Relevant bibliographies by topics / Nitric Oxide Synthase Type II / Journal articles

To see the other types of publications on this topic, follow the link: Nitric Oxide Synthase Type II.

Journal articles on the topic 'Nitric Oxide Synthase Type II'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 June 2025

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Nitric Oxide Synthase Type II.'

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.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

Olson, Susan, Richard Oeckler, Xinmei Li, et al. "Angiotensin II stimulates nitric oxide production in pulmonary artery endothelium via the type 2 receptor." American Journal of Physiology-Lung Cellular and Molecular Physiology 287, no. 3 (2004): L559—L568. http://dx.doi.org/10.1152/ajplung.00312.2003.

Full text

Abstract:

We previously reported that angiotensin II stimulates an increase in nitric oxide production in pulmonary artery endothelial cells. The aims of this study were to determine which receptor subtype mediates the angiotensin II-dependent increase in nitric oxide production and to investigate the roles of the angiotensin type 1 and type 2 receptors in modulating angiotensin II-dependent vasoconstriction in pulmonary arteries. Pulmonary artery endothelial cells express both angiotensin II type 1 and type 2 receptors as assessed by RT-PCR, Western blot analysis, and flow cytometry. Treatment of the endothelial cells with PD-123319, a type 2 receptor antagonist, prevented the angiotensin II-dependent increase in nitric oxide synthase mRNA, protein levels, and nitric oxide production. In contrast, the type 1 receptor antagonist losartan enhanced nitric oxide synthase mRNA levels, protein expression, and nitric oxide production. Pretreatment of the endothelial cells with either PD-123319 or an anti-angiotensin II antibody prevented this losartan enhancement of nitric oxide production. Angiotensin II-dependent enhanced hypoxic contractions in pulmonary arteries were blocked by the type 1 receptor antagonist candesartan; however, PD-123319 enhanced hypoxic contractions in angiotensin II-treated endothelium-intact vessels. These data demonstrate that angiotensin II stimulates an increase in nitric oxide synthase mRNA, protein expression, and nitric oxide production via the type 2 receptor, whereas signaling via the type 1 receptor negatively regulates nitric oxide production in the pulmonary endothelium. This endothelial, type 2 receptor-dependent increase in nitric oxide may serve to counterbalance the angiotensin II-dependent vasoconstriction in smooth muscle cells, ultimately regulating pulmonary vascular tone.

APA, Harvard, Vancouver, ISO, and other styles

Togashi, H., M. Sasaki, E. Frohman, et al. "Neuronal (type I) nitric oxide synthase regulates nuclear factor B activity and immunologic (type II) nitric oxide synthase expression." Proceedings of the National Academy of Sciences 94, no. 6 (1997): 2676–80. http://dx.doi.org/10.1073/pnas.94.6.2676.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Cuzzocrea, Salvatore, Tiziana Persichini, Laura Dugo, Marco Colasanti, and Giovanni Musci. "Copper induces type II nitric oxide synthase in vivo." Free Radical Biology and Medicine 34, no. 10 (2003): 1253–62. http://dx.doi.org/10.1016/s0891-5849(03)00110-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Tomimoto, Hidekazu, Masaki Nishimura, Toshihiko Suenaga, et al. "Distribution of Nitric Oxide Synthase in the Human Cerebral Blood Vessels and Brain Tissues." Journal of Cerebral Blood Flow & Metabolism 14, no. 6 (1994): 930–38. http://dx.doi.org/10.1038/jcbfm.1994.124.

Full text

Abstract:

The distribution of nitric oxide synthase was investigated in human cerebral blood vessels and brain tissues. NADPH-diaphorase histochemistry, which is a marker for nitric oxide synthase in neurons and endothelial cells, revealed periadventitial nerve fibers in the arteries of the circle of Willis and their cortical branches, as well as the common carotid and subclavian arteries. The fibers were mostly nonvaricose in the periadventitial nerve trunk and were varicose within the adventitia. Patchy reaction products were distributed in the perinuclear region of each endothelial cell. Smooth muscle cells in the tunica media were weakly stained. Staining was particularly intense in regions with atherosclerotic changes, which consist of macrophage infiltration and proliferation of fibroblasts. In the neural parenchyma, two types of NADPH-diaphorase reactive neurons were differentiated. Type I neurons were intensely stained, medium-sized, and bipolar or multipolar. They were distributed in the cerebral cortex and white matter, mostly in the subcortical white matter. Type II neurons were lightly stained, small oval neurons with fine processes and were distributed in the cerebral cortex. Endothelial cells were intensely reactive for NADPH-diaphorase in the arteries, arterioles, and capillaries but weakly in veins. Immuno-histochemistry for neural nitric oxide synthase labeled perivascular nerves in the larger arteries and those in the neural parenchyma. Both type I and type II neurons were labeled. Nitric oxide synthase in endothelial cells and the nerve encircling blood vessels further suggests a dual control of cerebral circulation by nitric oxide in human brain.

APA, Harvard, Vancouver, ISO, and other styles

Togashi, H., M. Sasaki, E. Frohman та ін. "NEURONAL (TYPE I) NITRIC OXIDE SYNTHASE REGULATES NUCLEAR FACTOR ϰ B ACTIVITY AND IMMUNOLOGIC (TYPE II) NITRIC OXIDE SYNTHASE EXPRESSION". Japanese Journal of Pharmacology 75 (1997): 6. http://dx.doi.org/10.1016/s0021-5198(19)31275-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Radionova, T. O., І. М. Skrypnyk, О. Ye Akimov, V. О. Kostenko, and V. І. Virchenko. "CORRECTION OF NITRIC OXIDE SYSTEM IN PATIENTS WITH HELICOBACTER PYLORI-ASSOCIATED CHRONIC GASTRITIS AND CONCOMITANT TYPE 2 DIABETES MELLITUS." Актуальні проблеми сучасної медицини: Вісник Української медичної стоматологічної академії 20, no. 2 (2020): 79–85. http://dx.doi.org/10.31718/2077-1096.20.2.79.

Full text

Abstract:

The current data suggest that Helicobacter pylori infection and type 2 diabetes mellitus may affect the state of nitric oxide system, which significantly influences stomach functioning. The aim of the research was to study the state of nitric oxide system in patients with Helicobacter pylori-associated chronic gastritis and concomitant type 2 diabetes mellitus, and to investigate the potential of eupatilin in its correction. 172 patients with confirmed chronic gastritis were enrolled into the study. They were divided into 4 groups: І (n=71) included individuals with Helicobacter pylori-positive chronic gastritis and type 2 diabetes mellitus; ІІ (n=21) included patients with Helicobacter pylori-negative chronic gastritis and type 2 diabetes mellitus; ІІІ (n=48) included patients with Helicobacter pylori-positive chronic gastritis without type 2 diabetes mellitus; IV (n=32) was made up with individuals having Helicobacter pylori-negative chronic gastritis without type 2 diabetes mellitus. According to prescribed therapeutic schemes the patients of groups І and ІІІ were additionally subdivided into the following subgroups: groups I-A (n=35) and III-A (n=24) underwent anti-Helicobacter therapy, groups I-В (n=36) and III-B (n=24) were prescribed to receive anti-Helicobacter therapy and eupatilin. Anti-Helicobacter therapy included pantoprazole 40 mg, amoxicillin 1000 mg and clarithromycin 500 mg bid for 10 days. The patients received Eupatilin as an active agent of Stilen preparation, which contains 0.48 – 1.44 mg of eupatilin, tid for 28 days. Nitrites content and activity of inducible and constitutional nitric oxide synthases were analyzed in blood serum before the treatment and on the 28th day after the therapy completed. The patients of group I before the treatment were found to have an increase of nitrites level in 1.4 times, inducible nitric oxide synthase in 1.5 times higher in comparison to the patients of group II. An activity of constitutional nitric oxide synthase in patients with chronic gastritis and type 2 diabetes mellitus was found to be decreased regardless the Helicobacter pylori-status in 2.3 and 2.7 times in comparison to the patients of groups III and IV respectively. Eupatilin prescription promoted Helicobacter therapy eradication and treatment outcomes through nitrites decrease in 1.5 times, reduction of inducible nitric oxide synthase activity in 1.2 times, and growth of constitutional nitric oxide synthase in1.2 times in patients of I-B group in comparison to group I-A. Combined anti-Helicobacter therapy with eupatilin promotes successful Helicobacter pylori eradication, which was 6.2% higher in patients of I-B group than in I-A group. Conclusions: Helicobacter pylori-associated chronic gastritis in patients with type 2 diabetes mellitus is followed by rise of nitrites, inducible nitric oxide synthase activity and simultaneous decline of constitutional nitric oxide synthase in blood serum. Eupatilin prescription as a component of integrated anti-Helicobacter therapy increases the efficacy of Helicobacter pylori eradication and improves the state of nitric oxide-system due to its anti-inflammatory, antioxidant and cytoprotective properties.

