14 to 180 days. Identification of MF type was performed on the basis of succinate dehydrogenase and NADH-diaphorase activity. Cholinesterase activity of the neuro-muscular synapse (NMS) and alkaline phosphatase activity in the vascular endothelium were demonstrated using a combined histochemical method. The diameter of vascular network and the number of enzyme-active zones (EAZ) per one MF were the earliest parameters to be stabilized (before day 30). Histochemical profile of skeletal muscle was stabilized by the end of day 60. Dynamics of MF diameter and EAZ in NMS, vessel diameter and numbers per one MF is characterized by the periods of active changes (days 14-30), decrease (days 30-60) and stabilization (after day 60) of variance rate. The association between the level of oxidative metabolism and MF diameter was demonstrated.
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PMID:[Differentiation of calf skeletal muscles in the postnatal period of ontogenesis]. 2096 Jul 12

The mediated electro-enzymatic electrolysis systems based on the tricarboxylic acid (TCA) cycle reaction were examined on a micro-bulk electrolytic system. A series of the enzyme-catalyzed reactions in the TCA cycle was coupled with electrode reaction. Electrochemical oxidation of NADH was catalyzed by diaphorase with an aid of a redox mediator with a formal potential of -0.15 V vs. Ag|AgCl. The mediator was also able to shuttle electrons between succinate dehydrogenase and electrode. The charge during the electrolysis increased on each addition of dehydrogenase reaction in a cascade of the TCA cycle. However, the electrolysis efficiencies were close to or less than 90% because of the product inhibition. Lactate oxidation to acetyl-CoA catalyzed by two NAD-dependent dehydrogenases was coupled with the bioelectrochemical TCA cycle reaction to achieve the 12-electron oxidation of lactate to CO(2). The charge passed in the bioelectrocatalytic oxidation of 5 nmol of lactate was 4 mC, which corresponds to 70% of the electrolysis efficiency.
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PMID:Micro-coulometric study of bioelectrochemical reaction coupled with TCA cycle. 2239 82

The aim of the study was the estimation of structural and metabolic changes in the rat cerebellum Purkinje cells (PC) in the dynamics of subhepatic cholestasis. Histological, histochemical and electron microscopic methods were used. It was found that the cholestasis induced the progressive intensification of the structural and metabolic disturbances in the cerebellar PC reaching their maximum on days 10-20 and resulting in PC death and PC number reduction. In the cytoplasm of these cells the reduction of the activities of succinate dehydrogenase, NADH-diaphorase, glucose-6-dehydrogenase was recorded together with the decrease of RNA content and the activation of lactate dehydrogenase and acid phosphatase. The disturbances of PC at the ultrastructural level included the destruction of the nucleus and organelles (especially, of the mitochondria), associated with the increase of phagosome size and number, augmentation of relative free ribosome number, appearance of close contacts between mitichondria and cell nucleus and organelles. After 45-90 days in survived animals gradual normalization of PC structure and metabolism took place apparently as a result of spontaneous cholestasis elimination due to the development of new bile ducts.
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PMID:[Structural and histochemical changes in the rat cerebellum Purkinje cells after cholestasis]. 2389 17


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