Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.6.99.1 (NADPH-diaphorase)
3,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The present study investigated the ultrastructure of neurons in the caudal spinal trigeminal nucleus. These neurons which are believed to function as interneurons in the transmission of orofacial nonreflexive nociceptive information, measured 20 microns x 11 microns, and were nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) positive. The reaction product, formazan, was localized in the nuclear envelope, mitochondria, rough endoplasmic reticulum, and multivesicular bodies of these neurons. It was also localized in the membrane of the smooth endoplasmic reticulum at the axon terminal. The neurons were contacted by both axosomatic and axodendritic synapses formed by both NADPH-d positive and NADPH-d negative axon terminals. Two types of NADPH-d positive axon terminals could be recognized. The first was a large terminal containing many stained mitochondria and unstained small round agranular vesicles mixed with some slightly flattened ones. It formed asymmetrical axodendritic synapse. The second type of axon terminals contained pleomorphic synaptic vesicles and formed asymmetrical synapses upon both dendrites and soma. The sources of NADPH-d positive axon terminals were discussed. Most of the unstained axon terminals forming axosomatic and axodendritic synapses with stained cell bodies and dendrites contained flattened vesicles. In addition to the above, complicated synaptic configurations showing NADPH-d positive axoaxonic synapses in relation to NADPH-d negative dendritic spines were also seen in which a NADPH-d negative dendritic spine was completely contacted by a NADPH-d positive bouton which was in turn contacted by another NADPH-d positive bouton.
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PMID:Ultrastructural study of NADPH-d positive neurons in laminae I and II of the rat caudal spinal trigeminal nucleus. 939 13

The distribution of the NADPH diaphorase activity was studied in mouse Leydig cells by means of light and electron microscopy. When observed by the light microscope, most Leydig cells appeared intensely stained; a few cells (about 10%) showed a slightly positive or apparently negative reaction. The inhibitory effects of N(G)-nitro-L-arginine and iodonium diphenyl on frozen sections suggest the colocalisation of NADPH diaphorase reaction with nitric oxide synthase. The ultrastructural study revealed that all the Leydig cells were positively stained for NADPH diaphorase; however, a small number of cells displayed weak enzymatic activity. The reaction product was located in the mitochondria, smooth endoplasmic reticulum and lipidic vacuoles, and the nuclear envelope was also stained. The possible meaning of the NADPH diaphorase activity in the Leydig cells of mice was discussed.
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PMID:Cytochemical localisation of the NADPH diaphorase activity in the Leydig cells of the mouse. 954 72

Intense immunoreactivity for the m2-muscarinic receptor was found in a population of interstitial polymorphic neurons embedded within the infracortical white matter and the adjacent deep layers of the cerebral cortex. These infracortical neurons were evenly distributed throughout architectonic subdivisions of the monkey cortex except for parts of primary visual cortex where they were less numerous. A similar set of m2-immunoreactive interstitial cells was also detected in the human lateral temporal neocortex obtained at surgery. Upon electron microscopic examination, they were found to receive unlabelled synaptic inputs and displayed abundant rough endoplasmic reticulum, a prominent nucleolus, and invaginations of the nuclear membrane. Double labelling of m2 immunoreactivity and acetylcholinesterase histochemistry demonstrated that approximately 90% of the m2-positive infracortical cells were acetylcholinesterase-rich in the monkey and human brains. Conversely, the proportion of acetylcholinesterase-rich infracortical neurons that were m2-immunoreactive was over 90% in the monkey and at least 50% in the human. The concurrent visualization of nicotinamide adenine dinucleotide phosphate diaphorase (NADPH-d) enzyme activity with m2 immunoreactivity in the monkey and human brain showed that 85-95% of m2-immunoreactive infracortical cells were NADPH-d positive. Conversely, about 70% of NADPH-d cells contained m2 immunoreactivity. These observations provide the most convincing information to date that many of the acetylcholinesterase-rich neurons located in the infracortical white matter of the cerebral cortex are likely to be cholinoceptive. The expression of NADPH-d by these neurons suggests that they may also provide a relay through which cholinergic innervation, originating predominantly from the nucleus basalis of Meynert, could regulate the release of nitric oxide in the cerebral cortex and subjacent white matter. The degeneration of these neurons may account for at least some of the depletion of m2 receptors that has been reported in Alzheimer's disease.
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PMID:Infracortical interstitial cells concurrently expressing m2-muscarinic receptors, acetylcholinesterase and nicotinamide adenine dinucleotide phosphate-diaphorase in the human and monkey cerebral cortex. 957 81

