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)

We have previously reported the isolation of old yellow enzyme complexed with a ligand of low molecular weight which imparts a distinctive charge-transfer absorption to the enzyme, making it green in color (Matthews, R. G., and Massey, V. (1969) J. Biol. Chem. 244, 1779-1789). This ligand has now been identified as p-hydroxybenzaldehyde by removal from the enzyme and characterization of its optical spectrum and subsequent mass spectral analysis. Similar compounds which are also bound to old yellow enzyme have been isolated from yeast extract and identified. These compounds give rise to complexes with old yellow enzyme which are characterized by broad long wavelength absorption bands, and they lead to inhibition of the NADPH-O2 oxidoreductase activity catalyzed by old yellow enzyme.
J Biol Chem 1975 Dec 25
PMID:Identification of p-hydroxybenzaldehyde as the ligand in the green form of old yellow enzyme. 119 84

The distribution of the urea cycle enzyme, argininosuccinate synthetase, in the rat brain was determined using immunohistochemistry. This enzyme participates in the only known metabolic pathway for citrulline, its condensation with aspartate to form argininosuccinate, which can then be cleaved to fumarate and arginine. It may thus provide a mechanism to recycle citrulline, formed in the nervous system via nitric oxide synthase activity, back to the nitric oxide precursor, L-arginine. Argininosuccinate synthetase immunoreactivity was detected in discrete populations of neurons throughout the brain. Double-staining with nicotinamide adenine dinucleotide phosphate (reduced form)-diaphorase histochemistry for the localization of nitric oxide synthase demonstrated that argininosuccinate synthetase coexists with nitric oxide synthase in some brain regions. However, many neurons were found that contained one of these two enzymes, but not the other. Thus some nitric oxide synthase-containing neurons appear able to recycle citrulline via argininosuccinate, while others do not. Additional roles for argininosuccinate synthetase in the brain are discussed.
Neuroscience 1992 Dec
PMID:Immunohistochemical localization of argininosuccinate synthetase in the rat brain in relation to nitric oxide synthase-containing neurons. 128 10

Laminar preparations of fixed segments of the guinea-pig intestine were examined for nitric oxide synthase activity using reduced nicotinamide adenine dinucleotide phosphate and nitroblue tetrazolium salt as substrates. Under conditions specific for detecting nitric oxide synthase-related diaphorase activity, a subpopulation of neural elements in the myenteric plexus, deep muscular plexus and submucosa were intensely stained. Intensely stained nerve fibres were distributed throughout the meshworks of the myenteric plexus and its innervation of the circular muscle, and in the submucosa within Henle's plexus. Intensely stained nerve cells and their processes were evident in most myenteric ganglia but were rare in ganglia of Henle's plexus. Stained ganglion cells comprised types I, II and VI of the morphologically defined enteric nerve cells. Stained neural elements were increasingly prevalent within successively more caudal segments of the intestine. In addition to neuronal staining, arterioles of the submucosal vascular network displayed distinct, punctate patches of staining distributed over their surface. Perivascular nerve fibre staining was absent. These results show nitric oxide synthase activity to be present within neurons and fibres of the major enteric nerve layers and within submucosal blood vessels throughout the guinea-pig small and large intestine.
Neuroscience 1992 Dec
PMID:Histochemical localization of nitric oxide-synthesizing neurons and vascular sites in the guinea-pig intestine. 128 11

NG-Nitro-L-arginine, an inhibitor of nitric oxide (NO) synthase, markedly (+50%) increased the L-arginine-induced insulin release from isolated mouse islets but did not itself influence insulin secretion. An abundance of mouse islet cells were positively stained for the enzyme NADPH diaphorase, which reportedly is a marker for NO synthase. The data suggest that the NO synthase activity in mouse islet tissue may inhibit insulin secreting processes and that L-arginine has a dual action on insulin release.
Eur J Pharmacol 1992 Dec 15
PMID:Inhibition of islet nitric oxide synthase increases arginine-induced insulin release. 128 75

Nitric oxide synthase (NOS) was selectively stained in nerve fibers of the uterine cervix and neurons of the paracervical (PG) and dorsal root ganglia (DRG) by NADPH diaphorase histochemistry. In the cervix, numerous NADPH-diaphorase-positive nerve fibers were observed in the myometrium, endometrium and around arteries. In addition, a subpopulation of neurons within ganglia that innervate the cervix, i.e., the PG and DRG, were NADPH-diaphorase positive; thus the fibers in the cervix could be sensory and/or autonomic. NADPH-diaphorase/NOS localization identifies sites where nitric oxide (NO) can be synthesized. Since NO relaxes vascular and nonvascular smooth muscle, the prevalence and anatomical localization of NADPH-diaphorase-positive fibers suggest that they could influence functions of the uterine cervix.
Neurosci Lett 1992 Dec 07
PMID:Distribution of NADPH-diaphorase-positive nerves in the uterine cervix and neurons in dorsal root and paracervical ganglia of the female rat. 128 61

