Academic literature on the topic 'Neuronal nitric oxide synthase (nNOS)'
Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles
Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Neuronal nitric oxide synthase (nNOS).'
Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.
You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.
Journal articles on the topic "Neuronal nitric oxide synthase (nNOS)"
1
Kourosh-Arami, Masoumeh, Nasrin Hosseini, Monireh Mohsenzadegan, Alireza Komaki, and Mohammad Taghi Joghataei. "Neurophysiologic implications of neuronal nitric oxide synthase." Reviews in the Neurosciences 31, no. 6 (August 27, 2020): 617–36. http://dx.doi.org/10.1515/revneuro-2019-0111.
Full textAbstract:
AbstractThe molecular and chemical properties of neuronal nitric oxide synthase (nNOS) have made it a key mediator in many physiological functions and signaling transduction. The NOS monomer is inactive, but the dimer form is active. There are three forms of NOS, which are neuronal (nNOS), inducible (iNOS), and endothelial (eNOS) nitric oxide synthase. nNOS regulates nitric oxide (NO) synthesis which is the mechanism used mostly by neurons to produce NO. nNOS expression and activation is regulated by some important signaling proteins, such as cyclic adenosine monophosphate (cAMP) response element-binding protein (CREB), calmodulin (CaM), heat shock protein 90 (HSP90)/HSP70. nNOS-derived NO has been implicated in modulating many physiological functions, such as synaptic plasticity, learning, memory, neurogenesis, etc. In this review, we have summarized recent studies that have characterized structural features, subcellular localization, and factors that regulate nNOS function. Finally, we have discussed the role of nNOS in the developing brain under a wide range of physiological conditions, especially long-term potentiation and depression.
2
Huber, Andrea, Dieter Saur, Manfred Kurjak, Volker Schusdziarra, and Hans-Dieter Allescher. "Characterization and splice variants of neuronal nitric oxide synthase in rat small intestine." American Journal of Physiology-Gastrointestinal and Liver Physiology 275, no. 5 (November 1, 1998): G1146—G1156. http://dx.doi.org/10.1152/ajpgi.1998.275.5.g1146.
Full textAbstract:
The aim of this study was to characterize neuronal nitric oxide synthase (nNOS) activity and 5′-end splice variants in rat small intestine. nNOS was predominantly expressed in the longitudinal muscle layer, with attached myenteric plexus (LM-MP). The biochemical properties of NOS activity in enriched nerve terminals resemble those of nNOS isolated from the brain. Western blot analysis of purified NOS protein with an nNOS antibody showed a single band in the particulate fraction and three bands in the soluble fraction. Rapid amplification of 5′ cDNA ends-PCR revealed the presence of three different 5′-end splice variants of nNOS. Two variants encode for nNOSα, which has a specific domain for membrane association. The third variant encodes for nNOSβ, which lacks the domain for membrane association and should therefore be soluble. nNOS is predominantly expressed in LM-MP and can be enriched in enteric nerve terminals. We present the first evidence that three 5′-end splice variants of nNOS encoding two different proteins are expressed in rat small intestine. These two nNOS enzymes exhibit different subcellular locations and might be implicated in different biological functions.
3
Rao, Y. Manjula, Arun Chaudhury, and Raj K. Goyal. "Active and inactive pools of nNOS in the nerve terminals in mouse gut: implications for nitrergic neurotransmission." American Journal of Physiology-Gastrointestinal and Liver Physiology 294, no. 3 (March 2008): G627—G634. http://dx.doi.org/10.1152/ajpgi.00519.2007.
Full textAbstract:
Nitric oxide (NO) is responsible for nitrergic neurotransmission in the gut, and its release is dependent on its de novo synthesis by neuronal nitric oxide synthase (nNOS). The magnitude of NO synthesis and release during neurotransmission may be related to the fraction of catalytically active nNOS out of a larger pool of inactive nNOS in the nerve terminals. The purpose of the present study was to identify catalytically active and inactive pools of nNOS in the varicosities from mouse gut. Enteric varicosities were confirmed as nitrergic by colocalization of nNOS with the nerve varicosity marker synaptophysin. Low-temperature SDS-PAGE of these varicosity extracts showed 320-, 250-, and 155-kDa bands when blotted with anti-nNOS1422–1433 and 320- and 155-kDa bands when blotted with anti-nNOS1–20 antibodies, respectively. The 320- and 155-kDa bands represent dimers and monomers of nNOSα; the 250- and 135-kDa bands represent dimers and monomers of nNOSβ. Immunoprecipitation with calmodulin (CaM) showed that a portion of nNOSα dimer was bound with CaM. On the other hand, a portion of nNOSα dimer, nNOSβ dimer, and all monomers lacked CaM binding. The CaM-lacking nNOS fractions reacted with anti-serine 847-phospho-nNOS. In vitro assays of NO production revealed that only the CaM-bound dimeric nNOSα was catalytically active; all other forms were inactive. We suggest that the amount of catalytically active nNOSα dimers may be regulated by serine 847 phosphorylation and equilibrium between dimers and monomers of nNOSα.
4
Di Giacomo, C., V. Sorrenti, L. Salerno, V. Cardile, F. Guerrera, M. A. Siracusa, M. Avitabile, and A. Vanella. "Novel Inhibitors of Neuronal Nitric Oxide Synthase." Experimental Biology and Medicine 228, no. 5 (May 2003): 486–90. http://dx.doi.org/10.1177/15353702-0322805-11.
Full textAbstract:
Selective inhibitors of neuronal nitric oxide synthase (nNOS), which are devoid of any effect on the endothelial isoform (eNOS), may be required for the treatment of some neurological disorders. In our search for novel nNOS inhibitors, we recently described some 1-[(Aryloxy)ethyl]-1 H-imidazoles as interesting molecules for their selectivity for nNOS against eNOS. This work reports a new series of 1-[(Aryloxy)alkyl]-1 H-imidazoles in which a longer methylene chain is present between the imidazole and the phenol part of molecule. Some of these molecules were found to be more potent nNOS inhibitors than the parent ethylenic compounds, although this increase in potency resulted in a partial loss of selectivity. The most interesting compound was investigated to establish its mechanism of action and was found to interact with the tetrahydrobiopterin (BH4) binding site of nNOS, without interference with any other cofactors or substrate binding sites.
5
YONEYAMA, Hirohito, Akira YAMAMOTO, and Hiroaki KOSAKA. "Neuronal nitric oxide synthase generates superoxide from the oxygenase domain." Biochemical Journal 360, no. 1 (November 8, 2001): 247–53. http://dx.doi.org/10.1042/bj3600247.
