Nanosized copper(ii) oxide/silica for catalytic generation of nitric oxide from S-nitrosothiols

2020 ◽  
Vol 8 (19) ◽  
pp. 4267-4277 ◽  
Author(s):  
Kostiantyn Kulyk ◽  
Liana Azizova ◽  
James M. Cunningham ◽  
Lyuba Mikhalovska ◽  
Mykola Borysenko ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Silica Nanoparticles ◽  
Biomedical Materials ◽  
Physiological Conditions

The findings of this study suggest that copper(ii) oxide–silica nanoparticles produce NO from the GSNO species at physiological conditions in situ and could be used for designing biomedical materials with NO generating activity.

Nitroxide-Mediated Polymerization of Styrene Initiated from the Surface of Silica Nanoparticles. In Situ Generation and Grafting of Alkoxyamine Initiators

2005 ◽  
Vol 38 (4) ◽  
pp. 1099-1106 ◽  
Author(s):  
C. Bartholome ◽  
E. Beyou ◽  
E. Bourgeat-Lami ◽  
P. Chaumont ◽  
F. Lefebvre ◽  
...  
Keyword(s):  
Silica Nanoparticles ◽  
In Situ Generation ◽  
Nitroxide Mediated Polymerization

Enzyme-functionalized vascular grafts catalyze in-situ release of nitric oxide from exogenous NO prodrug

2015 ◽  
Vol 210 ◽  
pp. 179-188 ◽  
Author(s):  
Zhihong Wang ◽  
Yaxin Lu ◽  
Kang Qin ◽  
Yifan Wu ◽  
Yingping Tian ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Vascular Grafts

scholarly journals Development of A Flexible Cell Targeting System Based on Silica Nanoparticles

1998 ◽  
Vol 530 ◽  
Author(s):  
T. Schiimstel ◽  
H. Schirra ◽  
J. Gerwann ◽  
C. Lesniak ◽  
A. Kalaghi-Nafchi ◽  
...  
Keyword(s):  
Silica Nanoparticles ◽  
Electrostatic Interactions ◽  
Particle Concentration ◽  
Biological Function ◽  
Particle Surface ◽  
Cell Types ◽  
Silica Particles ◽  
Hydrodynamic Diameter ◽  
Reaction Conditions ◽  
Physiological Conditions

AbstractCommercially available and synthesized silica particles were fluorescently labeled with FITC and modified to get a wide variety of particle systems with defined size and surface charge. By a variation of reaction conditions particles with diameters of 10 and 80 nm determined with TEM and with zetapotentials between -50 to +30 mV under physiological conditions (pH: 7.4, PBS-buffer) were available.A further molecular shell consisiting of avidin was obtained by binding the molecules to negatively charged particle surfaces through electrostatic interactions. The amount of avidin coupled to the silica particles was 1.7 μg per mg particle. Starting with particles with an hydrodynamic diameter determined with PCS of 260 nm, the size increased to 500 nm, while the zeta potential was altered to -8 mV under physiological conditions.Biotinylated wheat germ agglutinin (bio-WGA) can be bonded to such particles through avidin / biotin complex formation. Up to 2.8 μg lectin per mg particles could be coupled to the particle surface. This leads to a further increase of hydrodynamic diameter to 650 nm. It could be shown by hemagglutination test, that the bonded lectin is still active. No toxic effects of the silica particles were found at 1 wt.-% particle concentration with various cell types (Caco-2, L132). The binding of lectin-particle complexes to cells was increased by a factor of 4.4 in comparison to uncoated particles.In addition it was found that WGA can directly be coupled to the particle surface. An amount of 1.8 μg Lectin per mg particle was determined. The hydrodynamic diameter increases from 260 nm to 432 rm, while a zetapotential of-28 mV was found under physiological conditions.It could be shown, that negatively charged silica nanoparticles are suitable systems to couple various biomolecules retaining their biological function.

scholarly journals Differential mechanisms of inhibition of glyceraldehyde-3-phosphate dehydrogenase by S-nitrosothiols and NO in cellular and cell-free conditions

