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:1.6.5.2 (NQO1)
6,196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Recent studies in physiology have suggested that part of the inhibitory nonadrenergic noncholinergic (iN-ANC) response of airway smooth muscle is mediated by nitric oxide (NO). To examine this point morphologically, the guinea pig respiratory tract was investigated histochemically for nicotinamide adenine dinucleotide phosphate (NADPH)-diaphorase (NADPH-d), a marker for NO synthase (NOS). In addition, coexpression of NOS and vasoactive intestinal peptide (VIP) or calcitonin gene-related peptide (CGRP) was studied using a combination of histochemistry for NADPH-d and immunohistochemistry for VIP or CGRP. Nerve fibers showing NADPH-d activity were abundantly observed in the respiratory tract. They were distributed throughout smooth-muscle bundles, lamina propria, submucosal glands, and around bronchial and pulmonary arteries. NADPH-d-containing nerve-cell bodies were occasionally found within airway ganglia. The colocalization study demonstrated that NADPH-d-containing nerve fibers frequently coincided with VIP-like immunoreactive nerve fibers but not with CGRP-like immunoreactive nerve fibers. Among nonneural tissues, NADPH-d activity was noticed in the endothelium of both bronchial and pulmonary vessels, and in the pleura. These observations indicated that NO may be produced by neurons and vascular endothelium of the guinea pig respiratory tract, and may function as a neuronal mediator as well as endothelium-derived relaxing factor (EDRF). Colocalization of NADPH-d and VIP-like immunoreactivity in nerve fibers suggested that NO and VIP may function as cotransmitters.
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PMID:NADPH-diaphorase activity as a marker for nitric oxide synthase in neurons of the guinea pig respiratory tract. 752 81

In the present study, nicotinamide adenine dinucleotide hydrogen phosphate-diaphorase (NADPH-d) histochemistry has been used as a marker for nitric oxide synthase (NOS). The colored reaction product, formazan, was localized in neuronal cell bodies, nerve fibers, and vascular endothelium in the thyroid of chick and mouse. In these two animal species, most of the NADPH-d-labeled neuronal cell bodies were found in the thyroid capsule and interfollicular connective tissue while some were associated with blood vessels. Most nerve fibers travelled with blood vessels supplying the thyroid gland, while a few of them were intimately associated with the thyroid follicular cells. Control sections not incubated with beta-NADPH failed to show labeling of the above structures. It is concluded that nitric oxide may play an important role in endocrine secretion by controlling the regional blood flow in the thyroid gland and by directly acting on the thyroid follicular cells.
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PMID:Localization of NADPH-diaphorase reactivity in the chick and mouse thyroid gland. 753 60

Portal hypertension (PHT) is characterized by splanchnic hyperemia caused by a reduction in mesenteric vascular resistance. Mediators of this hyperemia include nitric oxide (NO). This is based on several reports indicating a marked splanchnic hyporesponsiveness in PHT to vaso-constrictor stimuli, both in vitro and in vivo, and a subsequent reversal using specific inhibitors of NO synthase (NOS). The objective of this study was to determine directly if the generation of NO is altered in PHT vasculature. Thus, we compared NOS activity in the hyperemic vasculature of normal rabbits and rabbits with PHT (after undergoing partial portal vein ligation). Nicotinamide adenine dinucleotide phosphate diaphorase staining indicated the presence of NOS within the vascular endothelium. Ca(2+)-dependent NOS activity was significantly increased (P < .05) in PHT particulate fractions from the superior mesenteric artery and thoracic aorta, but not from the portal vein. There was no change in NOS activity within the cytosolic fractions. Arterial wall cyclic guanosine monophosphate (cGMP) levels and plasma nitrite levels were both significantly increased in PHT. These results show enhanced NOS activity in PHT hyperemic vessels concurrent with increased tissue cGMP levels. We conclude that enhanced NO synthesis contributes to the hyperdynamic circulation of PHT.
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PMID:Enhanced nitric oxide synthase activity in portal hypertensive rabbits. 754 37

