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

Binding of [3H]Ro5-4864, a specific ligand for "peripheral type" benzodiazepine receptors, was determined in subcellular fractions of guinea pig lung. Even though the level of binding was predominant in the mitochondrial fraction, nuclear and cytosolic fractions also contained significantly measurable amounts of binding sites. The presence of binding sites in the microsomal fraction and in a fraction intermediate in density between the mitochondria and microsomes depended on which buffer was used to homogenize the tissue. If calcium-containing mannitol buffer was used, binding was negligible in the postmitochondrial organelles. However, in the case of sucrose buffer which did not contain any calcium, the postmitochondrial organelle fractions contained measurable amounts of binding sites. Most probably, these binding sites were of mitochondrial and nuclear origin. Furthermore, binding sites in the mitochondria were associated with the succinic dehydrogenase-enriched mitochondrial inner membrane, but not with the monoamine oxidase- and cholinephosphotransferase-enriched outer mitochondrial membrane. Furthermore, several proteolytic enzymes caused a decrease in binding of the ligand to the mitochondrial membrane only under hypotonic conditions and not under isotonic conditions, suggesting that the location of the receptors is inside the mitochondria.
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PMID:Subcellular distribution of "peripheral type" binding sites for [3H]Ro5-4864 in guinea pig lung. Localization to the mitochondrial inner membrane. 255 Apr 54

Tetrahymena pyriformis contains platelet-activating factor (PAF) as a minor lipid, which is biosynthesized de novo. A dithiothreitol-insensitive CDP-choline:cholinephosphotransferase (AAG-CPT), which utilizes alkyl-acetyl-glycerol as a substrate, had been detected in both the mitochondrial and microsomal fractions of the protozoan. In the present report, localization of this enzyme in submitochondrial fractions was studied. Cell fractionation was evaluated with enzyme and morphological markers. In this respect, succinate dehydrogenase, NADPH:cytochrome c reductase, glucose-6-phosphatase, alkaline phosphatase, monoaminoxidase, and cytochrome c oxidase activities were investigated. In the presence of antimycin A, mitochondrial activity of NADPH-cytochrome c reductase, was increased, while the microsomal one was reduced. Cardiolipin was distributed in the inner mitochondrial membrane. Alkaline phosphatase was found exclusively in the cytosol of the protozoan. The main portion of the dithiothreitol-insensitive AAG-CPT was localized in the inner mitochondrial membrane. Our data indicate that mitochondria are able to produce PAF, which might be associated with their function.
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PMID:Localization of an alkyl-acetyl-glycerol-CDP-choline: cholinephosphotransferase activity in submitochondrial fractions of Tetrahymena pyriformis. 1470 14

Actinomycin D prevents the full development in a 24-hour period of both wound respiration and cyanide resistance only when given in the first 10 to 12 hours following the cutting of potato tuber (Solanum tuberosum var. Russet) slices. The capacity for choline incorporation into phosphatidylcholine increases with slice aging and is inhibited by actinomycin D in the same time-restricted way. The time-restricted effectiveness of actinomycin D applies to the cutting-elicited enhanced synthesis of three critical enzymes of phosphatidylcholine synthesis, namely phosphorylcholine-glyceride transferase, phosphorylcholine-cytidyl transferase, and phosphatidylphosphatase. By contrast, actinomycim D given at any time is without effect on the measurable levels after 24 hours of a selection of glycolytic and mitochondrial respiratory enzymes. Neither succinic dehydrogenase nor cytochrome oxidase activity increases with time in aging potato slices in the presence or absence of chloramphenicol. The foregoing observations emphasize the central role of phospholipid, and ultimately membrane biosynthesis, in the development of wound-induced respiration.
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PMID:Dependence of Wound-induced Respiration in Potato Slices on the Time-restricted Actinomycin-sensitive Biosynthesis of Phospholipid. 1666 41

Thifluzamide, a succinate dehydrogenase inhibitor (SDHI) fungicide, has been widely used in rice fields throughout the world and causes hepatotoxicity in zebrafish (Danio reio). This study was conducted to investigate the effect of thifluzamide on lipid metabolism in zebrafish after exposure to a control or, 0.019, 0.19, or 1.90mg/L thifluzamide for 28days. Following exposure, pathological changes in the liver were evaluated. Total cholesterol (TCHO) level, and triglyceride (TG) levels as well as hepatic lipase (HL), lipoprotein lipase (LPL), fatty acid synthetase (FAS) and carnitine palmitoyltransferase (CPT-I) activities were measured. In addition, the expression levels of genes related to lipid metabolism were quantified. No obvious accumulation of lipid droplets was detected in the liver following any of the thifluzamide treatments. TCHO and TG levels were significantly decreased. FAS activity was markedly decreased, and CPT-I activity was significantly increased in the 0.19 and 1.90mg/L groups. However, no apparent changes in HL and LPL activities were observed in any of the treatment groups. Additionally, the expression of genes related to lipid metabolism showed corresponding changes. The results suggest that altered gene expression and enzyme activities might be responsible for the changes in lipid metabolism, as evidenced by the decreased TCHO and TG levels. Overall, thifluzamide altered lipid metabolism and led to events that might contribute to developmental toxicity in exposed zebrafish.
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PMID:Thifluzamide affects lipid metabolism in zebrafish (Danio reio). 2975 75