To clarify the role of nitric oxide (NO) in the pancreas, we histochemically investigated NADPH-diaphorase, a marker for NO synthase, in the rat pancreas. NADPH-diaphorase activity was localized in the neurons and endothelium of vessels. The nerve fibers with NADPH-diaphorase activity were observed in both the exocrine and the endocrine pancreas associated chiefly with the vascular systems. Most nerve cell bodies (98.5%) within the pancreatic parenchyma showed strong activity for this enzyme. These results suggest that NO may participate in the hemodynamic control of the pancreas and in the neuronal regulation of pancreatic exocrine and endocrine functions.
Neurosci Lett 1992 Dec 14
PMID:Histochemical demonstration of NADPH-diaphorase activity, a marker for nitric oxide synthase, in neurons of the rat pancreas. 128 46

The distribution and size of presumptive cholinergic somata in the brainstem of the Savanna monitor lizard Varanus exanthematicus were determined using the enzyme histochemical marker NADPH-diaphorase. Numerous neurons were labelled in the lizard brainstem with this technique. A three dimensional computer reconstruction of this population revealed that it shows marked similarity to the laterodorsal tegmental/pedunculopontine tegmental cholinergic cell column, an NADPH-diaphorase positive population in the mesopontine tegmentum of the mammalian brainstem.
Neurosci Lett 1992 Dec 14
PMID:Distribution of NADPH-diaphorase positive somata in the brainstem of the monitor lizard Varanus exanthematicus. 130 Apr 84

Coexistence of NADPH-diaphorase (ND) activity and somatostatin (SRIF) immunoreactivity was studied in the paraventricular nucleus (PVN) of the rat hypothalamus by successive incubations of the same sections. ND was found in all PVN subdivisions, mainly in the magnocellular ones. SRIF was practically restricted to the parvicellular periventricular subdivision. Contrary to other brain regions where a wide SRIF-ND coexistence has been observed, the periventricular parvicellular subdivision was the only place of the PVN where some neurons colocalize both markers. The combination of the immunocytochemical and the histochemical labelings allows a further permanent and easy-to-perform parcellation of periventricular PVN neurons.
Neurosci Lett 1992 Dec 14
PMID:Partial coexistence of NADPH-diaphorase and somatostatin in the rat hypothalamic paraventricular nucleus. 136 53

Participation of nitric oxide (NO) in the autonomic innervation of rat and guinea pig hearts was investigated by applying the NADPH diaphorase technique and immunohistochemistry with NO synthase antiserum. We present evidence that NO synthase is localized in cardiac ganglion cells and nerve fibers innervating the sinuatrial and atrioventricular nodes, the myocardium, local neurons, coronary arteries, and pulmonary vessels, suggesting an involvement of NO in neurogenic heart rate regulation, myocardial cell function, neuronal transmission in cardiac ganglia, and coronary as well as pulmonary vasodilation.
Circ Res 1992 Dec
PMID:Nitric oxide synthase in cardiac nerve fibers and neurons of rat and guinea pig heart. 138 6

Ferredoxin-NADP+ reductase from the cyanobacterium Anabaena sp. PCC 7119 was chemically modified by the alpha-dicarbonyl reagent phenylglyoxal. The studies of the inactivation by this compound, which is specific for arginyl residues, of both the diaphorase and NADPH-cytochrome c reductase activities, characteristic of the enzyme, are indicative of the involvement of at least one group of this kind in the binding site of NADP+ and a second one implicated in the interaction with ferredoxin. After specific cleavage of a FNR sample incubated with [7-14C]phenylglyoxal, two major labeled peptides were identified. The peptide which exhibited the higher degree of modification corresponded to residues 208-242. It contained four arginine residues but only two of them were the target of the modification: Arg224 and Arg233. Protection studies with protein substrates and sequence comparison with other reductases allow us to propose that these residues in Anabaena sp. PCC 7119 FNR must be involved in the interaction with the pyridine nucleotide. The second peptide corresponds to residues 75-103 and although it contains three arginine residues, Arg77 is the only one that exhibits the modification. This residue seems to be a key one in the interaction of this reductase with ferredoxin.
Arch Biochem Biophys 1992 Dec
PMID:Identification of arginyl residues involved in the binding of ferredoxin-NADP+ reductase from Anabaena sp. PCC 7119 to its substrates. 144 67


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