Functional Layer-by-Layer Thin Films of Inducible Nitric Oxide (NO) Synthase Oxygenase and Polyethylenimine: Modulation of Enzyme Loading and NO-Release Activity

2018 ◽  
Vol 10 (9) ◽  
pp. 7745-7755 ◽  
Author(s):  
Bhagya Gunasekera ◽  
Charbel Abou Diwan ◽  
Ghaith Altawallbeh ◽  
Haitham Kalil ◽  
Shaimaa Maher ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Thin Films ◽  
No Synthase ◽  
Layer By Layer ◽  
Enzyme Loading ◽  
Functional Layer ◽  
No Release ◽  
Inducible Nitric Oxide

INTERLEUKIN I (IL-1) AND ENDOTOXIN DEPRESS β-ADRENERGIC RESPONSE IN CARDIOMYOCYTES AND STIMULATE THE INDUCIBLE NITRIC OXIDE (NO) SYNTHASE (iNOS) AND NO RELEASE

Shock ◽  
1997 ◽  
Vol 7 (Supplement) ◽  
pp. 91
Author(s):  
U. Müller-Werdan ◽  
H. Schumann ◽  
H. Loppnow ◽  
F. Schlegel ◽  
S. Koch ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
No Synthase ◽  
Adrenergic Response ◽  
No Release ◽  
Inducible Nitric Oxide

Decrease in ambient [Cl-] stimulates nitric oxide release from cultured rat mesangial cells

1994 ◽  
Vol 267 (1) ◽  
pp. F190-F195 ◽  
Author(s):  
H. Tsukahara ◽  
Y. Krivenko ◽  
L. C. Moore ◽  
M. S. Goligorsky
Keyword(s):  
Nitric Oxide ◽  
Mesangial Cells ◽  
Ionic Composition ◽  
Juxtaglomerular Apparatus ◽  
Cytosolic Calcium ◽  
No Synthase ◽  
Tubuloglomerular Feedback ◽  
No Production ◽  
Rapid Reduction ◽  
No Release

It has been hypothesized that fluctuations of the ionic composition in the interstitium of juxtaglomerular apparatus (JGA) modulate the function of extraglomerular mesangial cells (MC), thereby participating in tubuloglomerular feedback (TGF) signal transmission. We examined the effects of isosmotic reductions in ambient sodium concentration ([Na+]) and [Cl-] on cytosolic calcium concentration ([Ca2+]i) in cultured rat MC. Rapid reduction of [Na+] or [Cl-] in the bath induced a concentration-dependent rise in [Ca2+]i. MC are much more sensitive to decreases in ambient [Cl-] than to [Na+]; a decrease in [Cl-] as small as 14 mM was sufficient to elicit a detectable [Ca2]i response. These observations suggest that MC can be readily stimulated by modest perturbations of extracellular [Cl-]. Next, we examined whether activation of MC by lowered ambient [Cl-] influences cellular nitric oxide (NO) production. Using an amperometric NO sensor, we found that a 13 mM decrease in ambient [Cl-] caused a rapid, Ca2+/calmodulin-dependent rise in NO release from MC. This response was not inhibitable by dexamethasone, indicating the involvement of the constitutive rather than the inducible type of NO synthase in MC. In addition, the NO release was blunted by indomethacin pretreatment, suggesting that a metabolite(s) of cyclooxygenase regulates the activation of NO synthase in MC. Our findings that small perturbations in external [Cl-] stimulate MC to release NO, a highly diffusible and rapidly acting vasodilator, provide a possible mechanism to explain the transmission of the signal for the TGF response within the JGA.

scholarly journals Intracoronary Des-Acyl Ghrelin Acutely Increases Cardiac Perfusion Through a Nitric Oxide-Related Mechanism in Female Anesthetized Pigs

Endocrinology ◽  
2016 ◽  
Vol 157 (6) ◽  
pp. 2403-2415 ◽  
Author(s):  
Elena Grossini ◽  
Giulia Raina ◽  
Serena Farruggio ◽  
Lara Camillo ◽  
Claudio Molinari ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Blood Pressure ◽  
Endothelial Cells ◽  
Blood Flow ◽  
Coronary Artery ◽  
Coronary Blood Flow ◽  
No Synthase ◽  
Cardiac Perfusion ◽  
No Release ◽  
Acyl Ghrelin