Full textAbstract:
When l-arginine is depleted, neuronal nitric oxide synthase (nNOS) has been reported to generate superoxide. A flavoprotein module construct of nNOS has been demonstrated to be sufficient for superoxide production. In contrast, nNOS was reported not to be involved in superoxide formation, because such formation occurred with a mixture of the boiled enzyme and redox-active cofactors. We aimed to resolve these controversial issues by examining superoxide generation, without the addition of redox-active cofactors, by recombinant wild-type nNOS and by C415A-nNOS, which has a mutation in the haem proximal site. In a superoxide-sensitive adrenochrome assay, the initial lag period of C415A-nNOS was increased 2-fold compared with that of native nNOS. With ESR using the spin trap 5,5-dimethyl-1-pyrroline-N-oxide, prominent signals of the superoxide adduct were obtained with wild-type nNOS, whereas an enzyme preparation boiled for 5min did not produce superoxide. Higher concentrations of NaCN (10mM) decreased superoxide formation by 63%. Although the activity of the reductase domain was intact, superoxide generation from C415A-nNOS was decreased markedly, to only 10% of that of the wild-type enzyme. These results demonstrate that nNOS truly catalyses superoxide formation, that this involves the oxygenase domain, and that full-length nNOS hinders the reductase domain from producing superoxide.
6
González-Martínez, Jorge A., Gabriel Möddel, Zhong Ying, Richard A. Prayson, William E. Bingaman, and Imad M. Najm. "Neuronal nitric oxide synthase expression in resected epileptic dysplastic neocortex." Journal of Neurosurgery 110, no. 2 (February 2009): 343–49. http://dx.doi.org/10.3171/2008.6.17608.
Full textAbstract:
Object Nitric oxide has been associated with epileptogenesis. Previous studies have shown increased expression of N-methyl-d-aspartate (NMDA) subunit NR2B receptors in epileptic dysplastic human neocortex. The expression of neuronal nitric oxide synthase (nNOS), and its relation to this subunit NR2B in epileptic dysplastic tissue has never been addressed. Methods Ten patients with medically intractable epilepsy caused by focal cortical dysplasia (CD), and 2 patients with mesial temporal sclerosis (control group) underwent pre- and/or intraoperative invasive monitoring evaluations. Cortical samples from epileptogenic and nonepileptogenic areas were collected from each patient intraoperatively. Samples were processed for cresyl violet staining, immunocytochemical tests with nNOS, NeuN, and NR2B, and immunofluorescence analyses to evaluate colocalized immunoreactivity between nNOS and NR2B. Results . All samples obtained in the patients with epilepsy revealed CD in various degrees. In the nonepileptic sample group, cresyl violet staining revealed normal cortical architecture in 9 samples, but a mild degree of CD in 3. The density and intensity of nNOS-stained neurons was remarkably increased in the epileptic tissue compared with nonepileptic samples (p < 0.05). Two types of nNOS-stained neurons were identified: Type I, expressing strong nNOS immunoreactivity in larger neurons; and Type II, expressing weak nNOS immunoreactivity in slightly smaller neurons. Different from Type I neurons, Type II nNOS-stained neurons revealed immunoreactivity colocalized with NR2B antibody. Conclusions The overexpression of nNOS in the epileptic samples and the immunoreactivity colocalization between nNOS and NR2B may suggest a possible role of nNOS and NO in the pathophysiological mechanisms related to in situ epileptogenicity.
7
Premaratne, Shyamal, Chun Xue, John M. McCarty, Muhammad Zaki, Robert W. McCuen, Roger A. Johns, Wolfgang Schepp, et al. "Neuronal nitric oxide synthase: expression in rat parietal cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 280, no. 2 (February 1, 2001): G308—G313. http://dx.doi.org/10.1152/ajpgi.2001.280.2.g308.
Full textAbstract:
Nitric oxide synthases (NOS) are enzymes that catalyze the generation of nitric oxide (NO) from l-arginine and require nicotinamide adenine dinucleotide phosphate (NADPH) as a cofactor. At least three isoforms of NOS have been identified: neuronal NOS (nNOS or NOS I), inducible NOS (iNOS or NOS II), and endothelial NOS (eNOS or NOS II). Recent studies implicate NO in the regulation of gastric acid secretion. The aim of the present study was to localize the cellular distribution and characterize the isoform of NOS present in oxyntic mucosa. Oxyntic mucosal segments from rat stomach were stained by the NADPH-diaphorase reaction and with isoform-specific NOS antibodies. The expression of NOS in isolated, highly enriched (>98%) rat parietal cells was examined by immunohistochemistry, Western blot analysis, and RT-PCR. In oxyntic mucosa, histochemical staining revealed NADPH-diaphorase and nNOS immunoreactivity in cells in the midportion of the glands, which were identified as parietal cells in hematoxylin and eosin-stained step sections. In isolated parietal cells, decisive evidence for nNOS expression was obtained by specific immunohistochemistry, Western blotting, and RT-PCR. Cloning and sequence analysis of the PCR product confirmed it to be nNOS (100% identity). Expression of nNOS in parietal cells suggests that endogenous NO, acting as an intracellular signaling molecule, may participate in the regulation of gastric acid secretion.
8
ROCZNIAK, AGNES, JAMES N. FRYER, DAVID Z. LEVINE, and KEVIN D. BURNS. "Downregulation of Neuronal Nitric Oxide Synthase in the Rat Remnant Kidney." Journal of the American Society of Nephrology 10, no. 4 (April 1999): 704–13. http://dx.doi.org/10.1681/asn.v104704.
Full textAbstract:
Abstract. Chronic renal failure is associated with disturbances in nitric oxide (NO) production. This study was conducted to determine the effect of 5/6 nephrectomy (5/6 Nx) on expression of intrarenal neuronal nitric oxide synthase (nNOS) in the rat. In normal rat kidney, nNOS protein was detected in the macula densa and in the cytoplasm and nuclei of cells of the inner medullary collecting duct by both immunofluorescence and electron microscopy. Western blot analysis revealed that 2 wk after 5/6 Nx, there were significant decreases in nNOS protein expression in renal cortex (sham: 95.42 ± 15.60 versus 5/6 Nx: 47.55 ± 12.78 arbitrary units, P < 0.05, n = 4) and inner medulla (sham: 147.70 ± 26.96 versus 5/6 Nx: 36.95 ± 17.24 arbitrary units, P < 0.005, n = 8). Losartan treatment was used to determine the role of angiotensin II (AngII) AT1 receptors in the inhibition of nNOS expression in 5/6 Nx. Losartan had no effect on the decreased expression of nNOS in the inner medulla, but partially increased nNOS protein expression in the cortex of 5/6 Nx rats. In contrast, in sham rats losartan significantly inhibited nNOS protein expression in the cortex (0.66 ± 0.04-fold of sham values, P < 0.05, n = 6) and inner medulla (0.74 ± 0.12-fold of sham values, P < 0.05, n = 6). nNOS mRNA was significantly decreased in cortex and inner medulla from 5/6 Nx rats, and the effects of losartan on nNOS mRNA paralleled those observed on nNOS protein expression. These data indicate that 5/6 Nx downregulates intrarenal nNOS mRNA and protein expression. In normal rats, AngII AT1 receptors exert a tonic stimulatory effect on expression of intrarenal nNOS. These findings suggest that the reduction in intrarenal nNOS expression in 5/6 Nx may play a role in contributing to hypertension and altered tubular transport responses in chronic renal failure.