APA, Harvard, Vancouver, ISO, and other styles

Oydanich, Marko, Denis Babici, Jie Zhang, Nicole Rynecki, Dorothy E. Vatner, and Stephen F. Vatner. "Mechanisms of sex differences in exercise capacity." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 316, no. 6 (2019): R832—R838. http://dx.doi.org/10.1152/ajpregu.00394.2018.

Full text

Abstract:

Sex differences are an important component of National Institutes of Health rigor. The goal of this investigation was to test the hypothesis that female mice have greater exercise capacity than male mice, and that it is due to estrogen, nitric oxide, and myosin heavy chain expression. Female C57BL6/J wild-type mice exhibited greater ( P < 0.05) maximal exercise capacity for running distance (489 ± 15 m) than age-matched male counterparts (318 ± 15 m), as well as 20% greater work to exhaustion. When matched for weight or muscle mass, females still maintained greater exercise capacity than males. Increased type I and decreased type II myosin heavy chain fibers in the soleus muscle from females are consistent with fatigue resistance and better endurance in females compared with males. After ovariectomy, female mice no longer demonstrated enhanced exercise, and treatment of male mice with estrogen resulted in exercise capacity similar to that of intact females (485 ± 37 m). Nitric oxide synthase, a downstream target of estrogen, exhibited higher activity in female mice compared with male mice, P < 0.05, whereas ovariectomized females exhibited nitric oxide synthase levels similar to males. Nitric oxide synthase activity also increased in males treated with chronic estrogen to levels of intact females. Nitric oxide synthase blockade with Nω-nitro-l-arginine methyl ester eliminated the sex differences in exercise capacity. Thus estrogen, nitric oxide, and myosin heavy chain expression are important mechanisms mediating the enhanced exercise performance in females.

APA, Harvard, Vancouver, ISO, and other styles

Tracey, W. R., J. S. Pollock, F. Murad, M. Nakane, and U. Forstermann. "Identification of an endothelial-like type III NO synthase in LLC-PK1 kidney epithelial cells." American Journal of Physiology-Cell Physiology 266, no. 1 (1994): C22—C28. http://dx.doi.org/10.1152/ajpcell.1994.266.1.c22.

Full text

Abstract:

Porcine kidney tubular epithelial cells (LLC-PK1) produce nitric oxide or a related compound (e.g., a nitrosothiol) after stimulation with various agonists. We now report the identification and characterization of a constitutive, particulate nitric oxide (NO) synthase from LLC-PK1 cells. After partial purification on adenosine 2',5'-bisphosphate-Sepharose, the particulate NO synthase activity eluted anomalously from Superose 6 gel permeation columns near the total included volume, similar to that observed for the endothelial (type III) NO synthase. Substrate/cofactor requirements of the epithelial and endothelial NO synthases were identical, i.e., dependency on L-arginine, (6R)-5,6,7,8-tetrahydrobiopterin, FAD, calcium and calmodulin. The epithelial enzyme activity was inhibited by the arginine analogues, NG-methyl-L-arginine (100 microM) and NG-nitro-L-arginine (100 microM), as well as the calmodulin antagonists, trifluoperazine (100 microM) and calmidazolium (30 microM). Anti-type III (H32), but not anti-type I (brain, 6763-5) or anti-type II (macrophage, 8196) NO synthase antibodies, detected a single immunoreactive band in the LLC-PK1 particulate fraction of approximately 140 kDa by Western blot analysis. Finally, the presence of type III NO synthase mRNA in LLC-PK1 cells was demonstrated using the polymerase chain reaction. These data indicate that LLC-PK1 kidney epithelial cells contain type III NO synthase, which has been classically associated with the vascular endothelium.

APA, Harvard, Vancouver, ISO, and other styles

Nicholls, David J., Andrew Kirk, and Alan V. Wallace. "Reversibility of inhibition of human type II nitric oxide synthase." Biochemical Society Transactions 24, no. 1 (1996): 20S. http://dx.doi.org/10.1042/bst024020s.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Moritoki, Hideki, Tetsuhiro Hisayama, Wataru Kondoh, and Kann Kida. "Protein kinases in induction of type II nitric oxide synthase." Japanese Journal of Pharmacology 71 (1996): 6. http://dx.doi.org/10.1016/s0021-5198(19)33973-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Grzybicki, D., R. Schelper, and S. Murphy. "EXPRESSION OF NITRIC OXIDE SYNTHASE TYPE II WITH CEREBRAL TRAUMA." Journal of Neuropathology and Experimental Neurology 55, no. 5 (1996): 647. http://dx.doi.org/10.1097/00005072-199605000-00175.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Fretland, Donald J., Barnett S. Pitzele, Jane R. Connor, Mark G. Currie, and Pamela T. Manning. "Inhibition of Nitric Oxide Synthase and Prospects For Therapy in Inflammatory Diseases." Current Pharmaceutical Design 3, no. 5 (1997): 447–62. http://dx.doi.org/10.2174/138161280305221010094339.

Full text

Abstract:

Abstract: Nitric oxide is synthesized enzymatically from arginine in numerous tissues and cell types by three_distinct isoforms of the enzyme nitric oxide synthase (NOS). Two of these isoforms are expressed in a constitutive manner (cNOS) predominantly in the vascular endothelium (eNOS, type III NOS) and in the nervous system (nNOS, type I NOS) and function in the maintenance of normal homeostasis. Under normal physiological conditions, these constitutive isoforms of NOS generate low levels of nitric oxide in response to increases in intracellular calcium concentrations. The expression of the third form (iNOS, type II NOS) is induced by endotoxin and/or inflammatory cytokines and generates high levels of nitric oxide over long periods of time. The excessive production of nitric oxide, generated either by iNOS or by the sustained activation of nNOS, elicits cellular cytotoxicity and tissue damage and is thought to contribute to the pathophysiology of human disease states. The development of selective inhibitors of iNOS and/or nNOS offers the potential of blocking the synthesis of a major injurious agent, nitric oxide, and ultimately reducing tissue damage during states of chronic inflammation or prolonged elevations in cytosolic calcium. In this review, the selective inhibition of the various isoforms of NOS is examined by structure activity relationships as unique targets for drug research and therapeutic intervention in a variety of disease states.

APA, Harvard, Vancouver, ISO, and other styles

Mattace Raso, Giuseppina, Emanuela Esposito, Anna Iacono, et al. "Leptin induces nitric oxide synthase type II in C6 glioma cells." Neuroscience Letters 396, no. 2 (2006): 121–26. http://dx.doi.org/10.1016/j.neulet.2005.11.022.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Murphy, S., and D. Grzybicki. "Induction of nitric oxide synthase (NOS) type II in experimental neuropathologies." Journal of Neuroimmunology 63, no. 1 (1995): 91. http://dx.doi.org/10.1016/0165-5728(96)80935-0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Angeline, T., H. R. Krithiga, W. Isabel, A. J. Asirvatham, and A. Poornima. "Endothelial Nitric Oxide Synthase Gene Polymorphism (G894T) and Diabetes Mellitus (Type II) among South Indians." Oxidative Medicine and Cellular Longevity 2011 (2011): 1–4. http://dx.doi.org/10.1155/2011/462607.

Full text

Abstract:

The objective of the study is to find out whether the endothelial nitric oxide synthase (eNOS) G894T single-nucleotide polymorphism is associated with type 2 diabetes mellitus in South Indian (Tamil) population. A total number of 260 subjects comprising 100 type 2 diabetic mellitus patients and 160 healthy individuals with no documented history of diabetes were included for the study. DNA was isolated, and eNOS G894T genotyping was performed using the polymerase chain reaction followed by restriction enzyme analysis usingBan II. The genotype distribution in patients and controls were compatible with the Hardy-Weinberg expectations (P>0.05). Odds ratio indicates that the occurrence of mutant genotype (GT/TT) was 7.2 times (95% CI = 4.09–12.71) more frequent in the cases than in controls. Thus, the present study demonstrates that there is an association of endothelial nitric oxide synthase gene (G894T) polymorphism with diabetes mellitus among South Indians.