Des-acyl ghrelin (DAG), the most abundant form of ghrelin in humans, has been found to reduce arterial blood pressure and prevent cardiac and endothelial cell apoptosis. Despite this, data regarding its direct effect on cardiac function and coronary blood flow, as well as the related involvement of autonomic nervous system and nitric oxide (NO), are scarce. We therefore examined these issues using both in vivo and in vitro studies. In 20 anesthetized pigs, intracoronary 100 pmol/mL DAG infusion with a constant heart rate and aortic blood pressure, increased coronary blood flow and NO release, whereas reducing coronary vascular resistances (P < .05). Dose responses to DAG were evaluated in five pigs. No effects on cardiac contractility/relaxation or myocardial oxygen consumption were observed. Moreover, whereas the blockade of muscarinic cholinoceptors (n = 5) or α- and β-adrenoceptors (n = 5 each) did not abolish the observed responses, NO synthase inhibition (n = 5) prevented the effects of DAG on coronary blood flow and NO release. In coronary artery endothelial cells, DAG dose dependently increased NO release through cAMP signaling and ERK1/2, Akt, and p38 MAPK involvement as well as the phosphorylation of endothelial NO synthase. In conclusion, in anesthetized pigs, DAG primarily increased cardiac perfusion through the involvement of NO release. Moreover, the phosphorylation of ERK1/2 and Akt appears to play roles in eliciting the observed NO production in coronary artery endothelial cells.

Nitric oxide induces apoptosis in megakaryocytic cell lines

Blood ◽  
2000 ◽  
Vol 95 (11) ◽  
pp. 3451-3459 ◽  
Author(s):  
Elisabeth Battinelli ◽  
Joseph Loscalzo
Keyword(s):  
Nitric Oxide ◽  
Cell Lines ◽  
Bone Marrow Cells ◽  
No Synthase ◽  
Cell Systems ◽  
Normal Human ◽  
Induced Apoptosis ◽  
Normal Human Bone Marrow ◽  
Megakaryocytic Cell ◽  
Inducible Nitric Oxide

Cytokines that stimulate inducible nitric oxide (NO) synthase can suppress the growth and differentiation of normal human bone marrow cells, including megakaryocytes. Since NO promotes apoptosis in other cell systems, we chose to study the determinants of apoptosis in megakaryocytic cells. We show that both exogenous and endogenous sources of NO can induce apoptosis in megakaryocytoid cell lines. The megakaryocyte growth factor thrombopoietin suppresses NO-induced apoptosis, whereas treatment with peroxynitrite, a cytotoxic product formed when NO reacts with superoxide, promotes apoptosis. Superoxide inhibitors suppress NO-induced apoptosis, and pretreatment with megakaryocyte growth and maturation factors attenuates NO-induced apoptosis. These data show that NO modulates megakaryocyte apoptosis and suggest that this process may occur in the cytokine-rich marrow milieu to regulate megakaryocyte turnover.

Profound biopterin oxidation and protein tyrosine nitration in tissues of ApoE-null mice on an atherogenic diet: contribution of inducible nitric oxide synthase

2007 ◽  
Vol 293 (5) ◽  
pp. H2878-H2887 ◽  
Author(s):  
Rita K. Upmacis ◽  
Mark J. Crabtree ◽  
Ruba S. Deeb ◽  
Hao Shen ◽  
Paul B. Lane ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Atherogenic Diet ◽  
No Synthase ◽  
Chow Diet ◽  
Tyrosine Nitration ◽  
Elevated Protein ◽  
Oxide Synthase ◽  
Lung And Kidney ◽  
Specific Contribution ◽  
Inducible Nitric Oxide

Diminished nitric oxide (NO) bioactivity and enhanced peroxynitrite formation have been implicated as major contributors to atherosclerotic vascular dysfunctions. Hallmark reactions of peroxynitrite include the accumulation of 3-nitrotyrosine (3-NT) in proteins and oxidation of the NO synthase (NOS) cofactor, tetrahydrobiopterin (BH4). The present study sought to 1) quantify the extent to which 3-NT accumulates and BH4 becomes oxidized in organs of apolipoprotein E-deficient (ApoE−/−) atherosclerotic mice and 2) determine the specific contribution of inducible NOS (iNOS) to these processes. Whereas protein 3-NT and oxidized BH4 were undetected or near the detection limit in heart, lung, and kidney of 3-wk-old ApoE−/− mice or ApoE−/− mice fed a regular chow diet for 24 wk, robust accumulation was evident after 24 wk on a Western (atherogenic) diet. Since 3-NT accumulation was diminished 3- to 20-fold in heart, lung, and liver in ApoE−/− mice missing iNOS, iNOS-derived species are involved in this reaction. In contrast, iNOS-derived species did not contribute to elevated protein 3-NT formation in kidney or brain. iNOS deletion also afforded marked protection against BH4 oxidation in heart, lung, and kidney of atherogenic ApoE−/− mice but not in brain or liver. These findings demonstrate that iNOS-derived species are increased during atherogenesis in ApoE−/− mice and that these species differentially contribute to protein 3-NT accumulation and BH4 oxidation in a tissue-selective manner. Since BH4 oxidation can switch the predominant NOS product from NO to superoxide, we predict that progressive NOS uncoupling is likely to drive atherogenic vascular dysfunctions.