9
Wang, Xianhong, Ming Lu, Yongzong Gao, Andreas Papapetropoulos, William C. Sessa, and Wenhui Wang. "Neuronal nitric oxide synthase is expressed in principal cell of collecting duct." American Journal of Physiology-Renal Physiology 275, no. 3 (September 1, 1998): F395—F399. http://dx.doi.org/10.1152/ajprenal.1998.275.3.f395.
Full textAbstract:
We used the RT-PCR technique and immunocytochemical methods to determine the expression of endothelial nitric oxide synthase (eNOS) or neuronal nitric oxide synthase (nNOS) in the cortical collecting duct (CCD) in rats on high-K+ diet. The microdissected CCDs of the rat kidney were lysed, and RT-PCR was carried out using rat nNOS and eNOS gene-specific primers. Southern analysis showed the presence of mRNA of nNOS but not eNOS in the CCD. The presence of nNOS in the CCD was further confirmed by light microscopy. We used the polyclonal nNOS antibody in immunocytochemical studies of the isolated CCD. We found that immunoreactivity to nNOS was present in the CCD and heterogeneous with positive and negative immunostaining. We performed the immunocytochemical studies in the split-open CCD and found that the immunoreactivity to nNOS was detected only in principal cells but not in intercalated cells. We conclude that nNOS is expressed in the rat CCD in rats on high-K+ diet. The presence of nNOS in the CCD is heterogeneous and mainly located in principal cells.
10
Smith, Cheryl A., Beth Santymire, Aaron Erdely, Vasuki Venkat, György Losonczy, and Chris Baylis. "Renal nitric oxide production in rat pregnancy: role of constitutive nitric oxide synthases." American Journal of Physiology-Renal Physiology 299, no. 4 (October 2010): F830—F836. http://dx.doi.org/10.1152/ajprenal.00300.2010.
Full textAbstract:
Functional studies show that increased renal nitric oxide (NO) mediates the renal vasodilation and increased glomerular filtration rate that occur during normal pregnancy. We investigated whether changes in the constitutive NO synthases (NOS), endothelial (eNOS) and neuronal (nNOS), were associated with the increased renal NO production in normal midterm pregnancy in the rat. In kidneys from midterm pregnant (MP: 11–13 days gestation), late-term pregnant (LP: 18–20 days gestation), and similarly aged virgin (V) rats, transcript and protein abundance for eNOS and the nNOSα and nNOSβ splice variants, as well as the rate of l-arginine-to-l-citrulline conversion, were determined as a measure of NOS activity. At MP, renal cortical abundance of the total eNOS protein and phosphorylated (Ser1177) eNOS was reduced, and l-arginine-to-l-citrulline conversion in the cortical membrane fraction was decreased; these declines were also seen in LP. There were no changes in the eNOS transcript. In contrast, l-arginine-to-l-citrulline conversion in the soluble fraction of renal cortex increased at MP and then declined at LP. This MP increase was ablated by S-methylthiocitrulline, a nNOS inhibitor. Using Western blotting, we did not detect a change in the protein abundance or transcript of the 160-kDa nNOSα, but protein abundance and transcript of the nNOSβ were increased at MP in cortex. Collectively, these studies suggest that the soluble nNOSβ is responsible for the increased renal cortical NO production during pregnancy.
Dissertations / Theses on the topic "Neuronal nitric oxide synthase (nNOS)"
1
Cheung, Nathan Yiutung. "Serotonin receptor and neuronal nitric oxide synthase expression in the rat brain : implications for MDMA toxicity." Thesis, King's College London (University of London), 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.368095.
Full text
2
Lu, Chieh-Ju. "Neuronal nitric oxide synthase-CAPON regulation of cardiac sympathetic activity in the development of hypertension." Thesis, University of Oxford, 2015. http://ora.ox.ac.uk/objects/uuid:1204dec9-9f09-458d-b361-c8d14589fcd1.
Full textAbstract:
The studies presented in this thesis were undertaken to investigate the cellular and molecular mechanisms responsible for sympathetic hyperactivity that is observed in the Spontaneous Hypertensive Rat (SHR) and whether these abnormalities arise even before the onset of hypertension. Moreover, selected molecular candidates related to oxidative state in cardiac autonomic signalling have been explored for their potential therapeutic effects. Chapter One is an overview of (i) the relevance of autonomic dysfunction in cardiovascular disease in both human and animal models, (ii) the physiological basis of cardiac sympathetic neurotransmission, (iii) the neuromodulators of peripheral cardiac sympathetic-vagal balance discussed along with how they may be involved in cardiac adrenergic control of neurotransmission and NO-cGMP signalling. This develops the formulation of the specific aims of the thesis. Chapter Two outlines a detailed rationale for the experimental approach taken to (i) characterise protein expression in the pre-hypertensive animal model with immunohistochemistry and Western blotting, (ii) manipulate selected gene expression to amplify NO-cGMP signalling in vivo and in vitro via viral gene transfer, (iii) investigate calcium handling in cardiac sympathetic stellate neurons with calcium imaging , (iv) measure cardiac noradrenergic neurotransmission from double atria using radioactive-labelled [3H]-noradrenaline. Chapter Three demonstrated abnormal NO-cGMP signalling in pre-hypertensive SHRs. Endogenous nNOS protein residing in both cardiac parasympathetic and sympathetic neurons was significantly lower in the pre-hypertensive SHR compared to aged-matched WKYs. This was associated with lower cGMP levels. An enhanced depolarization evoked [Ca2+]i transient was observed in cardiac stellate neurons from pre-hypertensive SHR when compared with the WKY, an effect that was reversed by nNOS or sGC inhibition. Chapter Four investigated the role of nNOS and brain natriuretic peptide (BNP) in cGMP signalling pathways. Gene transfer of nNOS via adenoviral vector in SHR cardiac sympathetic neurons increased cGMP concentration and normalised neuronal calcium handling during depolarization. BNP significantly reduces [3H]- noradrenaline release. Overexpression of PDE2 which facilitates the breakdown of cGMP caused an increase in [3H]- noradrenaline release in response to field stimulation and also prevented the inhibitory action of BNP. Chapter Five examined the role of the nNOS adaptor protein, CAPON in NO-cGMP signalling. Endogenous CAPON protein is present in cardiac sympathetic neurons in the WKY, and is significantly reduced in pre-hypertensive SHR cardiac neurons. Artificial up-regulation of cardiac sympathetic CAPON via targeted gene transfer directly attenuated neuronal Ca2+ transients, resulting in decreased noradrenaline release in the SHR. Chapter Six is a concluding discussion summarising the main findings from this thesis, placing them in a physiological context and discussing avenues for further research.
3
Bird, Diane Carol. "An investigation into the role of neuronal nitric oxide synthase (nNOS) in the phencyclidine mouse model of schizophrenia." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape4/PQDD_0015/MQ57249.pdf.