APA, Harvard, Vancouver, ISO, and other styles

Tracey, W. Ross, Masaki Nakane, Fatima Basha, and George Carter. "In vivo pharmacological evaluation off two novel type II (inducible) nitric oxide synthase inhibitors." Canadian Journal of Physiology and Pharmacology 73, no. 5 (1995): 665–69. http://dx.doi.org/10.1139/y95-085.

Full text

Abstract:

Selective type II (inducible) nitric oxide synthase (NOS) inhibitors have several potential therapeutic applications, including treatment of sepsis, diabetes, and autoimmune diseases. The ability of two novel, selective inhibitors of type II NOS, S-ethylisothiourea (EIT) and 2-amino-5,6-dihydro-6-methyl-4H-1,3-thiazine (AMT), to inhibit type II NOS function in vivo was studied in lipopolysaccharide (LPS) treated rats. Type II NOS activity was assessed by measuring changes in plasma nitrite and nitrate concentrations ([NOx]). Both EIT and AMT elicited a dose-dependent and >95% inhibition of the LPS-induced increase in plasma [NOx]. The ED50 values for EIT and AMT were 0.4 and 0.2 mg/kg, respectively. In addition, the administration of LPS and either NOS inhibitor resulted in a dose-dependent increase in animal mortality; neither compound was lethal when administered alone. Pretreatment with L-arginine (but not D-arginine) prevented the mortality, while not affecting the type II NOS-dependent NO production, suggesting the toxicity may be due to inhibition of one of the other NOS isoforms (endothelial or neuronal). Thus, although EIT and AMT are potent inhibitors of type II NOS function in vivo, type II NOS inhibitors of even greater selectivity may need to be developed for therapeutic applications.Key words: nitric oxide, nitrite, nitrate, sepsis, lipopolysaccharide.

APA, Harvard, Vancouver, ISO, and other styles

Chandler, L. J., K. Kopnisky, E. Richards, F. T. Crews, and C. Sumners. "Angiotensin II decreases inducible nitric oxide synthase expression in rat astroglial cultures." American Journal of Physiology-Cell Physiology 268, no. 3 (1995): C700—C707. http://dx.doi.org/10.1152/ajpcell.1995.268.3.c700.

Full text

Abstract:

Consistent with stimulation of expression of an inducible form of nitric oxide synthase (iNOS), exposure of rat astroglial cultures to lipopolysaccharide (LPS) caused a time-dependent increase in the accumulation of nitrite in the culture media. Addition of the peptide angiotensin II (ANG II) with LPS decreased subsequent formation of nitrite in a concentration-dependent manner (concentration inhibiting 50% of maximal response approximately 1 nM). The ANG II effect could be blocked by the ANG II type 1 (AT1 receptor antagonist losartan but not by the ANG II type 2 (AT2) receptor antagonist PD-123177. ANG II had no effect on nitrite formation stimulated by a combination of inflammatory cytokines (interleukin-1 beta, tumor necrosis factor-alpha, and interferon-gamma). A brief 10-min exposure to ANG II was sufficient to cause an approximately 30% inhibition of the LPS response, with maximal inhibition of approximately 65% after 3 h, and occurred only when ANG II was added during the iNOS induction phase. Consistent with partial inhibition of LPS-stimulated expression of iNOS, ANG II reduced the levels of both iNOS mRNA and iNOS protein. These results demonstrate that ANG II can decrease LPS-stimulated NO production in astroglia by inhibiting induction of iNOS expression.

APA, Harvard, Vancouver, ISO, and other styles

Blau, H., S. Riklis, J. F. Van Iwaarden, F. X. McCormack, and M. Kalina. "Nitric oxide production by rat alveolar macrophages can be modulated in vitro by surfactant protein A." American Journal of Physiology-Lung Cellular and Molecular Physiology 272, no. 6 (1997): L1198—L1204. http://dx.doi.org/10.1152/ajplung.1997.272.6.l1198.

Full text

Abstract:

Alveolar macrophage and type II cells are known to generate nitric oxide, which is a highly reactive molecule that plays a role in host defense against pathogens, as well as tissue damage associated with inflammation in the lung. Both types of cells are known to generate the nitric oxide by inducible nitric oxide synthase (iNOS). Surfactant-associated protein A (SP-A) from various sources (human alveolar proteinosis, rat and recombinant rat) was found to upregulate nitric oxide production by alveolar macrophages in a concentration- and time-dependent manner, whereas type II cells were unresponsive to SP-A. The increase in nitric oxide production was associated with elevation in the expression of iNOS. However, only 30-50% of the cells responded by expressing iNOS, as was observed by immunofluorescence staining. The stimulatory effect of SP-A was found to be 30-50% lower than the known nitric oxide agonists interferon-gamma (IFN-gamma) and lipopolysaccharide (LPS). However, addition of the cytokines interleukin-1 or granulocyte macrophage colony-stimulating factor elevated the levels of nitric oxide production to that of LPS and IFN-gamma. Special attention was given to exclude the possibility that contaminating LPS in the various SP-A species stimulated nitric oxide production by the macrophages. Our results indicate that SP-A is the agonist and not a contaminating LPS. The data presented in this report extend our knowledge regarding the nonsurfactant-related functions of SP-A.

APA, Harvard, Vancouver, ISO, and other styles

Wang, Hai. "Increased hepatic expression of nitric oxide synthase type II in cirrhotic rats." World Journal of Gastroenterology 10, no. 13 (2004): 1923. http://dx.doi.org/10.3748/wjg.v10.i13.1923.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Price, Suzanna, Jane A. Mitchell, Peter B. Anning, and Timothy W. Evans. "Type II nitric oxide synthase activity is cardio-protective in experimental sepsis." European Journal of Pharmacology 472, no. 1-2 (2003): 111–18. http://dx.doi.org/10.1016/s0014-2999(03)01826-0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Park, Song Kyu, and Sean Murphy. "Nitric Oxide Synthase Type II mRNA Stability Is Translation- and Transcription-Dependent." Journal of Neurochemistry 67, no. 4 (2002): 1766–69. http://dx.doi.org/10.1046/j.1471-4159.1996.67041766.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

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 (2009): 343–49. http://dx.doi.org/10.3171/2008.6.17608.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

Rajapakse, Niwanthi W., Amanda K. Sampson, Gabriela A. Eppel, and Roger G. Evans. "Angiotensin II and nitric oxide in neural control of intrarenal blood flow." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 289, no. 3 (2005): R745—R754. http://dx.doi.org/10.1152/ajpregu.00477.2004.

Full text

Abstract:

We investigated the roles of the renin-angiotensin system and the significance of interactions between angiotensin II and nitric oxide, in responses of regional kidney perfusion to electrical renal nerve stimulation (RNS) in pentobarbital sodium-anesthetized rabbits. Under control conditions, RNS (0.5–8 Hz) reduced total renal blood flow (RBF; −89 ± 3% at 8 Hz) and cortical perfusion (CBF; −90 ± 2% at 8 Hz) more than medullary perfusion (MBF; −55 ± 5% at 8 Hz). Angiotensin II type 1 (AT1)-receptor antagonism (candesartan) blunted RNS-induced reductions in RBF ( P = 0.03), CBF ( P = 0.007), and MBF ( P = 0.04), particularly at 4 and 8 Hz. Nitric oxide synthase inhibition with NG-nitro-l-arginine (l-NNA) enhanced RBF ( P = 0.003), CBF ( P = 0.001), and MBF ( P = 0.03) responses to RNS, particularly at frequencies of 2 Hz and less. After candesartan pretreatment, l-NNA significantly enhanced RNS-induced reductions in RBF ( P = 0.04) and CBF ( P = 0.007) but not MBF ( P = 0.66). Renal arterial infusion of angiotensin II (5 ng·kg−1·min−1) selectively enhanced responses of MBF to RNS in l-NNA-pretreated but not in vehicle-pretreated rabbits. In contrast, greater doses of angiotensin II (5–15 ng·kg−1·min−1) blunted responses of MBF to RNS in rabbits with intact nitric oxide synthase. These results suggest that endogenous angiotensin II enhances, whereas nitric oxide blunts, neurally mediated vasoconstriction in the renal cortical and medullary circulations. In the renal medulla, but not the cortex, angiotensin II also appears to be able to blunt neurally mediated vasoconstriction.

