Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.6.99.1 (NADPH-diaphorase)
 3,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

Glycollate dehydrogenase and NADFH-glyoxylate reductase are constitutive enzymes in Percoll-purified mitochondria from phototrophic, mixotrophic and organotrophic cells of Euglena gracilis Klebs strain z Pringsheim. Glycollate oxidation by isolated mitochondria is stimulated four-fold by the addition of glutamate but rates of glycine oxidation are low in mitochondria from all cell types, the ratio of malate to glycine oxidation always being greater than 4:1. Measurement of the rate of NADPH oxidation in intact mitochondria and mitoplasts showed that the outer mitochondrial membrane is impermeable to NADPH and in the absence of NADPH-dehydrogenase activity the oxidation of NADPH by mitoplasts is dependent on the presence of glyoxylate for NADPH-glyoxylate-reductase activity. It is concluded that glycollate oxidation in the mitochondrion provides glyoxylate which, in the presence of a suitable amino-donor, can be converted to glycine by glutamate-glyoxylate amino-transferase so providing essential intermediates for biosynthesis. Glycollate oxidation outside the mitochondrion is concerned with photorespiratory metabolism and the inability of mitochondria to oxidise exogenous glycine at appreciable rates means that the separation of photorespiratory metabolism from the biosynthesis of essential intermediates is effected.
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PMID:Glycollate-pathway enzymes in mitochondria from phototrophic, organotrophic and mixotrophic cells of Euglena. 2425 68