Full text
4
Barua, Anupama. "The role of neuronal nitric oxide synthase (nNOS) in ischaemia/reoxygenation-induced injury and in protection of the mammalian myocardium." Thesis, University of Leicester, 2010. http://hdl.handle.net/2381/8754.
Full textAbstract:
Background: In physiological condition, NO is produced by two constitutive NOS isoform; eNOS and nNOS. Both isoforms have specific cellular locations and although the role of eNOS in myocardial ischaemic injury and in cardioprotection has been thoroughly addressed, but the role of nNOS remains unclear. Therefore, the aims of the thesis were to: (i) investigate the role of nNOS in ischaemia/reoxygenation-induced injury, (ii) determine whether its effect is species-dependent, (iii) elucidate the relationship of nNOS with mitoKATP channels and p38MAPK, two key components of IP and (iv) investigate whether modulation of the NO metabolism can overcome the unresponsiveness of the diabetic myocardium to IP. Methods and Results: Ventricular myocardial slices from rats and mice, nNOS knockout mice, and also from human right atrial slices were subjected to 90min ischaemia and 120min reoxygenation (37°C). Muscles were randomized to receive various treatments. Both the provision of exogenous NO and the inhibition of endogenous NO production significantly reduced tissue injury (creatine kinase release, cell necrosis and apoptosis), an effect that was species–independent. The protection seen with nNOS inhibition was as potent as that of IP, however, in nNOS-knocked out mice the cardioprotective effect of non-selective NOS (L-NAME) and selective nNOS inhibition (TRIM) and also that of IP was blocked while the benefit of exogenous NO remained intact. Additional studies revealed that the cardioprotection afforded by of exogenous NO and by inhibition of nNOS were unaffected by the mitoKATP channel blocker 5-HD although it was abrogated by p38MAPK blocker SB203580. Finally, in diabetic myocardium, IP did not decrease CK release neither reduced cell necrosis or apoptosis. In diabetic myocardium NO donor SNAP, inhibitor L-NAME and TRIM significantly reduced CK leakage, cell necrosis and apoptosis. Conclusions: nNOS plays a dual role in ischaemia/reoxygenation on that its presence is necessary to afford cardioprotection by IP but its inhibition reduces myocardial ischaemic injury. The role of nNOS is species-independent and exerted downstream of the mitoKATP channels and upstream of p38MAPK. Moreover, both the provision of exogenous NO and the suppression of endogenous NO production resulted in potent protection of diabetic human myocardium, overcoming the unresponsiveness of these tissues to IP.
5
Balda, Mara A. "Ontogeny- and Sex-Dependent Contributions of the Neuronal Nitric Oxide Synthase (nNOS) Gene to Rewarding and Psychomotor Stimulating Effects of Cocaine." Scholarly Repository, 2009. http://scholarlyrepository.miami.edu/oa_dissertations/257.
Full textAbstract:
Multiple interactions between dopamine (DA), glutamate, and nitric oxide (NO) in mesolimbic and corticostriatal circuits suggest that NO may play a critical role in cocaine-induced behavioral and neural plasticity. Clinical and preclinical studies have revealed that females and adolescents display unique vulnerabilities to the behavioral and neurochemical effects of cocaine as a result of sex-dependent and ontogeny-dependent differences in dopaminergic systems. Thus, my research objectives were to investigate the contributions of the neuronal nitric oxide synthase (nNOS) gene, ontogeny, and gender on the rewarding and sensitizing effects of cocaine. I found that nNOS significantly influences the rewarding aspects of cocaine in adolescent mice and adult male mice (i.e., major deficits in several phases of cocaine conditioned place preference (CPP) were detected in nNOS knockout (KO) adolescent mice and nNOS KO adult male mice). However, the contribution of nNOS was sex-dependent as CPP phases were normal in KO adult females. In contrast to CPP, I found a major ontogeny-dependent contribution of nNOS to the sensitizing effects of cocaine. Namely, while nNOS is essential for the development of behavioral sensitization in adult males, this type of behavioral plasticity develops independently of nNOS during adolescence. The contribution of nNOS was once again sex-dependent as behavioral sensitization was normal in adult KO females. Together, this line of investigation has revealed that the NO-signaling pathway has a) a sex-dependent role in the neuroplasticity underlying cocaine CPP and b) a sex-dependent and ontogeny-dependent influence on cocaine-induced behavioral sensitization. Stereological and western blot analysis revealed that a sensitizing regimen of cocaine resulted in an increase in nNOS and tyrosine hydroxylase (TH) immunoreactivity in the dorsal striatum (dST) of adult, but not adolescent, wild-type (WT) male mice. In the absence of nNOS, dopaminergic neurons in the ventral tegmental area (VTA) were severely reduced and cocaine caused a downregulation of dST TH suggesting that nitrergic levels modulate TH. Thus, the finding that nNOS is essential for the development of sensitization in adulthood, but not adolescence, together with the fact that cocaine upregulated nNOS and TH in the dST in adult, but not adolescent mice, strongly suggest that the nitrergic system underlies behavioral sensitization through modulation of the dopaminergic system in adulthood. These findings suggest different approaches in the clinical treatment of drug craving and drug-seeking behavior in adolescent and adult patients.
6
Schonhoff, Christopher M. "The Regulation of nNOS During Neuronal Differentiation and the Effect of Nitric Oxide on Hdm2-p53 Binding: a Dissertation." eScholarship@UMMS, 2000. https://escholarship.umassmed.edu/gsbs_diss/57.
Full textAbstract:
Nitric oxide is a ubiquitous signaling molecule with both physiological and pathological functions in biological systems. Formed by the enzymatic conversion of arginine to citrulline, NO, has known roles in circulatory, immune and nervous tissues. In the nervous system nitric oxide has been implicated in long-term potentiation, neurotransmitter release, channel function, neuronal protection and neuronal degeneration. Much of our work has focused on yet another role for nitric oxide in cells, namely, neuronal differentiation.
During development, neuronal differentiation is closely coupled with cessation of proliferation. We use nerve growth factor (NGF)-induced differentiation of PC12 pheochromocytoma cells as a model and find a novel signal transduction pathway that blocks cell proliferation. Treatment of PC12 cells with NGF leads to induction of nitric oxide synthase (NOS). The resulting nitric oxide (NO) acts as a second messenger, activating the p21(WAF1) promoter and inducing expression of p21(WAF1) cyclin-dependent kinase inhibitor. NO activates the p21(WAF1) promoter by p53-dependent and p53-independent mechanisms. Blocking production of NO with an inhibitor of NOS reduces accumulation of p53, activation of the p21(WAF1) promoter, expression of neuronal markers, and neurite extension. To deternine whether p21(WAF1) is required for neurite extension, we prepared a PC12 line with an inducible p21(WAF1) expression vector. Blocking NOS with an inhibitor decreases neurite extension, but induction of p21(WAF1) with isopropyl-1-thio-beta-D-galactopyranoside restored this response. Levels of p21(WAF1) induced by isopropyl-1-thio-beta-D-galactopyranoside were similar to those induced by NGF. Therefore, we have identified a signal transduction pathway that is activated by NGF; proceeds through NOS, p53 and p21(WAF1) to block cell proliferation; and is required for neuronal differentiation by PC12 cells.
