Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Synthesis of phosphatidylglycerol from CDPdiacylglycerol and glycerol 3-phosphate by membranous subcellular fractions of rat lung and liver was optimal when assayed in the presence of bovine serum albumin and Triton X-100. Specific activities of glycerolphosphate phosphatidyltransferase in all membranous subcellular fractions of lung were several times higher than the corresponding fractions from liver. Distribution of this enzyme in subcellular fractions of lung or liver closely parallel the activity of the mitochondrial enzymes monoamine oxidase and succinate cytochrome c reductase. The phosphatidylglycerol-synthesizing activity in microsomes of both lung and liver was a minor fraction of total tissue activity and could be interpreted as due either to contamination with outer mitochondrial membrane or to a small amount of activity innate to microsomes. These results suggest that phosphatidylglycerol, which is believed to be a component of pulmonary surfactant, is synthesized by lung at a rapid rate relative to liver and that the subcellular distribution of its synthesis is similar in both tissues, with mitochondria as the major site.
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PMID:Optimal assay and subcellular location of phosphatidylglycerol synthesis in lung. 626 66

The binding of [14C]cholesterol into rat brain mitochondrial membranes follows an exponential path described by the general formula y = a X ebx. [14C]cholesterol glucoside binding has a sigmoidal character where the "best-fit" curve of this type of binding is the one described by the Hill equation with Hill coefficient h = 2.06. These findings suggest a positive cooperativity in the binding of both compounds into rat brain mitochondrial membranes. The specific activity of the outer mitochondrial membrane enzyme monoamine oxidase was linearly decreased at different concentration of cholesterol or its glucoside. The specific activity of the inner mitochondrial membrane enzyme succinate-cytochrome c reductase was linearly decreased, while that of Rotenone-sensitive NADH-cytochrome c reductase was exponentially increased, at different concentrations of cholesterol. These results are discussed in terms of specific interactions of cholesterol with constituent mitochondrial membrane lipids and their implications for deviations from normal neuronal function.
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PMID:Functional changes of rat brain mitochondrial enzymes induced by monomeric cholesterol. 631 78

NAD kinase activity from dark grown corn coleoptiles is shown to be almost totally dependent on Ca2+ and calmodulin. Nearly all of the enzyme activity is found in a particulate fraction. Upon differential and density gradient centrifugation the NAD kinase activity co-migrates with the mitochondrial cytochrome c oxidase whereas marker activities for nuclei, etioplasts, endoplasmic reticulum, and microbodies could well be separated, indicating that the NAD kinase is associated with mitochondria. This NAD kinase, associated with intact mitochondria, can be activated by exogenously added Ca2+ and calmodulin. In order to investigate the submitochondrial localization of the NAD kinase, the organelles were ruptured by osmotic treatment and sonication and the submitochondrial fractions were separated by density gradient centrifugation. The NAD kinase activity exhibits the same density pattern as the antimycin A-insensitive NADH-dependent cytochrome c reductase, a marker enzyme of the outer mitochondrial membrane. Marker enzymes for the mitochondrial matrix and the inner mitochondrial membrane reveal different density profiles. These results indicate that the Ca2+, calmodulin-dependent NAD kinase from coleoptiles of dark grown corn seedlings is located at the outer mitochondrial membrane. The physiological relevance of the location and the Ca2+, calmodulin-dependence of the NAD kinase will be discussed.
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PMID:A Ca2+, Calmodulin-dependent NAD kinase from corn is located in the outer mitochondrial membrane. 632

An injection of ionol-type antioxidants stimulates fast oxidation of extramitochondrial NADH in isolated liver mitochondria via an external pathway, which is sensitive to cyanide and resistant to amital and antimycin A. This activation is accompanied by a decrease in cytochrome a and cytochrome (c + C1) levels in liver homogenate. Part of the cytochrome c pool can be removed by washing the antioxidant-treated mitochondria. It is assumed that the injection of the antioxidants leads to desorption of the cytochrome c bound to the inner membrane into the intermembrane space of mitochondria. This cytochrome acts as a linking agent between NADH cytochrome c reductase of the outer mitochondrial membrane and cytochrome c oxidase of the inner membrane. The Li-derivative of ionol (5 x 10(-4) and 10(-3) M) decreases the transmembrane potential of the submitochondrial particles from bovine heart by 15-20%.
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PMID:[Effect of ionol-type antioxidants on the energetics of liver mitochondria]. 706 21