Nitric oxide-mediated arteriolar dilation after endothelial deformation

2001 ◽  
Vol 280 (2) ◽  
pp. H714-H721 ◽  
Author(s):  
Dong Sun ◽  
An Huang ◽  
Fabio A. Recchia ◽  
Yanning Cui ◽  
Edward J. Messina ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Vessel Diameter ◽  
No Synthase ◽  
Intraluminal Pressure ◽  
Silicone Membrane ◽  
Rat Mesentery ◽  
Original Length ◽  
No Release ◽  
Per Se ◽  
Diameter Reduction

Previously, we frequently observed dilation of arterioles after agonist-induced constrictions. We hypothesized that deformation of the endothelium during decreases in diameter of isolated arterioles elicits the release of nitric oxide (NO). In isolated arterioles of rat mesentery, phenylephrine (PE, 10−7 M)-, U-46619 (10−7 M)-, and KCl (50 mM)-induced constrictions were followed by potent dilations. Inhibition of NO synthase with N ω-nitro-l-arginine (l-NNA, 2 × 10−4 M) or removal of the endothelium significantly enhanced constriction and reduced the postconstriction dilation. In the presence of 80 mmHg of intraluminal pressure, an increase in extraluminal pressure (Pe) to 75 mmHg for 20 s and 1 and 2 min decreased vessel diameter. After release of Pe, arterioles dilated as a function of the duration of diameter reduction by Pe. Removal of the endothelium or administration of l-NNA significantly diminished the post-Pe dilations. In cultured mesenteric arteriolar endothelial cells (EC), PE, U-46619, or KCl did not increase, whereas ACh did increase, the production of NO, as measured by a fluorometric assay for nitrite. Furthermore, when EC, cultured on a stretched silicone membrane, were subjected to deformation by shortening the membrane to 50% of its original length, NO release increased significantly. Based on all of the above, we propose that deformation of EC per se elicits release of NO, a mechanism that modulates arteriolar constriction.

scholarly journals Adrenomedullin Stimulates Nitric Oxide Release from SK-N-SH Human Neuroblastoma Cells by Modulating Intracellular Calcium Mobilization

Endocrinology ◽  
2005 ◽  
Vol 146 (5) ◽  
pp. 2295-2305 ◽  
Author(s):  
Yong Xu ◽  
Teresa L. Krukoff
Keyword(s):  
Nitric Oxide ◽  
Protein Kinase ◽  
Intracellular Calcium ◽  
Protein Kinase A ◽  
Neuroblastoma Cells ◽  
No Synthase ◽  
Human Neuroblastoma Cells ◽  
Human Neuroblastoma ◽  
No Release ◽  
Kinase A

Abstract We used SK-N-SH human neuroblastoma cells to test the hypothesis that adrenomedullin (ADM), a multifunctional neuropeptide, stimulates nitric oxide (NO) release by modulating intracellular free calcium concentration ([Ca2+]i) in neuron-like cells. We used a nitrite assay to demonstrate that ADM (10 pm to 100 nm) stimulated NO release from the cells, with a maximal response observed with 1 nm at 30 min. This response was blocked by 1 nm ADM22–52, an ADM receptor antagonist or 2 μm vinyl-l-NIO, a neuronal NO synthase inhibitor. In addition, 5 μm 1,2-bis(2-aminophenoxy)ethane-N,N,N′,N′-tetraacetic acid acetoxymethyl ester, an intracellular calcium chelator, eliminated the ADM-induced NO release. Similar results were observed when the cells were incubated in calcium-free medium or when l-type calcium channels were inhibited with 5 μm nifedipine or 10 μm nitrendipine. Depletion of calcium stores in the endoplasmic reticulum (ER) with 1 μm cyclopiazonic acid or 150 nm thapsigargin, or inhibition of ryanodine-sensitive receptors in the ER with 10 μm ryanodine attenuated the ADM-induced NO release. NO responses to ADM were mimicked by 1 mm dibutyryl cAMP, a cAMP analog, and were abrogated by 5 μm H-89, a protein kinase A inhibitor. Furthermore, Fluo-4 fluorescence-activated cell sorter analysis showed that ADM (1 nm) significantly increased [Ca2+]i at 30 min. This response was blocked by nifedipine (5 μm) or H-89 (5 μm) and was reduced by ryanodine (10 μm). These results suggest that ADM stimulates calcium influx through l-type calcium channels and ryanodine-sensitive calcium release from the ER, probably via cAMP-protein kinase A-dependent mechanisms. These elevations in [Ca2+]i cause activation of neuronal NO synthase and NO release.

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