In further studies of this pathway, we have examined the role of MAP kinase pathways in neuronal nitric oxide synthase (nNOS) induction during the differentiation of PC12 cells. In NGF-treated PC12 cells, we find that nNOS is induced at RNA and protein levels, resulting in increased NOS activity. We note that neither nNOS mRNA, nNOS protein nor NOS activity is induced by NGF treatment in cells that have been infected with a dominant negative Ras adenovirus. We have also used drugs that block MAP kinase pathways and assessed their ability to inhibit nNOS induction. Even though U0126 and PD98059 are both MEK inhibitors, we find that U0126, but not PD98059, blocks nNOS induction and NOS activity in NGF-treated PC12 cells. Also, the p38 kinase inhibitor, SB 203580, does not block nNOS induction in our clone of PC12 cells. Since the JNK pathway is not activated in NGF-treated PC12 cells, we determine that the Ras-ERK pathway and not the p38 or JNK pathway is required for nNOS induction in NGF-treated PC12 cells. We find that U0l26 is much more effective than PD98059 in blocking the Ras-ERK pathway, thereby explaining the discrepancy in nNOS inhibition. We conclude that the Ras-ERK pathway is required for nNOS induction.
The activation of soluble guanylate cyclase and the production of cyclic GMP is one of the best characterized modes of NO action. Having shown that inhibition of NOS blocks PC12 cell differentiation we tested whether nitric oxide acts through soluble guanylate cyclase to lead to cell cycle arrest and neuronal differentiation. Unlike NOS inhibition, the inhibition of soluble guanylate cylcase does not block the induction of neuronal markers. Moreover, treatment of NGF-treated, NOS-inhibited PC12 cells with a soluble analog of cyclic GMP was unable to restore differentiation of those cells. Hence, cGMP is not a component of this pathway and we had to consider other mechanisms of NO action.
It has become increasingly evident that another manner by which NO may exert its effects is by S-nitrosylation of cysteine residues. We tested, in vitro whether nitric oxide may control p53 by S-nitrosylation and inactivation of the p53 negative regulator, Hdm2. Treatment of Hdm2 with a nitric oxide donor inhibits Hdm2-p53 binding, the first step in Hdm2 regulation of p53. The presence of cysteine or DTT blocks this inhibition of binding. Moreover, nitric oxide inhibition of Hdm2-p53 binding was found to be reversible. Sulfhydryl-sensitivity and reversibility are consistent with nitrosylation. Finally, we have identified a critical cysteine residue that nitric oxide modifies in order to disrupt Hdm2-p53 binding. Mutation of this residue from a cysteine to an alanine does not interfere with binding but rather eliminates the sensitivity of Hdm2 to nitric oxide inactivation.
7
Silva, Maria Isabel. "Distribuição de celulas imunorreativas para sintase neuronal do oxido nitrico (nNOS) no hipocampo de pombos (Columba livia) apos aprendizagem de escolha alimentar." [s.n.], 2007. http://repositorio.unicamp.br/jspui/handle/REPOSIP/314142.
Full textAbstract:
Orientadores: Elenice Aparecida de Moraes Ferrari, Claudio Antonio Barbosa de ToledoDissertação (mestrado) - Universidade Estadual de Campinas, Instituto de Biologia
Made available in DSpace on 2018-08-10T10:38:58Z (GMT). No. of bitstreams: 1 Silva_MariaIsabel_M.pdf: 1381550 bytes, checksum: 9cb336aef794086ff363f071f8040818 (MD5) Previous issue date: 2007
Resumo: O hipocampo exerce papel fundamental no processamento de aprendizagem e memória espaciais. Comparações das características funcionais, anatômicas e neuroquímicas do hipocampo são favorecidas por evidência oriunda de estudo sobre aprendizagem especial em mamíferos e aves. O objetivo do presente estudo foi analisar a marcação imunohistoquímica de células nNOS- positivas no hipocampo de pombos (C. lívia) após diferentes duração do treino em aprendizagem especial. Foram analisados grupos de animais não treinados (MAN), treinados em 1 sessão (EXP1), treinados em 5 sessões (EXP5), exposto à arena em 1 sessão (CONT1) ou em 5 sessões (CONT5). As sessões foram realizadas numa arena onde havia quatro comedouros, um dos quais com alimento. Em cada sessão, com seis tentativas, registrou-se a latência (seg) e a assertividade da escolha de um comedouro. Após os testes comportamentais, usou-se imunoistoquímica para a análise da marcação de células nNOS-positiva no hipocampo dorsal e ventral. O grupo EXP5 teve diminuição da latência de escolha ('F IND. 4,28¿= 23,74; p < 0,001) e aumento das respostas corretas ('F IND. 4,35¿= 8,66; p < 0,001) em função do treino. A marcação das células nNOS-positivas no hipocampo foi significativamente maior no hipocampo dorsal dos animais EXP5 em comparação com o hipocampo ventral ('F IND. 4,22¿= 104,79; p<0,001) e com os demais grupos ('F IND. 4,22¿= 10,17; p < 0,001). O aumento da imunorratividade de células nNOS- positivas no hipocampo dorsal de pombos após a aprendizagem da localização do comedouro correto sugere o envolvimento desta região e de processos mediados pro transmissão glutamatérgica nesse processo de aprendizagem e memória em pombos
Abstract: The hippocampus has fundamental role in spatial learning and memory processes. Functional and neurochemical analysis of the hippocampus are favored by evidence on spatial learning in mammals and birds. The present study examined the immunohistochemical expression of nNOS-positive cells in the hippocampus of pigeons (C. livia) after training in food location task. Animals were trained in one (EXP1) or five (EXP5) sessions or had one (CONT1) or five sessions (CONT5) of exposure to the experimental arena. The six trials sessions were conducted daily in one arena with 4 food bowls, one of which had food. Latency and accuracy of choise recorded. After behavioral tests, nNOS immunoractivity in hippocampal cells was analyzed. EXP 5 showed reduction imunoreactivity in hippocampal cells was analysed. EXP5 showed reduction in latency of choise ('F IND. 4,28¿= 23,74; p < 0,001) and increassis in correct choise ('F IND. 4,35¿= 8,66; p < 0,001) as function of the training. The expression of nNOS- positive cells was significantily higher in the dorsal hippocampus of EXP5 group as compared with the ventral hippocampus ('F IND. 4,22¿= 104,79; p < 0,001) and the other groups ('F IND. 4,28¿= 10,17; p < 0,001). The increases of nNOS immunoreactive neurons after learning of the food location suggest that nNOS is involved in processes of spatial learning and memory that are mediated by the dorsal hippocampus of pigeons
Mestrado
Fisiologia
Mestre em Biologia Funcional e Molecular
8
Denadai, Magda Aline. "Efeitos do 7-nitroindazole, um inibidor da sintase neuronal do oxido nitrico (nNOS), sobre o condiciomaneto contextural em pombos." [s.n.], 2008. http://repositorio.unicamp.br/jspui/handle/REPOSIP/314745.