Preparations enriched with plasmalemmal, outer mitochondrial, or Golgi complex membranes from rat liver were subfractionated by isopycnic centrifugation, without or after treatment with digitonin, to establish the subcellular distribution of a variety of enzymes. The typical plasmalemmal enzymes 5'-nucleotidase, alkaline phosphodiesterase I, and alkaline phosphatase were markedly shifted by digitonin toward higher densities in all three preparations. Three glycosyltransferases, highly purified in the Golgi fraction, were moderately shifted by digitonin in both this Golgi complex preparation and the microsomal fraction. The outer mitochondrial membrane marker, monoamine oxidase, was not affected by digitonin in the outer mitochondrial membrane marker, monoamine oxidase, was not affected by digitonin in the out mitochondrial membrane preparation, in agreement wit its behavior in microsomes. With the exception of NADH cytochrome c reductase (which was concentrated in the outer mitochondrial membrane preparation), typical microsomal enzymes (glucose-6-phosphatase, esterase, and NADPH cytochrome c reductase) displayed low specific activities in the three preparations; except for part of the glucose-6-phosphatase activity in the plasma membrane preparation, their density distributions were insensitive to digitonin, as they were in microsomes. The influence of digitonin on equilibrium densities was correlated with its morphological effects. Digitonin induced pseudofenestrations in plasma membranes. In Golgi and outer mitochondrial membrane preparations, a few similarly altered membranes were detected in subfractions enriched with 5'-nucleotidase and alkaline phosphodiesterase I. The alterations of Golgi membranes were less obvious and seemingly restricted to some elements in the Golgi preparation. No morphological modification was detected in digitonin-treated outer mitochondrial membranes. These results indicate that each enzyme is associated with the same membrane entity in all membrane preparations and support the view that there is little overlap in the enzymatic equipment of the various types of cytomembranes.
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PMID:Analytical study of microsomes and isolated subcellular membranes from rat liver VIII. Subfractionation of preparations enriched with plasma membranes, outer mitochondrial membranes, or Golgi complex membranes. 725 62

The rotenone-insensitive NADH-cytochrome c reductase activity and cytochrome b5 content in mitochondria and microsomes of liver of 1-, 3-, 12- and 24-month-old rats were studied. Thyroxine injection caused a considerable decrease in the microsomal activity in all age groups under study; in mitochondria this effect was increased with age. The decrease of the cytochrome b5 content was maximal in the microsomes and mitochondria of 12- and 24-month-old animals and was insignificant in 1-month-old rats. It was assumed that the age variations in regulation of the outer mitochondrial membrane function can be due changes in their population.
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PMID:[Effect of thyroxine on the NADH cytochrome c reductase activity of microsomes and outer mitochondrial membrane of rat liver depending on age]. 730 1

Rat liver microsomes and, to a lesser extent, nuclei were previously shown to produce reactive oxygen species at elevated rates after chronic ethanol treatment. The ability of intact rat liver mitochondria to interact with iron and either NADH or NADPH, and the effects of ethanol treatment, on production of reactive oxygen intermediates was determined. In the presence of ferric-ATP, NADH or NADPH catalyzed mitochondrial lipid peroxidation. Rates were elevated two- to threefold with mitochondria from ethanol-fed rats with both reductants. Mitochondrial lipid peroxidation was insensitive to superoxide dismutase, catalase, or hydroxyl radical scavengers but was sensitive to GSH and anti-oxidants such as trolox. Mitochondrial generation of hydroxyl radical-like species (assayed by oxidation of chemical scavengers) was increased after chronic ethanol treatment, as was H2O2 production. Modifiers of mitochondrial metabolism such as rotenone, cyanide, or an uncoupling agent, had no effect on mitochondrial production of reactive oxygen intermediates. The membrane-impermeable thiol reagent, p-chloromercuribenzoate, was complete inhibitory with both mitochondrial preparations. The activity of the rotenone-insensitive NADH-cytochrome c reductase, an enzyme of the outer mitochondrial membrane, was increased 40 to 60% by the ethanol treatment. These results suggest that NADH acting via the outer membrane NADH reductase can catalyze an iron-dependent production of oxygen radicals by rat liver mitochondria. The outer mitochondrial membrane fraction, prepared by digitonin fractionation, displayed increased rotenone-insensitive NADH-cytochrome c reductase activity after ethanol treatment and was more reactive in catalyzing scission of pBR322 DNA from the supercoiled form to the open circular forms. Rates of oxygen radical production by mitochondria and the extent of increase produced by chronic ethanol treatment are similar to those previously found with microsomes when NADH is the cofactor. Oxidation of ethanol by alcohol dehydrogenase generates NADH, and NADH-dependent production of reactive oxygen species by various organelles is increased after chronic ethanol treatment. These acute metabolic interactions coupled to induction by chronic ethanol treatment may play an important role in the development of a state of oxidative stress in the liver by ethanol.
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PMID:Increased production of reactive oxygen species by rat liver mitochondria after chronic ethanol treatment. 813 51