Nicotinamide adenine dinucleotide phosphate diaphorase (NADPH-d) histochemistry was used to demonstrate the presence of nitric oxide in the developing chicken thymus. NADPH-d was first expressed in the epithelial cells located at the corticomedullary junction of the thymic rudiment on day 13 of incubation. The number of labelled cells gradually increased from day 13 to day 21. Ultrastructural evidence showed that the labelling was localized in a heterogeneous population of cells in the medulla near the corticomedullary junction, comprising the cystic, undifferentiated, myoid, lymphoid and epithelial reticular cells. At this age, the vascular endothelium was NADPH-d positive. Labelling was also detected in some macrophages. The reaction product primarily labelled profiles of rough endoplasmic reticulum and to a lesser extent the outer membranes of mitochondria, portions of the nuclear envelope and the Golgi apparatus. By day 18/19, NADPH-d-labelled nerve fibres were occasionally observed in the interlobular connective tissue. By day 21, these fibres formed perivascular plexuses. Labelled nerve fibres were occasionally observed in the medullary parenchyma. Possible functions of nitric oxide in the embryonic thymus are discussed.
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PMID:Ontogeny of NADPH-d expression in the thymic microenvironment of the chick embryo. 979 49

This study examined the distribution of reduced nicotinamide adenine dinucleotide phosphate diaphorase (NADPH-d) reactivity and nitric oxide synthase (NOS) immunoreactivity in the lumbosacral dorsal root ganglia (DRG) in male guinea pigs. A differential distribution of NADPH-d reactivity and NOS immunoreactivity was detected in neurons of DRG at different segmental levels. There were numerically more intensely stained NADPH-d and NOS reactive cells in the rostral (L1-L3) DRG compared with those at the caudal (L6-S4) levels. In the corresponding DRG, NADPH-d reactivity was not paralleled by NOS immunoreactivity. This was evidenced by the wide distribution of afferent neurons in the lumbosacral DRG stained for NADPH-d, yet only a small number of them exhibited NOS immunoreactivity. Double labelling study has shown that some of the NADPH-d positive neurons were NOS negative. Ultrastructurally, NADPH-d reaction product was associated with the membranes of various subcellular organelles, including the rough endoplasmic reticulum (rER), Golgi saccules, mitochondria and some segments of the nuclear envelop, whereas NOS immune-precipitate was patchily distributed throughout the cytoplasm. Present results suggest that nitric oxide (NO) may function as a neurotransmitter in the afferent pathways at lumbosacral segments. On the other hand, in view of their marked disparity in numbers and the lack of total one-to-one correspondence, it seems likely that the NOS positive neurons represent only a subpopulation of the NADPH-d positive cells in the lumbosacral DRG.
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PMID:Localization of nicotinamide adenine dinucleotide phosphate-diaphorase reactivity and nitric oxide synthase immunoreactivity in the lumbosacral dorsal root ganglia in guinea pigs. 1002 35

We investigated the subcellular localization of nicotinamide adenine dinucleotide phosphate diaphorase (NADPH-d) activity, a histo- and cyto-chemical marker of nitric oxide synthase, in human placental trophoblast obtained from women with normal term pregnancies. Tetrazolium salt BSPT was used as the capturing agent. Precipitates of BSPT-formazan indicative of NADPH-d reaction were observed on the membranes of endoplasmic reticulum and nuclear envelope of syncytiotrophoblasts. Our results indicate these two intracytoplasmic organellae are the sites of nitric oxide generation in the syncytiotrophoblasts of normal term human placenta.
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PMID:Enzyme-cytochemically detectable NADPH-diaphorase activity is present in the endoplasmic reticulum and nuclear envelope of the syncytiotrophoblast of the human placenta. 1056 58

The cellular and subcellular distribution of neuronal nitric oxide synthase and its related reduced beta-nicotinamide adenine dinucleotide phosphate (NADPH)-diaphorase activity was compared in wild-type and homozygous knockout mice, in which the gene for neuronal nitric oxide synthase has been disrupted, resulting in a lack of the predominant splice isoform alpha. In the laterodorsal tegmental nucleus, used as a model structure, the cholinergic principal neurons also exhibited an intensive neuronal nitric oxide synthase immunoreactivity. Using the tetrazolium salt 2-(2-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazidyl)-tetrazo++ +-lium chloride (BSPT), these neurons were filled with NADPH-diaphorase reaction product, whereas the equivalent neurons of knockout mice showed, if at all, only traces of neuronal nitric oxide synthase immunoreactivity in parallel to a diminished NADPH-diaphorase labelling. Subcellularly, the neuronal nitric oxide synthase-related diaminobenzidine product was, apparently owing to diffusion artifact, more or less evenly distributed in the cytosol of the neuronal perikarya and dendrites of wild-type mice. In contrast, the BSPT reaction product formazan was closely and discretely attached to endocellular membranes. In the intensely NADPH-diaphorase stained neurons of wild-type mice, 85% of the mitochondria were, at least partly, labelled for BSPT-formazan, whilst in the equivalent neurons of mutant mice, only 13% of mitochondria were NADPH-diaphorase positive. Related to the NADPH-diaphorase activity in the principal neurons of wild-type mice, only 10% of membranes of the endoplasmic reticulum, 27% of mitochondrial membranes and 26% of the nuclear envelope exhibited NADPH-diaphorase activity in the mutant mice. Our findings with the BSPT histochemistry suggest that residues of NADPH-diaphorase positivity in mutant mice are attributed to the alternative splice isoforms beta and/or gamma of neuronal nitric oxide synthase. The splice isoform a is located predominantly at the membranes of the endoplasmic reticulum.
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PMID:Ultrastructural localization of neuronal nitric oxide synthase in the laterodorsal tegmental nucleus of wild-type and knockout mice. 1061 9