Full textAbstract:
Orientador: Elenice Aparecida de Moraes FerrariDissertação (mestrado) - Universidade Estadual de Campinas, Instituto de Biologia
Made available in DSpace on 2018-08-11T20:16:54Z (GMT). No. of bitstreams: 1 Denadai_MagdaAline_M.pdf: 823511 bytes, checksum: 1887972f9e5047fecbd7195247b586a8 (MD5) Previous issue date: 2008
Resumo: O óxido nítrico (NO), um neurotransmissor não convencional, tem papel importante em processos neurobiológicos de comportamento e de memória. Sua síntese é mediada por três isoformas de sintase do óxido nítrico (NOS): a neuronal (nNOS), a endotelial (eNOS) e induzível (iNOS). Este trabalho analisou o efeito do 7-nitroindazole (7-NI), um inibidor seletivo da nNOS, no condicionamento clássico aversivo em pombos. Foram usados 4 grupos: tratados com 7-NI (grupo 7-nitroindazole; G7-NI, n=5), tratados com óleo de amendoim (grupo veículo; GV, n=5), controle/sem tratamento (grupo controle; GC, n=5) e grupo não tratado/não condicionado (grupo manipulação; GM, n=5). A administração i.p. de 7-NI (25 mg/kg), ou do óleo de amendoim foi feita imediatamente após o treinamento. O G7-NI, o GV e o GC receberam três associações som-choque (5°, 10° e 15º minutos) numa sessão de 20 min. O teste a o contexto foi realizado 24 horas depois. As sessões foram gravadas para posterior transcrição e análise comportamental. A ocorrência da resposta de congelamento durante o treino não diferiu entre os grupos (p>0,05), mas durante o teste foi menor para o G7-NI em comparação ao treino (p<0.01) e aos demais grupos no teste (p<0.001). A atividade da NOS dependente de Ca++ no hipocampo foi menor no G7-NI do que nos outros grupos (p<0,01). Análise por Western blot indicou aumento na expressão de nNOS no G7-NI (p<0,05). A administração sistêmica de 7-NI teve um efeito amnésico sobre a memória contextual aversiva, indicando que a atividade da NOS dependente de Ca++ é importante para os processos de condicionamento clássico aversivo em pombos.
Abstract: Nitric oxide (NO) is an unsual neurotransmitter that plays an important role in neurobiological functions underlying behavior and memory. NO synthesis and release can be mediated by three isoforms of NO synthases (NOS): neuronal (nNOS), endothelial (eNOS) and inducible (iNOS). This study examined the effect of 7-nitroindazole (7-NI), a selective nNOS inhibitor, on contextual fear conditioning in pigeons. Four groups of pigeons were used: treated with 7-NI (7-NI; n=5), treated with peanut oil (Vehicle; n=5), non treated controls (Control; n=5) and non treated and no-trained controls (Non-trained; n=5). Treatment consisted in 7-NI (25 mg/kg; i.p.) or vehicle (peanut oil) administration, immediately after training. All the animals were trained in one 20 min session during which three tone-shock pairings (5th, 10th and 15th minutes) were presented. The test to the context was conducted 24h later. Behavioral categories were analyzed through the transcription of video-tapes of the sessions. The groups 7-NI, Vehicle and Control showed no significant differences in freezing during the conditioning session (p>0.05). During the test to the context the group 7-NI expressed significantly lower freezing as compared to Vehicle and Control (p<0.05). The 7-NI pigeons showed lower hippocampal activity of Ca++ dependent-NOS than Vehicle and Control groups (p<0.01). Western blot analysis indicated significant increase in nNOS expression (p<0.05). The systemic administration of 7-NI induced amnestic effects on contextual fear memory that evidence that Ca++-dependent NOS activity is required for fear conditioning in pigeons.
Mestrado
Fisiologia
Mestre em Biologia Funcional e Molecular
9
Machado, Aline Vilar da Silva. "Variação circadiana da expressão da sintase neuronal de óxido nítrico (nNOS) no hipocampo e o condicionamento contextual aversivo em pombos (Columba livia)." [s.n.], 2011. http://repositorio.unicamp.br/jspui/handle/REPOSIP/314744.
Full textAbstract:
Orientador: Elenice Aparecida de Moraes FerrariDissertação (mestrado) - Universidade Estadual de Campinas, Instituto de Biologia
Made available in DSpace on 2018-08-18T00:49:19Z (GMT). No. of bitstreams: 1 Machado_AlineVilardaSilva_M.pdf: 2487506 bytes, checksum: ec15fc1b78bef814d6d459499276cdf5 (MD5) Previous issue date: 2011
Resumo: A ritmicidade circadiana, expressa na alteração do comportamento e em aspectos morfofisiológicos e moleculares ao longo das 24 horas do dia, é uma das funções básicas dos organismos vivos. Os processos comportamentais e os mecanismos moleculares no hipocampo, que estão envolvidos na aprendizagem e memória, demonstram oscilação circadiana. Vários estudos sugeriram que o condicionamento clássico aversivo é afetado pelo sistema de temporização circadiana e que a oscilação circadiana de vias moleculares específicas é requerida para a consolidação da memória aversiva. O presente trabalho investigou a oscilação circadiana da expressão da nNOS e da atividade da proteína NOS no hipocampo de pombos e as suas relações com a modulação temporal do condicionamento contextual aversivo. Na Parte I, caracterizou-se o padrão temporal da expressão da nNOS, que foi detectada por Western Blotting e o padrão temporal da atividade enzimática da NOS, determinada pela quantidade de L-citrulina produzida por minuto e por micrograma de proteína na reação. Na Parte II, nos horários de mínima e máxima atividade enzimática da proteína, pombos foram treinados e testados em condicionamento aversivo ao contexto. As sessões foram gravadas para posterior análise comportamental. Após o teste foi realizada a imunoistoquímica para marcação da nNOS em neurônios do hipocampo. Foi evidenciada ritmicidade circadiana significativa (p < 0,05) na expressão protéica da nNOS e na atividade enzimática da NOS, segundo os valores fornecidos pelo método Cosinor para caracterização do padrão temporal. As médias da densitometria óptica dos grupos com horários mais próximos da acrofase - ZT04 (10hs; 0,944 ± 0,12) e a batifase - ZT16-(22hs; 0,572 ± 0,16) foram significativamente diferentes (F5,18 p < 0,0001). Os grupos condicionados, em ambos os horários, mostraram maior duração e maior ocorrência do comportamento de congelamento do que os controles (p < 0,05). Houve uma variação dia-noite para o comportamento de congelamento nos grupos controles (p < 0,05). A marcação de células nNOS-positivas foi maior no hipocampo dos grupos condicionados sendo que o total de células nNOS-positivas na área dorsal do grupo experimental testado à noite foi maior do que aquele observado nos grupos controles e no experimental da manhã (p < 0,05). Os dados mostraram que a expressão protéica da nNOS e da atividade enzimática da NOS no hipocampo de pombos mostram uma oscilação que caracteriza um padrão temporal circadiano. Tanto no horário de máxima como no de mínima atividade da nNOS, o condicionamento contextual aversivo resultou em medo condicionado ao contexto e em expressão de células nNOS-positivas no hipocampo que foi maior nos pombos condicionados do que nos controles. Contudo, no hipocampo do grupo testado à noite houve um maior número de células nNOS-positivas. Esse dado estimula questionamento sobre se ocorreria a ativação de mecanismos compensatórios para o aumento da expressão da proteína nNOS, quanto essa é requisitada em situações de baixa disponibilidade