Subcellular localization of hexokinase in the honeybee drone retina was examined following fractionation of cell homogenate using differential centrifugation. Nearly all hexokinase activity was found in the cytosolic fraction, following a similar distribution as the cytosolic enzymatic marker, phosphoglycerate kinase. The distribution of enzymatic markers of mitochondria (succinate dehydrogenase, rotenone-insensitive cytochrome c reductase, and adenylate kinase) indicated that the outer mitochondrial membrane was partly damaged, but their distributions were different from that of hexokinase. The activity of hexokinase in purified suspensions of cells was fivefold higher in glial cells than in photoreceptors. This result is consistent with the hypothesis based on quantitative 2-deoxy[3H]glucose autoradiography that only glial cells phosphorylate significant amounts of glucose to glucose-6-phosphate. The activities of alanine aminotransferase and to a lesser extent of glutamate dehydrogenase were higher in the cytosolic than in the mitochondrial fraction. This important cytosolic activity of glutamate dehydrogenase was consistent with the higher activity found in mitochondria-poor glial cells. In conclusion, this distribution of enzymes is consistent with the model of metabolic interactions between glial and photoreceptor cells in the intact bee retina.
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PMID:Cellular and subcellular localization of hexokinase, glutamate dehydrogenase, and alanine aminotransferase in the honeybee drone retina. 815 42

The distribution of nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) in the central grey region (lamina X of Rexed) of the rat upper thoracic cord was examined by LM and EM. Numerous NADPH-d positive neuronal somata and fibres were present in the subependymal areas of the central grey region at levels T1-T3. Most of the neurons were located dorsal to the central canal in horizontal sections through this region. Many medially-directed NADPH-d positive fibres arising from neurons in n. intermediolateralis pars principalis, n. intercalatus spinalis and longitudinally-directed NADPH-d positive fibres arising from neurons in n. intercalatus pars paraependymalis formed a subependymal plexus. In horizontal sections through the central canal, some NADPH-d positive nerve fibres appeared to traverse the ependyma to enter and run along the central canal. By EM, NADPH-d reaction products were localized on the nuclear membrane, outer mitochondrial membrane and Golgi apparatus of both neurons and ependymal cells and in some axon terminals containing pleomorphic and round agranular synaptic vesicles. Present results suggest that besides the traditional monoamine-, amino acid- and peptide-containing axon terminals, the central grey region also contains fibres in which nitric oxide is utilized as a neurotransmitter or neuromodulator. The finding of NADPH-d positive fibres in the central canal suggests that nitric oxide may be released into DPH-cerebrospinal fluid. Since some of the ependymal cells were NADPH-d positive, it is suggested that they may be involved in the modulation of nitric oxide levels in the cerebrospinal fluid.
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PMID:The distribution of NADPH-d in the central grey region (lamina X) of rat upper thoracic spinal cord. 858 94

QSR1 (quinol-cytochrome c reductase subunit-requiring) is a highly conserved, essential gene in Saccharomyces cerevisiae that was identified through a synthetic lethal screen by its genetic relationship to QCR6, the gene for subunit 6 (Qcr6p) of the mitochondrial cytochrome bc1 complex. The function of the QSR1-encoded protein (Qsr1p) and its relationship to the QCR6-encoded protein are unknown. When yeast cell lysates are fractionated by density gradient centrifugation, Qsr1p separates from organelles and sediments with a uniformly sized population of particles that are similar to eukaryotic ribosomes upon velocity gradient centrifugation. When 40 S and 60 S ribosomal subunits are separated on velocity gradients, Qsr1p is found exclusively with the 60 S subunits, where it is a stoichiometric component. Extracts prepared from qsr1-1 cells are defective in in vitro translation assays relative to the wild type. In yeast cell lysates in which QCR6 rescues an otherwise lethal qsr1-1 mutation, Qcr6p is found only in mitochondria, both in respiratory-competent cells and in rho0 cells in which the bc1 complex is no longer present. These results suggest that suppression of the qsr1-1 mutation by QCR6 occurs by a trans-relationship across the outer mitochondrial membrane.
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PMID:QSR1, an essential yeast gene with a genetic relationship to a subunit of the mitochondrial cytochrome bc1 complex, codes for a 60 S ribosomal subunit protein. 914 60


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