2010 ◽  
Vol 299 (4) ◽  
pp. H1212-H1219 ◽  
Author(s):  
Katarzyna A. Broniowska ◽  
Neil Hogg
Keyword(s):  
Nitric Oxide ◽  
Signaling Mechanism ◽  
Aortic Endothelial Cells ◽  
Signaling Specificity ◽  
Physiological Conditions ◽  
Irreversible Inhibition ◽  
Bovine Aortic Endothelial Cells ◽  
Mechanism Of Inhibition ◽  
Dependent Inhibition ◽  
Inhibition Pattern

S-nitrosothiols are nitric oxide (NO)-derived molecules found in biological systems. They have been variously discussed as both NO reservoirs and as major actors in NO-dependent, but cGMP-independent, signal transduction. Although S-nitrosation of specific cysteine residues has been suggested to represent a novel redox-based signaling mechanism, the exact mechanisms of S-nitrosothiol formation under (patho)physiological conditions and the determinants of signaling specificity have not yet been established. Here we examined the sensitivity of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to inhibition by S-nitrosocysteine (CysNO) and NO both intracellularly and in isolation. Bovine aortic endothelial cells (BAECs) and purified GAPDH preparations were treated with CysNO or NO, and enzymatic activity was monitored. Intracellular GAPDH was irreversibly inhibited upon CysNO administration, whereas treatment with NO resulted in a DTT-reversible inhibition of the enzyme. Purified GAPDH was inhibited by both CysNO and NO, but the inhibition pattern was diametrically opposite to that observed in the cells; CysNO-dependent inhibition was reversed with DTT, whereas NO-dependent inhibition was not. In the presence of GSH, NO inhibited purified GAPDH in a DTT-reversible way. Our data suggest that in response to CysNO treatment, cellular GAPDH undergoes S-nitrosation, which results in an irreversible inhibition of the enzyme under turnover conditions. In contrast, NO inhibits the enzyme via oxidative mechanisms that do not involve S-nitrosation and are reversible. In summary, our data show that GAPDH is a target for CysNO- and NO-dependent inhibition; however, these two agents inhibit the enzyme via different mechanisms both inside the cell and in isolation. Additionally, the differences observed between the cellular system and purified protein strongly imply that the intracellular environment dictates the mechanism of inhibition.

Cellular Localization of Inducible Nitric Oxide Synthase in Experimental Endotoxic Shock in the Rat

1994 ◽  
Vol 87 (2) ◽  
pp. 179-186 ◽  
Author(s):  
H. Terence Cook ◽  
Alison J. Bune ◽  
Albertine S. Jansen ◽  
G. Michael Taylor ◽  
Rashpal K. Loi ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
In Situ Hybridization ◽  
Cellular Localization ◽  
Endotoxic Shock ◽  
No Synthase ◽  
Similar Distribution ◽  
Mouse Macrophage ◽  
Inducible No Synthase ◽  
Monocytes And Macrophages

1. Endotoxin induces a shock-like syndrome with increased nitric oxide synthesis. To clarify the cellular source of NO in endotoxic shock we used immunohistochemistry and in situ hybridization to localize inducible NO synthase in rats given lipopolysaccharide or Corynebacterium parvum and lipopolysaccharide. Immunohistochemistry was carried out with an antibody raised against a synthetic peptide of mouse macrophage NO synthase. In situ hybridization was performed with 35S-labelled oligonucleotide probes corresponding to cDNA sequences common to mouse macrophage inducible NO synthase and rat vascular smooth inducible NO synthase. Monocytes and macrophages were identified by immunohistochemistry with the mouse monoclonal antibody ED1. 2. After lipopolysaccharide alone, the major site of NO synthase induction was monocytes and macrophages in multiple organs, principally liver and spleen. Bronchial, bile duct, intestinal and bladder epithelium and some hepatocytes also expressed inducible NO synthase. Expression peaked at 5 h and had returned to normal by 12 h except in spleen. 3. After priming with C. parvum, lipopolysaccharide led to a similar distribution of inducible NO synthase as lipopolysaccharide alone, but in addition there was more prominent hepatocyte staining, staining in macrophage granulomas in the liver and inducible NO synthase was present in some endothelial cells in the aorta. 4. These findings provide a direct demonstration of the cellular localization of inducible NO synthase after lipopolysaccharide.

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