Abstract: The circadian rhythm, expressed in changing behavior and the morphophysiologic and molecular aspects over 24 hours of the day is one of the basic functions of living organisms. The behavioral processes and molecular mechanisms in the hippocampus, which are involved in learning and memory, show circadian oscillation. Several studies have suggested that classical fear conditioning is affected by the circadian timing system and the circadian oscillation of specific molecular pathways is required for the consolidation of aversive memory. This study investigated the circadian oscillation of nNOS expression and activity of NOS protein in the hippocampus of pigeons and their relationship with the temporal modulation of aversive contextual conditioning. In Part I, we have characterized the temporal pattern of nNOS expression, which was detected by Western blotting and temporal pattern of NOS enzyme activity, determined by the amount of L-citrulline produced per minute and per microgram of protein in the reaction. In Part II, at the times of minimum and maximum activity of the protein, pigeons were trained and tested in aversive conditioning to context. The sessions were taped for later behavioral analysis. After the test was performed immunohistochemical for labeling of nNOS in neurons in the hippocampus. Circadian rhythm was evident (p <0.05) in nNOS protein expression and enzyme activity of NOS, according to figures provided by Cosinor method to characterize the temporal pattern. The mean optical density of groups with times closer to the acrophase - ZT04 (10hrs; 0.944 ± 0.12) and nadir - ZT16-(22hs; 0.572 ± 0.16) were significantly different (F5, 18 p <0.0001 ). The groups conditioned in both schedules, showed more frequent and longer duration of freezing behavior than controls (p <0.05). There was a day-night variation for freezing behavior in control groups (p <0.05). Labeling of nNOS-positive cells was higher in the hippocampus of the groups conditioned with total nNOS-positive cells in the dorsal area of the experimental group tested at night was higher than that observed in control groups and experimental group in the morning (p <0.05). The data showed that nNOS protein expression and enzymatic activity of NOS in the hippocampus of pigeons show an oscillation that characterizes a circadian temporal pattern. Both at the time of maximum as the low activity of nNOS, the aversive contextual conditioning resulted in fear conditioning to context and expression of nNOS-positive cells in the hippocampus was higher in pigeons conditioned than in controls. However, in the hippocampus of the group tested in the evening there was a greater number of nNOS-positive cells. This fact encourages questioning of whether there would be activation of compensatory mechanisms for the increased expression of nNOS protein, as this is required in situations of low availability
Mestrado
Fisiologia
Mestre em Biologia Funcional e Molecular
10
Faria, Larissa Oliveira Melloni de 1985. "Participação da sintase neuronal de óxido nítrico (nNOS) na consolidação e reconsolidação da memória do condicionamento clássico aversivo em pombos (Columba livia)." [s.n.], 2013. http://repositorio.unicamp.br/jspui/handle/REPOSIP/314128.
Full textAbstract:
Orientador: Elenice Aparecida de Moraes FerrariDissertação (mestrado) - Universidade Estadual de Campinas, Instituto de Biologia
Made available in DSpace on 2018-08-23T06:24:39Z (GMT). No. of bitstreams: 1 Faria_LarissaOliveiraMellonide_M.pdf: 1121073 bytes, checksum: 5a3108ca0447b5fae98988b4611d7616 (MD5) Previous issue date: 2013
Resumo: O óxido nítrico (NO) é um neurotransmissor não convencional o qual tem papel importante em processos neurobiológicos de comportamento e de memória. Sua síntese é mediada por três isoformas de sintase do óxido nítrico (NOS): a neuronal (nNOS), a endotelial (eNOS) e a induzível (iNOS). Este trabalho investigou os efeitos da administração do 7- nitroindazol (7-NI), inibidor preferencial da nNOS, na consolidação e reconsolidação da memória do condicionamento clássico aversivo. Pombos adultos foram atribuídos a 5 grupos: Foram usados 5 grupos: grupo 7-nitroindazole (7-NI) (100nmol/0.5?/l; DMSO (20%), NaOH (50mM) e Tween-80 (16%) diluído em PBS; i.c.v.), grupo veículo (VEIC) (0,5?/l; DMSO (20%), NaOH (50mM) e Tween-80 (16%) diluído em PBS, i.c.v.), grupo condicionado/não tratado (COND), grupo contexto/não-tratado (CONT) e grupo não tratado/não condicionado (NÄIVE). Sete dias após implante de microcânula intracerebroventricular (i.c.v.), ocorreu o condicionamento com três associações contextochoque numa sessão de 20 min. O teste e o re-teste consistiram na re-exposição ao contexto do condicionamento por 5 min. O intervalo entre sessões foi de 24h. A administração de 7-NI ou do veículo ocorreu imediatamente após o treino (Experimento 1) ou após o re-teste (Experimento 2). A atividade enzimática da NOS dependente e independente de Ca2+ e da expressão protéica da nNOS foram realizadas no tecido hipocampal. No Experimento 1, a ocorrência de congelamento no teste do 7-NI foi menor do que no treino (p<0.01) e no teste do COND e VEIC (p < 0.001). A atividade da NOS dependente de Ca++ no 7-NI foi menor do que no COND e VEIC (p<0,01), mas não diferiu do CONT e do NÄIVE. A expressão protéica de nNOS não diferiu entre os grupos (p<0,05). No Experimento 2, houve diminuição dos comportamentos defensivos, incluindo o congelamento, no re-teste do 7-NI comparado com VEIC e COND (p<0.05), mas os grupos não diferiram quanto à atividade de NOS dependente de Ca2+ ou à expressão protéica da nNOS. Conclui-se que o 7-NI interferiu na consolidação e a reconsolidação da memória, indicando a ativação da via de sinalização do óxido nítrico no hipocampo em processos da memória de medo condicionado ao contexto em pombos
Abstract: Nitric oxide (NO) is an unconventional neurotransmitter which plays an important role in neurobiological processes of behavior and memory. Its synthesis is mediated by three isoforms of nitric oxide synthase (NOS): the neuronal (nNOS), the endothelial (eNOS) and the inducible (iNOS). This study investigated the effects of the administration of 7- nitroindazole (7-NI), a preferential nNOS inhibitor, in the consolidation and reconsolidation of aversive classical conditioning memory. Adult male pigeons were assigned to 5 groups: 7-nitroindazole, 7-NI (100nmol/0.5?/l; DMSO (20%), NaOH (50 mM) and Tween-80 (16%) diluted in PBS; i.c.v.) Vehicle group; VEH (0.5 ? / L; DMSO (20%), NaOH (50 mM) and Tween-80 (16%) diluted in PBS; i.c.v.), conditioning/non-treated group (COND), context/non-treated group (CONT) and non-conditioning/non-treated group (NÄIVE). Seven days after implantation of intracerebral ventricular (i.c.v.) microcannula the conditioning occurred with three context-shock associations in a session of 20 min. During the testing and retesting sessions pigeons were reexposed to the conditioning context for 5 min. The between sessions interval was 24h. Administration of 7-NI or vehicle occurred immediately after training (Experiment 1) or after testing (Experiment 2). The enzymatic activity of Ca2+ dependent and independent NOS and protein expression of nNOS in the hippocampus tissue were carried out following the behavioral test or retest. In Experiment 1, the occurrence of freezing in the testing session of 7-NI group was lower than in the training (p <0.01) and the testing sessions of COND and VEH groups (p <0.001). The activity of Ca2+ dependent NOS in the 7-NI group was lower than in COND and VEH groups (p <0.01) but did not differ from CONT and NÄIVE groups. The nNOS protein expression in the hippocampus did not differ among the different groups (p<0.05). In Experiment 2, there was a decrease of defensive behaviors, which include freezing, in the retest of the 7-NI compared with VEH and COND groups (p <0.05), but the groups did not differ in the activity of Ca2+ dependent NOS or the protein expression of nNOS. We conclude that 7-NI interfered on the consolidation and reconsolidation of memory, indicating activation of the nitric oxide signaling pathway in the hippocampus and in memory processes of conditioned fear context in pigeons
Mestrado
Fisiologia
Mestra em Biologia Funcional e Molecular
Books on the topic "Neuronal nitric oxide synthase (nNOS)"
1
McLaren, Anya T. Increased expression of hypoxia inducible factor-1alpha (HIF-1alpha) and neuronal nitric oxide synthase (nNOS) in the cerebral cortex of anemic rats. 2006.