Nitric oxide synthase activities in the facial motor nucleus were studied in rats after unilateral compression of the facial nerve. Using a radiometric assay which measured the total soluble nitric oxide synthase activities in the facial motor nucleus and the surrounding tissues, it was found that nitric oxide synthase activities were markedly increased during facial paralysis that resulted from compression of the facial nerve. The subsequent decrease in nitric oxide synthase activities between postoperative days 20 and 40 coincided with the recovery of facial functions. In contrast, staining with NADPH-diaphorase histochemistry revealed that the diaphorase activities in the facial motor neurons were markedly increased between days 20-40 when the total activities as measured biochemically were in decline. However, staining of the vascular endothelium was increased on postoperative day 7 when the total activity was high. It is suggested that the increase in total nitric oxide synthase activities immediately after facial nerve compression may be predominantly endothelial. Since the increase in neuronal NADPH-diaphorase reactivity coincided with the recovery of facial functions, increased neuronal nitric oxide synthase may be a contributing factor to the restoration of facial innervation. The results of this study show that biochemical measurements of soluble nitric oxide synthase activities in tissue homogenates and NADPH-diaphorase histochemical staining in tissue sections may represent two distinct populations of nitric oxide synthase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Compression of the facial nerve caused increased nitric oxide synthase activity in the facial motor nucleus. 754 97

Endothelial nitric oxide (NO) synthase, a unique NO synthase (NOS) isoform that is expressed constitutively by the vascular endothelium both in vivo and in vitro, is believed to be essential to systemic and/or local vascular integrity. NOS expression by endothelial cells may indicate vascular activation. We successfully established a simple method for the culture of microvascular endothelial cells from a small amount of tissue and investigated ulcerative colitis (UC), in which condition vascular factors have not been studied extensively. We cultured endothelial cells from the mesenteries of surgical patients with UC and assayed NOS activity by reduced nicotinamide adenine dinucleotide phosphate (NADPH)-diaphorase histochemistry. Strong NOS activity was demonstrated in the cells from all UC patients (5/5), whereas no activity was detected in the cells from human umbilical veins and the mesenteries of colon cancer patients (0/10 and 0/5, respectively). This strong NOS activity was not diminished by incubation with a high concentration of glucocorticoid, suggesting that it was constitutive. These results indicate a close relationship of vascular activation (high NOS activity) with the pathogenesis of UC.
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PMID:High nitric oxide synthase activity in endothelial cells in ulcerative colitis. 755 Aug 72

The nasal mucosa plays an important role in defense of the lung against harmful agents. It has been suggested that this is partly mediated by the production of nitric oxide (NO). We have investigated the localization of the messenger ribonucleic acids (MRNAs) for human endothelial NO synthase (Type III NOS) and inducible NO synthase (Type II NOS) and the immunoreactivities of these enzymes in human nasal mucosa by immunohistochemistry, in situ hybridization, and reduced nicotinamide adenine diphosphate (NADPH) diaphorase histochemistry. Inferior nasal turbinates were obtained from 27 patients at the time of surgery for local disease. Strong immunostaining for Type III NOS was localized to vascular endothelium, surface epithelium, and submucosal glands in all subjects. Moderate immunostaining for Type II NOS was seen in surface epithelium; glandular, inflammatory, and vascular endothelial cells; and smooth-muscle cells in the specimens from patients with chronic rhinitis only. In situ hybridization showed expression of the mRNA for Type III NOS in similar sites to those shown by immunohistochemistry, whereas the mRNA for Type II NOS was predominantly localized to inflammatory cells. The sites of NOS expression were further confirmed by NADPH histochemical staining. These findings demonstrate the cellular expression of NOS in the human nasal mucosa and suggest a possible role for Types II and III NO synthase in the regulation of blood flow, nasal secretion, and ciliary movement in health and disease.
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PMID:Expression of nitric oxide synthase in the human nasal mucosa. 856 42

The ultimobranchial glands of 20 chickens, aged 2-3 months, were investigated for their nicotinamide adenine dinucleotide hydrogen phosphate-diaphorase (NADPH-d) reactivity and the distribution of nitric oxide synthase (NOS), using NADPH-d histochemistry and NOS immunocytochemistry respectively. Formazan, the blue reaction product of NADPH-d, was localised in the neuronal cell bodies and nerve fibres. Most of the cell bodies were found in the parenchyma. Some of them occurred in the wall of the ultimobranchial cysts, and a few in the immediate vicinity of the blood vessels. Labelled nerve fibres mostly travelled with blood vessels, while few of them appeared in the cystic lining. In addition to neuronal profiles, some C cells, cystic lining, and vascular endothelium were also labelled. NOS staining was found in neuron-like cells and fibres that were confirmed as neurons in adjacent sections stained with antibodies against neuron-specific enolase. It was also detected in cystic lining and in some C cells, but not in vascular endothelium. The distribution patterns of NADPH-d and NOS suggest that NO may play a role in the regulation of the secretory activity of and the blood flow through the ultimobranchial glands.
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PMID:Localization of nitrergic neuronal and non-neuronal cells in the ultimobranchial glands of the chicken. 874 56

