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)

Cultured cells from human colon adenocarcinoma spontaneously release structures which display an intense 31P NMR signal from RNA and mobile phospholipids. Furthermore, the DPH probe in the cell supernatant shows an intense fluorescence, thus indicating its insertion in lipid vesicles. The total membranes, prepared from the same cells, also release similar structures. The fatty acid chain signals from the mobile lipids, observable in the H NMR spectrum, and the fluorescence polarization of the DPH probe are strongly affected by RNAase digestion, thus indicating an association between RNA molecules and lipids. The enzymatic marker cytochrome c reductase was assayed to rule out possible contamination from endoplasmatic reticulum. A high alkaline phosphatase activity was instead found in the supernatant samples, thus indicating that the shed material is released by the plasma membrane.
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PMID:RNA-lipid complexes released from the plasma membrane of human colon carcinoma cells. 335 12

In this study, we wished to clarify the distribution and co-localization of nitric oxide synthase and NA-DPH-diaphorase (NADPH-d) in nerve cells, nerve fibres and parenchymal cells in exocrine and endocrine pancreas, and to assess the influence of fixation on the staining pattern obtained. For this purpose, we applied nitric oxide synthase immunocytochemistry and NADPH-d histochemistry to rat and human pancreas under different fixation conditions. Antibodies to neuronal and endothelial nitric oxide synthase were similarly applied. We found complete co-localization of neuronal nitric oxide synthase and NADPH-d in ganglion cells, and in nerve fibres around acini, excretory ducts, blood vessels and in islets of Langerhans of rat and human pancreas. Immunoreactivity for endothelial nitric oxide synthase was co-localized with NADPH-d in endothelial cells. However, in NADPH-d reactive islet and ductal epithelial cells we could detect neither brain nor endothelial nitric oxide synthase immunoreactivity with any fixation protocol applied. There were marked differences in NADPH-d staining of both neurons and parenchymal cells under different fixation conditions. These results indicate the existence of different types of NADPH-d, which are associated or not associated with nitric oxide synthase(s), and which are differently influenced by various fixation procedures in rat and human pancreas.
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PMID:Neuronal and endothelial nitric oxide synthase immunoreactivity and NADPH-diaphorase staining in rat and human pancreas: influence of fixation. 753 38

Paramecium is a valuable eukaryotic model system for studying chemosensory transduction, adaptation and cellular sensory integration. While millimolar amounts of many attractants hyperpolarize and cause faster forward swimming, oxidants are repellents that depolarize and cause backward swimming at micromolar concentrations. The non-permeant oxidants cytochrome c, nitro blue tetrazolium and ferricyanide are repellents with half maximal concentrations of 0.4 microM, 2.2 microM and 100 microM respectively. In vivo reductase activities follow the same order of potencies. The concentration dependence of the cytochrome c reductase activity is well correlated with cytochrome c-induced depolarizations. This suggests that plasma membrane reduction of external cytochrome c is electrogenic, causing membrane depolarization and chemorepulsion. The reductase activity also appears to be voltage dependent. Depolarization by either K+, Na+, Ca++ or Mg++ correlates with inhibition of both in vivo reductase activities and cytochrome c-induced membrane potential changes. These responses were also seen in deciliated cells, showing that the body plasma membrane is sufficient for the response. Both chloroquine and diphenyleneiodonium inhibited reductase activities but only at unusually high concentrations. This activity showed no pH dependence in the physiological range. We propose that a plasma membrane bound NA-DPH-dependent reductase controls oxidant-induced depolarizations and consequent chemorepulsion.
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PMID:Oxidants act as chemorepellents in Paramecium by stimulating an electrogenic plasma membrane reductase activity. 796 25

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