APA, Harvard, Vancouver, ISO, and other styles

Velasco, M., M. J. Díaz-Guerra, P. Díaz-Achirica, D. Andreu, L. Rivas, and L. Boscá. "Macrophage triggering with cecropin A and melittin-derived peptides induces type II nitric oxide synthase expression." Journal of Immunology 158, no. 9 (1997): 4437–43. http://dx.doi.org/10.4049/jimmunol.158.9.4437.

Full text

Abstract:

Abstract Triggering of RAW 264.7 cells with a cecropin A-melittin hybrid peptide (CA(1-8)M(1-18)) promoted a rapid rise in the intracellular calcium concentration that was followed, after a lag period of 6 h, by nitric oxide synthesis through the expression of the cytokine-inducible form of nitric oxide synthase (type II NOS or iNOS). The maximal effect was obtained at peptide concentrations in the 2 to 5-microM range. Simultaneous incubation with the peptide and LPS abrogated the nitric oxide synthesis elicited after LPS treatment of the cells. CA(1-8)M(1-18) induced a rapid activation of nuclear factor kappaB as evidenced by the presence of p50/p65 heterodimers of the nuclear factor kappaB/c-Rel family in the nuclei of activated cells. This peptide also activated the reporter activity of cells transfected with a plasmid harboring a 1-kb fragment corresponding to the 5'-flanking region of the murine iNOS gene. CA(1-8)M(1-18) promoted apoptotic cell death at concentrations below 1 to 2 microM, whereas higher concentrations altered the plasma membrane integrity. These results suggest the involvement of multiple intracellular signaling pathways in the mechanism by which this peptide elicits macrophage triggering.

APA, Harvard, Vancouver, ISO, and other styles

Sunil, Vasanthi R., Agnieszka J. Connor, Yan Guo, Jeffrey D. Laskin, and Debra L. Laskin. "Activation of type II alveolar epithelial cells during acute endotoxemia." American Journal of Physiology-Lung Cellular and Molecular Physiology 282, no. 4 (2002): L872—L880. http://dx.doi.org/10.1152/ajplung.00217.2001.

Full text

Abstract:

Lung injury induced by acute endotoxemia is associated with increased generation of inflammatory mediators such as nitric oxide and eicosanoids, which have been implicated in the pathophysiological process. Although production of these mediators by alveolar macrophages (AM) has been characterized, the response of type II cells is unknown and was assessed in the present studies. Acute endotoxemia caused a rapid (within 1 h) and prolonged (up to 48 h) induction of nitric oxide synthase-2 (NOS-2) in type II cells but a delayed response in AM (12–24 h). In both cell types, this was associated with increased nitric oxide production. Although type II cells, and to a lesser extent AM, constitutively expressed cyclooxygenase-2, acute endotoxemia did not alter this activity. Endotoxin administration had no effect on mitogen-activated protein kinase or protein kinase B-α (PKB-α) expression. However, increases in phosphoinositide 3-kinase and phospho-PKB-α were observed in type II cells. The finding that this was delayed for 12–24 h suggests that these proteins do not play a significant role in the regulation of NOS-2 in this model. After endotoxin administration to rats, a rapid (within 1–2 h) activation of nuclear factor-κB was observed. This response was transient in type II cells but was sustained in AM. Interferon regulatory factor-1 (IRF-1) was also activated rapidly in type II cells. In contrast, IRF-1 activation was delayed in AM. These data demonstrate that type II cells, like AM, are highly responsive during acute endotoxemia and may contribute to pulmonary inflammation.

APA, Harvard, Vancouver, ISO, and other styles

Carolina, Pustrovh, Alicia Jawerbaum, Sinner Debora, Perotti Christian, Martha A. F. Gimeno, and Elida T. Gonzalez. "Diminished levels of prostaglandin E in type I diabetic oocyte - cumulus complexes. Influence of nitric oxide and superoxide dismutase." Reproduction, Fertility and Development 11, no. 2 (1999): 105. http://dx.doi.org/10.1071/rd99033.

Full text

Abstract:

In the present work the prostaglandin E (PGE) production by ovulated, immature and in vitromatured oocyte–cumulus complexes (OCC) was evaluated in a rat model of type I diabetes induced by streptozotocin (60 mg kg–1). A diminished number of ovulated OCC were found in the type I diabetic rat. In contrast to the increment in PGE generation found previously in OCC and embryos from type II diabetic rats, it was found that PGE production by type I diabetic OCC was diminished in comparison with the controls. Nitric oxide synthase (NOS) activity is enhanced in proestrous ovaries from type I diabetic rats, but cGMP levels are diminished. SIN-1 (300 µМ), a nitric oxide donor, significantly enhanced PGE generation by control OCC, but was unable to modify the PGE levels in type I diabetic OCC. L-NMMA, a nitric oxide inhibitor that diminished PGE values in type II diabetic OCC, did not modify PGE generation in either control and type I diabetic OCC. Superoxide dismutase (SOD, 1000 U mL–1), and SOD (1000 U mL–1) plus SIN-1 (300 µМ), enhanced PGE generation by both control and diabetic OCC. The present results suggest that even when nitric oxide (NO) is overproduced in diabetic ovaries, the NO–PGE pathway is impaired in type I diabetic OCC. As SOD additions are able to increase PGE generation by diabetic OCC, high concentrations of free oxygen radicals might be quenching the NO, impairing its physiological functions.

APA, Harvard, Vancouver, ISO, and other styles

Miles, P. R., L. Bowman, and L. Huffman. "Nitric oxide alters metabolism in isolated alveolar type II cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 271, no. 1 (1996): L23—L30. http://dx.doi.org/10.1152/ajplung.1996.271.1.l23.

Full text

Abstract:

Alveolar type II cells may be exposed to nitric oxide (.NO) from external sources, and these cells can also generate .NO. Therefore we studied the effects of altering .NO levels on various type II cell metabolic processes. Incubation of cells with the .NO generator, S-nitroso-N-acetylpenicillamine (SNAP; 1 mM), leads to reductions of 60-70% in the synthesis of disaturated phosphatidylcholines (DSPC) and cell ATP levels. Cellular oxygen consumption, an indirect measure of cell ATP synthesis, is also reduced by SNAP. There is no direct effect of SNAP on lung mitochondrial ATP synthesis, suggesting that .NO does not directly inhibit this process. On the other hand, incubation of cells with NG-nitro-L-arginine methyl ester (L-NAME), an inhibitor of nitric oxide synthase (NOS), the enzyme responsible for .NO synthesis, results in increases in DSPC synthesis, cell ATP content, and cellular oxygen consumption. The L-NAME effects are reversed by addition of L-arginine, the substrate for NOS. Production of .NO by type II cells is inhibited by L-NAME, a better inhibitor of constitutive NOS (cNOS) than inducible NOS (iNOS), and is reduced in the absence of external calcium. Aminoguanidine, a specific inhibitor of iNOS, has no effect on cell ATP content or on .NO production. These results indicate that alveolar type II cell lipid and energy metabolism can be affected by .NO and suggest that there may be cNOS activity in these cells.

APA, Harvard, Vancouver, ISO, and other styles

Zhang, Hanfang, Connie Snead, and John D. Catravas. "Nitric Oxide Differentially Regulates Induction of Type II Nitric Oxide Synthase in Rat Vascular Smooth Muscle Cells Versus Macrophages." Arteriosclerosis, Thrombosis, and Vascular Biology 21, no. 4 (2001): 529–35. http://dx.doi.org/10.1161/01.atv.21.4.529.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Suzuki, Hiroyuki, Kunie Eguchi, Haruhiko Ohtsu, et al. "Activation of Endothelial Nitric Oxide Synthase by the Angiotensin II Type 1 Receptor." Endocrinology 147, no. 12 (2006): 5914–20. http://dx.doi.org/10.1210/en.2006-0834.