The bursa of Fabricius of 24 chickens, 2-4 weeks old, was investigated to determine the distribution of nicotinamide adenine dinucleotide hydrogen phosphate-diaphorase (NADPH-d) staining and nitric oxide synthase (NOS) antigen, by use of NADPH-d histochemistry and NOS immunohistochemistry, respectively. NADPH-d reaction product was localised in neuronal cell bodies and nerve fibres. The stained cell bodies were predominantly in the different bursal compartments; some occurred in the wall and between the lymphoid follicles, and some in the immediate vicinity of blood vessels. Stained nerve fibres travelled mostly with blood vessels, but many were also observed in the connective tissue of the bursa, independent of blood vessels, and some in contact with the lymphoid follicle and interfollicular epithelium. In addition to neuronal profiles, the interfollicular epithelium of the plicae, and the vascular endothelium were densely stained, and lymphocytes were moderately labelled. NOS immunoreactivity was found in neuron-like cells and fibres which were confirmed to be neuronal in adjacent sections stained with antibodies raised against neuron-specific enolase. It was also detected in interfollicular epithelium and lymphocytes but not in vascular endothelium. The distribution patterns of NADPH-d and NOS suggest that nitric oxide (NO) may play a role in the regulation of the secretory activity of interfollicular epithelium and the blood flow through the bursa.
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PMID:Histochemical and immunohistochemical localisation of nitrergic neuronal and non-neuronal cells in the bursa of Fabricius of the chicken. 876 63

NADPH diaphorase histochemistry has been used extensively for detecting nitric oxide synthase (NOS) activity in various cell types including neuronal cell bodies, vascular endothelium, cells of the immune system and epithelial cells. The use of the diaphorase technique in cell cultures to study the induction of NOS has not been investigated. In this paper we report the use of diaphorase histochemistry as a good marker for the detection of NOS activity in cultured cells. This technique can be used in conjunction with other established techniques to determine the presence and activity of NOS in cultured cells.
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PMID:Histochemical method for detecting nitric oxide synthase activity in cell cultures. 906 7

We investigated the localization of nitric oxide synthase in the pancreas of the dog in comparison to the rat by the methods of immunocytochemistry using antineuronal type nitric oxide synthase serum and histochemistry using NADPH-diaphorase activity. In both species, the most intense staining was observed in neuronal cell bodies and fibers in the pancreas and nitric oxide synthase immunoreactivity was completely colocalized with NADPH-diaphorase activity. However, there were differences of the distribution between the two species. In the dog pancreas, immuno- and NADPH-diaphorase-positive nerve fibers were numerous around pancreatic ducts and moderate around the arteries and the acini but few in the islets. In contrast, in the rat pancreas, immuno- and diaphorase-positive fibers were fewer around the pancreatic ducts and acini and more abundant in the islets. The expression ratio of NADPH-diaphorase in intrapancreatic ganglion cell bodies that were scattered in the interlobular connective tissue was low to moderate (28.1% in the right lobe, 49.5% in the left lobe) in the dog, while the ratio in rat pancreas was very high in both lobes of the pancreas (about 86%). Except for neuronal staining, weak NADPH-diaphorase-positive reactions were detected in the vascular endothelial cells of the pancreas in both species. In rat islet cells, weak neuronal type nitric oxide synthase immunoreactivity was observed; however, in dog islet cells, no immunoreactivity was detected. These results suggest that nitric oxide in the pancreas is derived from vascular endothelium and neuronal tissue in both species and that the neuronal nitrergic regulation of the exocrine and endocrine pancreas is different between the species.
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PMID:Comparative distribution of nitric oxide synthase (NOS) in pancreas of the dog and rat: immunocytochemistry of neuronal type NOS and histochemistry of NADPH-diaphorase. 912 23


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