Find full text
2
Newton, Derek Colin. The human neuronal nitric oxide synthase gene: RNA biology guiding expressional regulation. 2004.
Find full textBook chapters on the topic "Neuronal nitric oxide synthase (nNOS)"
1
Tiro, Jasmin, Simon J. Craddock Lee, Steven E. Lipshultz, Tracie L. Miller, James D. Wilkinson, Miriam A. Mestre, Barbara Resnick, et al. "Neuronal Nitric Oxide Synthase (nNOS)." In Encyclopedia of Behavioral Medicine, 1326. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-1005-9_101144.
Full text
2
Saini, Rashmi, Zaffar Azam, Leena Sapra, and Rupesh K. Srivastava. "Neuronal Nitric Oxide Synthase (nNOS) in Neutrophils: An Insight." In Reviews of Physiology, Biochemistry and Pharmacology, 49–83. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/112_2021_61.
Full text
3
Pichiule, P., J. C. Chavez, R. J. Przybylski, and J. C. LaManna. "Increase of Neuronal Nitric Oxide Synthase during Chronic Hypoxia." In Oxygen Transport to Tissue XX, 319–23. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-4863-8_37.
Full text
4
Prabhakar, Nanduri R., Shobha Rao, David Premkumar, Sean F. Pieramici, Ganesh K. Kumar, and Rajesh K. Kalaria. "Regulation of Neuronal Nitric Oxide Synthase Gene Expression by Hypoxia." In Frontiers in Arterial Chemoreception, 345–48. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5891-0_53.
Full text
5
Kitamura, M., H. Matsuda, S. Kimura, and T. Iyanagi. "One-Electron Reduction of Quinones by the Neuronal Nitric-Oxide Synthase Reductase Domain." In Advances in Experimental Medicine and Biology, 323–26. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-0667-6_50.
Full text
6
Rokutan, Kazuhito, Shigetada Teshima, Tomoko Kawai, Tsukasa Kawahara, Kenji Kusumoto, and Kyoichi Kishi. "Regulation of Mucin Synthesis by Neuronal Nitric Oxide Synthase in Gastric Pit Cells." In Trends in Gastroenterology and Hepatology, 90–94. Tokyo: Springer Japan, 2001. http://dx.doi.org/10.1007/978-4-431-67895-3_15.
Full text
7
Li, Yi-Fan, Yu Wang, Keith M. Channon, Harold D. Schultz, Irving H. Zucker, and Kaushik P. Patel. "Manipulation of Neuronal Nitric Oxide Synthase Within the Paraventricular Nucleus Using Adenovirus and Antisense Technology." In Molecular Cardiology, 59–79. Totowa, NJ: Humana Press, 2005. http://dx.doi.org/10.1385/1-59259-879-x:059.
Full text
8
Ding, Chuanqing, Benjamin Walcott, and Kent T. Keyser. "Neuronal Nitric Oxide Synthase is Expressed in the Mouse Lacrimal Gland and Neurons of Pterygopalatine Ganglion." In Advances in Experimental Medicine and Biology, 91–95. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0717-8_11.
Full text
9
Masters, B. S. S., K. McMillan, J. Nishimura, P. Martasek, L. J. Roman, E. Sheta, S. S. Gross, and J. Salerno. "Understanding the Structural Aspects of Neuronal Nitric Oxide Synthase (NOS) Using Microdissection by Molecular Cloning Techniques." In Advances in Experimental Medicine and Biology, 163–69. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4757-9480-9_22.
Full text
10
Migita, Catharina Taiko, John C. Salerno, Bettie Sue Siler Masters, and Masao Ikeda-Saito. "Electron Paramagnetic Resonance Studies on Substrate Binding to the NO Complex of Neuronal Nitric Oxide Synthase." In Oxygen Homeostasis and Its Dynamics, 298–303. Tokyo: Springer Japan, 1998. http://dx.doi.org/10.1007/978-4-431-68476-3_37.
Full textConference papers on the topic "Neuronal nitric oxide synthase (nNOS)"
1
Jackson, Claire L., Jacqueline King, Edith N. Quinn, Peter M. Lackie, and Jane S. Lucas. "The Importance Of Being NNOS? Unique Localization Of Neuronal Nitric Oxide Synthase To Cilia And Investigating A Nitric Oxide Synthase-1 Polymorphism In Primary Ciliary Dyskinesia." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a5504.
Full text
2
Razee, A., S. Banerjee, M. Zargari, J. Hong, and S. Umar. "Intrathecal Neuronal Nitric Oxide Synthase Inhibition Attenuates Pulmonary Hypertension and Rescues Right Ventricular Failure in Rats." In American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a3692.
Full text
3
Pineda, Joseba, Patricia Pablos, and Aitziber Mendiguren. "Effect of neuronal nitric oxide synthase inhibitors and antioxidants on the development of tolerance by different opioid agonists in the rat locus coeruleus." In MOL2NET, International Conference on Multidisciplinary Sciences. Basel, Switzerland: MDPI, 2015. http://dx.doi.org/10.3390/mol2net-1-b022.
Full text