Full text

Abstract:

Enhanced angiotensin II (AngII) action has been implicated in endothelial dysfunction that is characterized as decreased nitric oxide availability. Although endothelial cells have been reported to express AngII type 1 (AT1) receptors, the exact role of AT1 in regulating endothelial NO synthase (eNOS) activity remains unclear. We investigated the possible regulation of eNOS through AT1 in bovine aortic endothelial cells (BAECs) and its functional significance in rat aortic vascular smooth muscle cells (VSMCs). In BAECs infected with adenovirus encoding AT1 and in VSMCs infected with adenovirus encoding eNOS, AngII rapidly stimulated phosphorylation of eNOS at Ser1179. This was accompanied with increased cGMP production. These effects were blocked by an AT1 antagonist. The cGMP production was abolished by a NOS inhibitor as well. To explore the importance of eNOS phosphorylation, VSMCs were also infected with adenovirus encoding S1179A-eNOS. AngII did not stimulate cGMP production in VSMCs expressing S1179A. However, S1179A was able to enhance basal NO production as confirmed with cGMP production and enhanced vasodilator-stimulated phosphoprotein phosphorylation. Interestingly, S1179A prevented the hypertrophic response similar to wild type in VSMCs. From these data, we conclude that the AngII/AT1 system positively couples to eNOS via Ser1179 phosphorylation in ECs and VSMCs if eNOS and AT1 coexist. However, basal level NO production may be sufficient for prevention of AngII-induced hypertrophy by eNOS expression. These data demonstrate a novel molecular mechanism of eNOS regulation and function and thus provide useful information for eNOS gene therapy under endothelial dysfunction.

APA, Harvard, Vancouver, ISO, and other styles

Morris, Sidney M., Diane Kepka-Lenhart, and Li-Chun Chen. "Differential regulation of arginases and inducible nitric oxide synthase in murine macrophage cells." American Journal of Physiology-Endocrinology and Metabolism 275, no. 5 (1998): E740—E747. http://dx.doi.org/10.1152/ajpendo.1998.275.5.e740.

Full text

Abstract:

Activated macrophages avidly consume arginine via the action of inducible nitric oxide synthase (iNOS) and/or arginase. In contrast to our knowledge regarding macrophage iNOS expression, the stimuli and mechanisms that regulate expression of the cytosolic type I (arginase I) or mitochondrial type II (arginase II) isoforms of arginase in macrophages are poorly defined. We show that one or both arginase isoforms may be induced in the RAW 264.7 murine macrophage cell line and that arginase expression is regulated independently of iNOS expression. For example, 8-bromo-cAMP strongly induced both arginase I and II mRNAs but not iNOS. Whereas interferon-γ induced iNOS but not arginase, 8-bromo-cAMP and interferon-γ mutually antagonized induction of iNOS and arginase I mRNAs. Dexamethasone, which did not induce either arginase or iNOS, almost completely abolished induction of arginase I mRNA by 8-bromo-cAMP but enhanced induction of arginase II mRNA. Lipopolysaccharide (LPS) induced arginase II mRNA, but 8-bromo-cAMP plus LPS resulted in synergistic induction of both arginase I and II mRNAs. In all cases, increases in arginase mRNAs were sufficient to account for the increases in arginase activity. These complex patterns of expression suggest that the arginase isoforms may play distinct, although partially overlapping, functional roles in macrophage arginine metabolism.

APA, Harvard, Vancouver, ISO, and other styles

Alhamyani, Abdulrahman, A. S. M. Hasan Mahmood, Ayed Alshamrani, Mostafa M. H. Ibrahim, and Karen P. Briski. "Central Type II Glucocorticoid Receptor Regulation of Ventromedial Hypothalamic Nucleus Glycogen Metabolic Enzyme and Glucoregulatory Neurotransmitter Marker Protein Expression in the Male Rat." Journal of Endocrinology and Diabetes 8, no. 1 (2021): 1–12. http://dx.doi.org/10.15226/2374-6890/8/1/001148.

Full text

Abstract:

The ventromedial hypothalamic nucleus (VMN) glucoregulatory neurotransmitters γ-aminobutyric acid (GABA) and nitric oxide (NO) signal adjustments in glycogen mobilization. Glucocorticoids control astrocyte glycogen metabolism in vitro. The classical (type II) glucocorticoid receptor (GR) is expressed in key brain structures that govern glucostasis, including the VMN. Current research addressed the hypothesis that forebrain GR regulation of VMN glycogen synthase (GS) and phosphorylase (GP) protein expression correlates with control of glucoregulatory transmission. Groups of male rats were pretreated by intracerebroventricular (icv) delivery of the GR antagonist RU486 or vehicle prior to insulin-induced hypoglycemia (IIH), or were pretreated icv with dexamethasone (DEX) or vehicle before subcutaneous insulin diluent injection. DEX increased VMN GS and norepinephrine-sensitive GP-muscle type (GPmm), but did not alter metabolic deficit-sensitive GP-brain type (GPbb) expression. RU486 enhanced GS and GPbb profiles during IIH. VMN astrocyte (MCT1) and neuronal (MCT2) monocarboxylate transporter profiles were up-regulated in euglycemic and hypoglycemic animals by DEX or RU486, respectively. Glutamate decarboxylase65/67 and neuronal nitric oxide synthase (nNOS) proteins were both increased by DEX, yet RU486 augmented hypoglycemic nNOS expression patterns. Results show that GR exert divergent effects on VMN GS, MCT1/2, and nNOS proteins during eu- (stimulatory) versus hypoglycemia (inhibitory); these findings imply that up-regulated NO transmission may reflect, in part, augmented glucose incorporation into glycogen and/or increased tissue lactate requirements. Data also provide novel evidence for metabolic state-dependent GR regulation of VMN GPmm and GPbb profiles; thus, GABA signaling of metabolic stability may reflect, in part, stimulus-specific glycogen breakdown during eu- versus hypoglycemia. Key Words: Glucocorticoid receptor; Ventromedial hypothalamic nucleus; RU486; Dexamethasone; Glycogen phosphorylase; Nitric oxide synthase

APA, Harvard, Vancouver, ISO, and other styles

Tracey, W. R., C. Xue, V. Klinghofer, et al. "Immunochemical detection of inducible NO synthase in human lung." American Journal of Physiology-Lung Cellular and Molecular Physiology 266, no. 6 (1994): L722—L727. http://dx.doi.org/10.1152/ajplung.1994.266.6.l722.

Full text

Abstract:

Type II (inducible) nitric oxide synthase (NOS) may play an important role in pulmonary pathophysiology, yet it remains controversial whether human tissues are capable of expressing this protein. Therefore, a polyclonal antibody (8196) was raised against type II NOS from induced RAW 264.7 macrophages and used to investigate the expression of this enzyme in human lung tissue. Anti-type II NOS antibody did not cross-react with either neuronal (type I) or endothelial (type III) constitutive NOS, whereas a 130-kDa protein was detected in cytosol from induced macrophages or liver removed from lipopolysaccharide (25 mg/kg)-treated rats. Cells or tissues that lacked NOS activity did not express immunoreactive proteins. Similarly, in grossly normal human lung tissue, no immunoreactivity was detected with the anti-type II NOS antibody. In contrast, strong immunoreactivity was detected in alveolar macrophages present in lung tissue from a patient with bronchiectasis and acute bronchopneumonia. These data demonstrate that human alveolar macrophages are able to express type II NOS and support a role for this enzyme in pulmonary inflammatory pathophysiology.

APA, Harvard, Vancouver, ISO, and other styles

Wang, Hui, Ze Yuan, Bianbian Wang, et al. "COMP (Cartilage Oligomeric Matrix Protein), a Novel PIEZO1 Regulator That Controls Blood Pressure." Hypertension 79, no. 3 (2022): 549–61. http://dx.doi.org/10.1161/hypertensionaha.121.17972.

Full text

Abstract:

Background: Vascular endothelial cells are critical for maintaining blood pressure (BP) by releasing biologically active molecules, such as nitric oxide. A non-endothelial cell resident matricellular protein, COMP (cartilage oligomeric matrix protein), plays a pivotal role in maintaining cardiovascular homeostasis, but little is known about its regulatory effect on BP. Methods: Mice were infused with AngII (angiotensin II; 450 ng/kg per minute) for 3 days via an osmotic minipump, and BP was monitored by a tail-cuff system. Second-order mesenteric arteries were isolated from mice for microvascular tension measurement. Nitric oxide was detected by an electron paramagnetic resonance technique. Small-interfering RNA transfection, co-immunoprecipitation, bioluminescence resonance energy transfer assays, and patch-clamp electrophysiology experiments were used for further detailed mechanism investigation. Results: COMP −/− mice displayed elevated BP and impaired acetylcholine-induced endothelium-dependent relaxation compared with wild-type mice with or without AngII. Inhibition of eNOS (endothelial nitric oxide synthase) abolished the difference in endothelium-dependent relaxation between wild-type and COMP −/− mice. Furthermore, COMP directly interacted with the C-terminus of Piezo1 via its C-terminus and activated the endogenous Piezo1 currents, which induced intracellular Ca 2+ influx, Ca 2+ /calmodulin-dependent protein kinase type II and eNOS activation, and nitric oxide production. The Piezo1 activator, Yoda1, reduced the difference in endothelium-dependent relaxation and BP in wild-type and COMP − /− mice. Moreover, COMP overexpression increased eNOS activation and improved endothelium-dependent relaxation and BP. Conclusions: Our study demonstrated that COMP is a novel Piezo1 regulator that plays a protective role in BP regulation by increasing cellular Ca 2+ influx, eNOS activity, and nitric oxide production.