Light and electron microscopy was used to study the distribution and changes of NADPH-diaphorase in the cutaneous nerve biopsy specimens in different periods of diphtheritic polyneuropathy (DP). there was a reduction in the reaction rate of the enzyme in Schwann's cells of the destructively changed nerve fibers and an increase in the remyelinated nerve fibers. The enzyme is located on the nuclear and endoplasmic reticulum membranes and ribosomes. It is suggested that there is an association of the synthesis of nitric oxide with the myelin-producing function of Schwann's cells.
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PMID:[The ultrastructural localization of NO-synthase NADPH diaphorase in a peripheral nerve and its change in diphtheritic polyneuropathy]. 1083 14

It has recently been suggested that, in addition to nitric oxide (NO), carbon monoxide (CO) is an important gaseous messenger which might be involved in vertebrate olfactory transduction because its effects include activation of guanylyl cyclase and the formation of cGMP. As there is no information regarding the presence of heme oxygenase-2 -- the constitutive isoform of the heme oxygenase system -- in olfactory neurons of non-rodent species, we have investigated the distribution pattern of heme oxygenase-2 in the olfactory epithelium of the bovine, a representative of macrosmatics. Localization of nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) activity of the olfactory epithelium was compared with heme oxygenase-2 and NO synthase (NOS) immunoreactivities in order to obtain possible hints at functional significance. NADPH-d activity was particularly intense in apical dendrites of receptor neurons. It was also found in Bowman glands and intraepithelial duct cells. Less intense, discrete NADPH-d activity was present also at intermediate and basal levels of the olfactory epithelium, corresponding to the layer of receptor neuron somata and basal cells. While heme oxygenase-2 activity mainly occurred in neuronal perikarya, a very intense NOS immunoreactivity, exclusively for the inducible isoform, was detected in the apical dendrites. Ultrastructurally, NADPH-d histochemistry showed distinct labelling of membranes, in particular of endoplasmic reticulum, mitochondria and nucleus. The coincident localization of the moderate NADPH-d activity and heme oxygenase-2 immunoreactivity in receptor cell perikarya suggest a functional association between NADPH-cytochrome P450 reductase and heme oxygenase-2. In contrast, dendritic localization of NADPH-d activity is topically and possibly functionally related to the presence of the inducible isoform of NOS. The results suggest that both CO and NO may be generated in bovine receptor neurons and thus involved in odorant stimulation. Based on immunocytochemical localization of synthesizing enzymes, NO might be regarded as a direct regulator of transduction related processes while CO might act as a modulator of the initial signal.
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PMID:Heme oxygenase-2 and nitric oxide synthase immunoreactivity of bovine olfactory receptor neurons and a comparison with the distribution of NADPH-diaphorase staining. 1094 53

The effects of the chronic ethanol treatment on the NOS-related NADPH-diaphorase activity were described in the mouse Leydig cells by means of transmission electron microscope. The recovery of the Leydig cells was also examined during a period of four weeks. About 10% of the Leydig cells showed various degrees of morphological alterations, consisting in increased number of lipid droplets, rarefaction and vacuolization of the cytoplasmic matrix. Other groups of Leydig cells (about 10%) revealed evident signs of degeneration. The NADPH-d activity was reduced both in apparently normal and injured Leydig cells and a moderate enzymatic reaction was only detected in the smooth endoplasmic reticulum. A week after the treatment an increased number of the degenerating Leydig cells and a further reduction of the enzymatic reaction were observed. Then, the Leydig cells showed a progressive recovery and four weeks after the treatment they exhibited a normal morphology and NADPH-d enzymatic reaction. These results demonstrated for the first time the inhibition of NOS activity in the Leydig cells after chronic ethanol administration.
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PMID:The ultrastructural localization of NADPH-diaphorase enzymatic activity in the Leydig cells of mouse. effects of ethanol administration. 1131 46


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