APA, Harvard, Vancouver, ISO, and other styles

Chen, Jinn-Yang, Jen-Hwey Chiu, Hui-Ling Chen, Tzen-Wen Chen, Wu-Chang Yang, and An-Hang Yang. "Human Peritoneal Mesothelial Cells Produce Nitric Oxide: Induction by Cytokines." Peritoneal Dialysis International: Journal of the International Society for Peritoneal Dialysis 20, no. 6 (2000): 772–77. http://dx.doi.org/10.1177/089686080002000631.

Full text

Abstract:

Objective To investigate the induction of nitric oxide synthase type II (iNOS) in human peritoneal mesothelial cells (HPMC) using cytokines and bacterial lipopolysaccharide (LPS). Design Confluent monolayers of HPMC were exposed to cytokines [tumor necrosis factor alpha (TNFα), interleukin-1 beta (IL-1β), interferon gamma (IFNγ)] or LPS, individually or in various double and triple combinations, for 24 – 72 hours. Concentrations of nitrate and nitrite in the media were quantified using the Griess reaction and used as indirect indices of nitric oxide (NO) production. The expression of iNOS was assessed using reverse transcriptase-polymerase chain reaction (RT-PCR) and Western blot. Results Neither single cytokines nor LPS was able to induce iNOS mRNA or NO production. Both double combinations of TNFα+ IFNγ and IL-1β + IFNγ were able to induce iNOS mRNA expression, but only TNFα + IFNγ induced significant NO production. The triple combination of TNFα + IFNγ + IL-1β induced even more NO production than TNFα + IFNγ. There was no constitutive NO synthase type III (eNOS) expression in HPMC. Conclusions Certain combinations of cytokines could stimulate cultured HPMC to produce NO, and HPMC might be a source of intraperitoneal NO production during peritonitis.

APA, Harvard, Vancouver, ISO, and other styles

Sampath, Chethan, Shanthi Srinivasan, Michael L. Freeman та Pandu R. Gangula. "Inhibition of GSK-3β restores delayed gastric emptying in obesity-induced diabetic female mice". American Journal of Physiology-Gastrointestinal and Liver Physiology 319, № 4 (2020): G481—G493. http://dx.doi.org/10.1152/ajpgi.00227.2020.

Full text

Abstract:

Inhibition of glycogen synthase kinase 3β (GSK-3β) with SB 216763 attenuates delayed gastric emptying through gastric nuclear factor erythroid 2-related factor 2 (Nrf2) -phase II enzymes in high-fat diet-fed female mice. SB 216763 restored impaired gastric PI3K/AKT/ β-catenin/caspase 3 expression. Inhibition of GSK-3β normalized gastric dihydrofolate reductase, neuronal nitric oxide synthase-α expression, dimerization and nitrergic relaxation. SB 216763 normalized both serum estrogen and nitrate levels in female obese/Type 2 diabetes mice. SB 216763 reduced downstream signaling of GSK-3β in enteric neuronal cells in vitro.

APA, Harvard, Vancouver, ISO, and other styles

Oh, Seung Jun, Yang-Gi Min, Seung-Ju Lee, Jeong-Whun Kim, and Peter R. Jarin. "Expression of Nitric Oxide Synthases in Nasal Mucosa from a Mouse Model of Allergic Rhinitis." Annals of Otology, Rhinology & Laryngology 112, no. 10 (2003): 899–903. http://dx.doi.org/10.1177/000348940311201013.

Full text

Abstract:

Nitric oxide (NO), which is produced by nitric oxide synthase (NOS), has been recently identified as a multifunctional mediator. As for nasal tissue, however, the distribution and expression patterns of 3 isoforms of NOS, including neuronal NOS (nNOS, type I NOS), inducible NOS (iNOS, type II NOS), and endothelial NOS (eNOS, type III NOS), are still unclear. To evaluate the function of NO in the pathophysiology of nasal allergy, we investigated the distribution of NOSs in the nasal mucosa of C57BL/6 mice with allergic rhinitis to the house dust mite, Dermatophagoides farinae. Immunoreactivity to each isoform of NOS was immunohisto-chemically observed. In the allergic nasal mucosa, many eosinophils had infiltrated. Immunoreactivity to NOS types I and III was localized to the surface epithelial and vascular endothelial cells in both allergic and control groups without a statistically significant difference. In contrast, the type II NOS immunoreactivity was weak in normal mice and increased after allergic sensitization. The type II NOS expression of the surface epithelial and vascular endothelial cells was significantly elevated in the allergic group as compared with the control group. These findings suggest that a large amount of NO may be produced in the nasal mucosa of mice by type II NOS after allergic sensitization and that type II NOS may play an important role in the pathogenesis of allergic rhinitis.

APA, Harvard, Vancouver, ISO, and other styles

Pechkovsky, D. V., G. Zissel, T. Goldmann, et al. "Pattern of NOS2 and NOS3 mRNA expression in human A549 cells and primary cultured AEC II." American Journal of Physiology-Lung Cellular and Molecular Physiology 282, no. 4 (2002): L684—L692. http://dx.doi.org/10.1152/ajplung.00320.2000.

Full text

Abstract:

The human alveolar type II epithelium-like cell line A549 expresses nitric oxide synthase type 2 (NOS2), but not NOS3, and produces nitric oxide (NO) upon appropriate stimulation. However, relatively little is known regarding the NOS2 and NOS3 expression of type II human alveolar epithelial cells (AEC II) in primary culture. We detected NOS3 mRNA in freshly isolated AEC II and after 24 h of culture. NOS3 mRNA levels were much higher in AEC II cultured for 24 h with or without interferon-γ, interleukin-1β, and tumor necrosis factor-α, compared with freshly isolated cells. Cytokine stimulation did not change the NOS3 mRNA expression level in AEC II compared with unstimulated cells. NOS3 protein expression was verified by Western blot, and measuring nitrate/nitrite revealed that the protein is active. In contrast, neither NOS2 mRNA nor protein could be detected in freshly isolated, unstimulated or cytokine-stimulated human AEC II in 24- or 72-h primary cultures, whereas A549 cells expressed NOS2 message and protein upon stimulation with proinflammatory cytokines. In situ hybridization confirmed that AEC II express NOS3, but not NOS2 mRNA in vivo. These data demonstrate that there are significant differences between primary AEC II and A549 cells in NOS mRNA expression pattern.

APA, Harvard, Vancouver, ISO, and other styles

Schwaninger, RoseAnn M., Hong Sun, and William G. Mayhan. "Impaired nitric oxide synthase-dependent dilatation of cerebral arterioles in type II diabetic rats." Life Sciences 73, no. 26 (2003): 3415–25. http://dx.doi.org/10.1016/j.lfs.2003.06.029.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Loot, Annemarieke E., Judith G. Schreiber, Beate Fisslthaler, and Ingrid Fleming. "Angiotensin II impairs endothelial function via tyrosine phosphorylation of the endothelial nitric oxide synthase." Journal of Experimental Medicine 206, no. 13 (2009): 2889–96. http://dx.doi.org/10.1084/jem.20090449.

Full text

Abstract:

Proline-rich tyrosine kinase 2 (PYK2) can be activated by angiotensin II (Ang II) and reactive oxygen species. We report that in endothelial cells, Ang II enhances the tyrosine phosphorylation of endothelial NO synthase (eNOS) in an AT1-, H2O2-, and PYK2-dependent manner. Low concentrations (1–100 µmol/liter) of H2O2 stimulated the phosphorylation of eNOS Tyr657 without affecting that of Ser1177, and attenuated basal and agonist-induced NO production. In isolated mouse aortae, 30 µmol/liter H2O2 induced phosphorylation of eNOS on Tyr657 and impaired acetylcholine-induced relaxation. Endothelial overexpression of a dominant-negative PYK2 mutant protected against H2O2-induced endothelial dysfunction. Correspondingly, carotid arteries from eNOS−/− mice overexpressing the nonphosphorylatable eNOS Y657F mutant were also protected against H2O2. In vivo, 3 wk of treatment with Ang II considerably increased levels of Tyr657-phosphorylated eNOS in the aortae of wild-type but not Nox2y/− mice, and this was again associated with a clear impairment in endothelium-dependent vasodilatation in the wild-type but not in the Nox2y/− mice. Collectively, endothelial PYK2 activation by Ang II and H2O2 causes the phosphorylation of eNOS on Tyr657, attenuating NO production and endothelium-dependent vasodilatation. This mechanism may contribute to the endothelial dysfunction observed in cardiovascular diseases associated with increased activity of the renin–angiotensin system and elevated redox stress.

APA, Harvard, Vancouver, ISO, and other styles

Reiser, Peter J., William O. Kline, and Pal L. Vaghy. "Induction of neuronal type nitric oxide synthase in skeletal muscle by chronic electrical stimulation in vivo." Journal of Applied Physiology 82, no. 4 (1997): 1250–55. http://dx.doi.org/10.1152/jappl.1997.82.4.1250.

Full text

Abstract:

Reiser, Peter J., William O. Kline, and Pal L. Vaghy.Induction of neuronal type nitric oxide synthase in skeletal muscle by chronic electrical stimulation in vivo. J. Appl. Physiol. 82(4): 1250–1255, 1997.—Fast-twitch skeletal muscles contain more neuronal-type nitric oxide synthase (nNOS) than slow-twitch muscles because nNOS is present only in fast (type II) muscle fibers. Chronic in vivo electrical stimulation of tibialis anterior and extensor digitorum longus muscles of rabbits was used as a method of inducing fast-to-slow fiber type transformation. We have studied whether an increase in muscle contractile activity induced by electrical stimulation alters nNOS expression, and if so, whether the nNOS expression decreases to the levels present in slow muscles. Changes in the expression of myosin heavy chain isoforms and maximum velocity of shortening of skinned fibers indicated characteristic fast-to-slow fiber type transformation after 3 wk of stimulation. At the same time, activity of NOS doubled in the stimulated muscles, and this correlated with an increase in the expression of nNOS shown by immunoblot analysis. These data suggest that nNOS expression in skeletal muscle is regulated by muscle activity and that this regulation does not necessarily follow the fast-twitch and slow-twitch pattern during the dynamic phase of phenotype transformation.

APA, Harvard, Vancouver, ISO, and other styles

Cho, Sunghee, Eun-Mi Park, Ping Zhou, Kelly Frys, M. Elizabeth Ross, and Costantino Iadecola. "Obligatory Role of Inducible Nitric Oxide Synthase in Ischemic Preconditioning." Journal of Cerebral Blood Flow & Metabolism 25, no. 4 (2005): 493–501. http://dx.doi.org/10.1038/sj.jcbfm.9600058.

Full text

Abstract:

Sublethal insults can induce a transient tolerance toward subsequent lethal ischemia, a phenomenon termed ischemic preconditioning (IPC). In the myocardium, nitric oxide derived from ‘inducible’ nitric oxide synthase (iNOS or NOS II) plays a critical role in the expression of IPC produced by sublethal ischemia. Here, we investigated whether iNOS is involved in IPC in brain. Ischemic preconditioning was produced in mice by three episodes of 1-min bilateral common carotid artery (BCCA) occlusion, each followed by 5 mins of reperfusion. After 24 h, mice underwent middle cerebral artery (MCA) occlusion for 20 mins. Intraischemic cerebral blood flow was monitored during both in BCCA and MCA occlusion (MCAO) by laser-Doppler flowmetry. Mice were killed 3 days after MCAO, and infarct volume was determined in thionine-stained sections. Infarct volume was significantly reduced 24 h after IPC (70%; P<0.05). Treatment with the iNOS inhibitor aminoguanidine (400 mg/kg), abolished the IPC-induced protection. Furthermore, IPC failed to induce ischemic tolerance in iNOS-null mice. In wild-type mice, IPC increased the resistance to Ca2+-mediated depolarization in isolated brain mitochondria. However, in iNOS-null mice IPC failed to induce such resistance. We conclude that iNOS is required for the full expression of IPC and that such effect is coupled to an increased resistance of mitochondria to injury. Thus, iNOS-derived nitric oxide, in addition to its deleterious effects on the late stages of ischemic brain damage, can also be beneficial by promoting ischemic tolerance through signaling, ultimately resulting in mitochondrial protection.

APA, Harvard, Vancouver, ISO, and other styles

Suehiro, Takaichi, Kazuhiko Tsuruya, Hirofumi Ikeda, et al. "Systemic Aldosterone, But Not Angiotensin II, Plays a Pivotal Role in the Pathogenesis of Renal Injury in Chronic Nitric Oxide-Deficient Male Rats." Endocrinology 156, no. 7 (2015): 2657–66. http://dx.doi.org/10.1210/en.2014-1369.

Full text

Abstract:

Chronic inhibition of nitric oxide synthase by Nω-nitro-L-arginine methyl ester (L-NAME) causes progressive renal injury and systemic hypertension. Angiotensin II (Ang II) has been conventionally regarded as one of the primary causes of renal injury. We reported previously that such renal injury was almost completely suppressed by both an Ang II type I receptor blocker and an aldosterone antagonist. The aldosterone antagonist also inhibited the systemic Ang II elevation. Therefore, it remains to be elucidated whether Ang II or aldosterone directly affects the development of such renal injury. In the present study, we investigated the role of aldosterone in the pathogenesis of renal injury induced by L-NAME-mediated chronic nitric oxide synthase inhibition in male Wistar rats (aged 10 wk). Serial analyses demonstrated that the renal injury and inflammation in L-NAME-treated rats was associated with elevation of both Ang II and aldosterone. To investigate the direct effect of aldosterone on the renal injury, we conducted adrenalectomy (ADX) and aldosterone supplementation in L-NAME-treated rats. In ADX rats, aldosterone was undetectable, and renal injury and inflammation were almost completely prevented by ADX, although systemic and local Ang II and blood pressure were still elevated. Aldosterone supplementation reversed the beneficial effect of ADX. The present study indicates that aldosterone rather than Ang II plays a central and direct role in the pathogenesis of renal injury by L-NAME through inflammation, independent of its systemic hemodynamic effects.

APA, Harvard, Vancouver, ISO, and other styles

Jesmin, S., I. Sakuma, A. Salah-Eldin, K. Nonomura, Y. Hattori, and A. Kitabatake. "Diminished penile expression of vascular endothelial growth factor and its receptors at the insulin-resistant stage of a type II diabetic rat model: a possible cause for erectile dysfunction in diabetes." Journal of Molecular Endocrinology 31, no. 3 (2003): 401–18. http://dx.doi.org/10.1677/jme.0.0310401.

Full text

Abstract:

Erectile dysfunction (ED) is commonly experienced in men with diabetes mellitus. Vascular endothelial growth factor (VEGF) has been extensively documented for its pathogenic significance in different complications of diabetes. We hypothesized that expressions of VEGF, its receptors and its signaling pathway Akt may be drastically altered in diabetic penile tIssues and their alterations may modulate penile expression of the molecules that are believed to play a role in diabetic ED. Otsuka Long-Evans Fatty (OLETF) rats, a type II (non-insulin-dependent) diabetes mellitus, were used at the insulin-resistant stage of type II diabetes (20 weeks of age). We determined protein and mRNA expressions of VEGF, its receptors, Akt, nitric oxide synthase isoforms, and apoptosis-related molecules in the penis using immunohistochemistry, Western blotting, in situ hybridization, and real-time quantitative PCR analyses. The penile sections were also submitted to the Tdt-mediated dUTP nick end labeling assay for apoptosis. OLETF rats showed marked reductions in penile expression of VEGF, its two receptors and Akt. In OLETF rat penises, endothelial and neuronal nitric oxide synthase isoforms were expressed less abundantly. Furthermore, while anti-apoptotic markers, Bcl-2 and phosphorylated Bad, were down-regulated, pro-apoptotic markers, active caspase-3 and Bax, were up-regulated, resulting in the appearance of apoptotic cells in the penile tIssues of OLETF rats. The VEGF signaling system would work less well in diabetic penile tIssues as a result of the reduced expression, leading to diminished endothelial production of nitric oxide and apoptosis-related erectile tIssue damage. We propose that the abnormalities of the VEGF signaling system in the penis may play a role in the pathophysiology of diabetic ED.

APA, Harvard, Vancouver, ISO, and other styles

Matsuhisa, Seiji, Hajime Otani, Toru Okazaki, et al. "Angiotensin II type 1 receptor blocker preserves tolerance to ischemia-reperfusion injury in Dahl salt-sensitive rat heart." American Journal of Physiology-Heart and Circulatory Physiology 294, no. 6 (2008): H2473—H2479. http://dx.doi.org/10.1152/ajpheart.91533.2007.

Full text

Abstract:

Oxidative stress is involved in the tolerance to ischemia-reperfusion (I/R) injury. Because angiotensin II type 1 receptor blockers (ARBs) inhibit oxidative stress, there is concern that ARBs abolish the tolerance to I/R injury. Dahl salt-sensitive (DS) hypertensive and salt-resistant (DR) normotensive rats received an antioxidant, 2-mercaptopropionylglycine (MPG), or an ARB, losartan, for 7 days. Losartan and MPG significantly inhibited oxidative stress as determined by tissue malondialdehyde + 4-hydroxynoneal and increased expression of inducible nitric oxide synthase (iNOS) in the DS rat heart. However, losartan but not MPG activated endothelial nitric oxide synthase (eNOS) as assessed by phosphorylation of eNOS on Ser1177. Infarct size after 30-min left coronary artery occlusion followed by 2-h reperfusion was comparable between DS and DR rat hearts. Although MPG and losartan had no effect on infarct size in the DR rat heart, MPG but not losartan significantly increased infarct size in the DS rat heart. A selective iNOS inhibitor, 1400W, increased infarct size in the DS rat heart, but it had no effect on infarct size in the losartan-treated DS rat heart. However, a nonselective NOS inhibitor, Nω-nitro-l-arginine methyl ester, increased infarct size in the losartan-treated DS rat heart. These results suggest that losartan preserves the tolerance to I/R injury by activating eNOS despite elimination of redox-sensitive upregulation of iNOS and iNOS-dependent cardioprotection in the DS rat heart.

APA, Harvard, Vancouver, ISO, and other styles

Nakatake, Richi, Hiroya Iida, Morihiko Ishizaki, et al. "Metformin inhibits expression of the proinflammatory biomarker inducible nitric oxide synthase in hepatocytes." Functional Foods in Health and Disease 8, no. 3 (2018): 175. http://dx.doi.org/10.31989/ffhd.v8i3.423.

Full text

Abstract:

Background: Metformin is used to treat patients with type II diabetes. However, there are few scientific reports on its anti-inflammatory effects. In the inflamed liver, proinflammatory cytokines stimulate liver cells, followed by inducible nitric oxide synthase (iNOS) expression. Excessive NO levels produced by iNOS have been implicated as a factor in liver injury. As a result, it is essential to inhibit iNOS induction to prevent liver injury.Objective: This study aimed to investigate liver protective effects of metformin by examining interleukin (IL)-1β-stimulated hepatocytes. Methods: Primary cultured rat hepatocytes were treated with interleukin (IL)-1β in the presence or absence of metformin. iNOS induction and its signaling pathway were analyzed.Results: Metformin decreased iNOS protein and mRNA expression, resulting in the inhibition of hepatic NO production. Metformin also reduced tumor necrosis factor (TNF)-α and IL-6 mRNA expression. Metformin inhibited an essential signaling pathway for iNOS induction, type I IL-1 receptor upregulation. Transfection experiments revealed that metformin reduced iNOS mRNA levels through both promoter transactivation and mRNA stabilization. Delayed metformin administration after IL-1β addition also inhibited iNOS induction. Conclusions: Metformin affects the induction of inflammatory mediators including iNOS and TNF-α, demonstrating its therapeutic potential for organ injuries, including the liver.Keywords: metformin, inducible nitric oxide synthase, liver injury, primary cultured hepatocytes, type I interleukin-1 receptor, tumor necrosis factor-α

APA, Harvard, Vancouver, ISO, and other styles

Brennan, P. A., M. Palacios-Callender, T. Umar, et al. "Correlation between type II nitric oxide synthase and p53 expression in oral squamous cell carcinoma." British Journal of Oral and Maxillofacial Surgery 38, no. 6 (2000): 627–32. http://dx.doi.org/10.1054/bjom.2000.0540.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Mehta, Sanjay, Jacques Boudreau, Craig M. Lilly, and Jeffrey M. Drazen. "Endogenous pulmonary nitric oxide in the regulation of airway microvascular leak." American Journal of Physiology-Lung Cellular and Molecular Physiology 275, no. 5 (1998): L961—L968. http://dx.doi.org/10.1152/ajplung.1998.275.5.l961.

Full text

Abstract:

Endogenous nitric oxide (NO) is an important modulator of airway function, but its role in the regulation of airway microvascular leak (AMVL) remains unclear. Thus we assessed the effects of NO synthase (NOS) inhibition on expired NO (ENO) levels and on AMVL measured by the Evans blue dye technique in guinea pigs. In control unsensitized animals, systemic N G-nitro-l-arginine methyl ester (l-NAME) reduced ENO by 70 ± 8% ( P < 0.01) and reduced AMVL by 92 ± 1 and 44 ± 17% ( P < 0.05 for both) in the extrapulmonary and intrapulmonary airways, respectively. In animals sensitized and challenged with intratracheal antigen, markedly increased levels of AMVL and ENO were similarly attenuated byl-NAME. In contrast, aminoguanidine, a relatively selective type II NOS inhibitor, reduced ENO in both antigen-sensitized and control unsensitized animals by 39 ± 3% ( P < 0.01) but had no effect on AMVL. These data indicate that endogenous pulmonary NO contributes to both basal and antigen-stimulated levels of AMVL in guinea pigs and that this NO-dependent activity does not appear to be derived from type II NOS.

APA, Harvard, Vancouver, ISO, and other styles

Ding, M., and J. E. Merrill. "The kinetics and regulation of the induction of type II nitric oxide synthase and nitric oxide in human fetal glial cell cultures." Molecular Psychiatry 2, no. 2 (1997): 117–19. http://dx.doi.org/10.1038/sj.mp.4000222.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Punjabi, C. J., J. D. Laskin, K. J. Pendino, N. L. Goller, S. K. Durham, and D. L. Laskin. "Production of nitric oxide by rat type II pneumocytes: increased expression of inducible nitric oxide synthase following inhalation of a pulmonary irritant." American Journal of Respiratory Cell and Molecular Biology 11, no. 2 (1994): 165–72. http://dx.doi.org/10.1165/ajrcmb.11.2.7519435.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Yang, Guang, Yi Zhang, M. Elizabeth Ross, and Costantino Iadecola. "Attenuation of activity-induced increases in cerebellar blood flow in mice lacking neuronal nitric oxide synthase." American Journal of Physiology-Heart and Circulatory Physiology 285, no. 1 (2003): H298—H304. http://dx.doi.org/10.1152/ajpheart.00043.2003.

Full text

Abstract:

We used mice deficient in neuronal nitric oxide (NO) synthase (nNOS) to specifically investigate the role of neuronal NO in the increase of cerebellar blood flow (BFcrb) produced by neural activation. Crus II, a region of the cerebellar cortex that receives trigeminal sensory afferents, was activated by low-intensity stimulation of the upper lip (5–25 V, 4–16 Hz) in anesthetized mice. BFcrb was recorded in Crus II by using a laser-Doppler flow probe. In wild-type mice, upper lip stimulation increased BFcrb in the Crus II by 28 ± 3% (25 V, 10 Hz, n = 6). The rise in BFcrb was attenuated by 73 ± 3% in nNOS-/- mice ( P < 0.05, n = 6). The increases in BFcrb produced by superfusion of Crus II with glutamate or by systemic administration of harmaline were also attenuated in nNOS-/- mice ( P < 0.05). In contrast, the increases in BFcrb produced by topical superfusion of Crus II with acetylcholine or adenosine and the increase in BFcrb produced by hypercapnia were not affected ( P > 0.05). The field potentials evoked in the Crus II by upper lip stimulation did not differ between wild-type and nNOS-null mice. These data provide the first nonpharmacological evidence that nNOS-derived NO is a critical link between glutamatergic synaptic activity and blood flow in the activated cerebellum.

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!