scholarly journals Synthesis and characterization of a fluorinated S-nitrosothiol as the nitric oxide donor for fluoropolymer-based biomedical device applications

2018 ◽  
Vol 6 (38) ◽  
pp. 6142-6152 ◽  
Author(s):  
Yang Zhou ◽  
Qi Zhang ◽  
Jianfeng Wu ◽  
Chuanwu Xi ◽  
Mark E. Meyerhoff

The first nitric oxide (NO) releasing fluorinated polymer was developed via incorporating a new fluorinated NO donor into polyvinylidene fluoride tubing.

1997 ◽  
Vol 83 (4) ◽  
pp. 1326-1332 ◽  
Author(s):  
William J. Perkins ◽  
Young-Soo Han ◽  
Gary C. Sieck

Perkins, William J., Young-Soo Han, and Gary C. Sieck.Skeletal muscle force and actomyosin ATPase activity reduced by nitric oxide donor. J. Appl. Physiol.83(4): 1326–1332, 1997.—Nitric oxide (NO) may exert direct effects on actin-myosin cross-bridge cycling by modulating critical thiols on the myosin head. In the present study, the effects of the NO donor sodium nitroprusside (SNP; 100 μM to 10 mM) on mechanical properties and actomyosin adenosinetriphosphatase (ATPase) activity of single permeabilized muscle fibers from the rabbit psoas muscle were determined. The effects of N-ethylmaleimide (NEM; 5–250 μM), a thiol-specific alkylating reagent, on mechanical properties of single fibers were also evaluated. Both NEM (≥25 μM) and SNP (≥1 mM) significantly inhibited isometric force and actomyosin ATPase activity. The unloaded shortening velocity of SNP-treated single fibers was decreased, but to a lesser extent, suggesting that SNP effects on isometric force and actomyosin ATPase were largely due to decreased cross-bridge recruitment. The calcium sensitivity of SNP-treated single fibers was also decreased. The effects of SNP, but not NEM, on force and actomyosin ATPase activity were reversed by treatment with 10 mMdl-dithiothreitol, a thiol-reducing agent. We conclude that the NO donor SNP inhibits contractile function caused by reversible oxidation of contractile protein thiols.


2015 ◽  
Vol 12 (8) ◽  
pp. 1209-1223 ◽  
Author(s):  
Shefaat Ullah Shah ◽  
Nuno Martinho ◽  
Marie Socha ◽  
Catarina Pinto Reis ◽  
Stéphane Gibaud

2004 ◽  
Vol 378 (3) ◽  
pp. 785-791 ◽  
Author(s):  
Gabriella FIORE ◽  
Annarita POLI ◽  
Anna Di COSMO ◽  
Marco d'ISCHIA ◽  
Anna PALUMBO

The biosynthesis, localization and fate of catecholamines in the ink gland of the cuttlefish Sepia officinalis were investigated by combined biochemical and immunohistocytochemical methodologies. HPLC analysis of crude ink gland extracts indicated the presence of dopa (2.18±0.82 nmol/mg of protein) and DA (dopamine, 0.06±0.02 nmol/mg of protein), but no detectable noradrenaline or adrenaline. DA was shown to derive from l-tyrosine, according to experiments performed by incubating intact ink glands with [l-14C]tyrosine. The biosynthetic process involves a tyrosine hydroxylase and a dopa decarboxylase pathway and is independent of tyrosinase. The tyrosine hydroxylase activity was detected under conditions of tyrosinase suppression in the cytosolic fraction, but not in the melanosomal fraction, of ink gland extracts, and the presence of the enzyme was confirmed by Western-blot analysis. Dopa and DA were found to be released from the ink glands by processes controlled through the NMDA-nitric oxide-cGMP (where NMDA stands for N-methyl-d-aspartate) signalling pathway, as apparent from incubation experiments performed with [l-14C]tyrosine in the presence of NMDA, diethylamine NONOate (diethylamine diazeniumdiolate), a nitric oxide donor, 8-bromo-cGMP or a guanylyl cyclase inhibitor. Immunohistochemical results coupled with electron microscopy indicated that DA was concentrated in vesicles specifically localized in the mature melanin-producing cells of the ink gland proximal to the lumen and separated from the melanin-containing melanosomes. NMDA receptor stimulation or exposure to an NO donor caused a marked loss of DA immunoreactivity in mature cells, consistent with a release process. In the lumen of the ink gland, where mature exhausted cells pour their contents, DA immunoreactivity was found to be associated with the melanin granules, due apparently to physical adsorption. Overall, these results point to DA as a marker of cell maturation in Sepia ink gland subject to release by the NO/cGMP signalling pathway, and disclose apparently overlooked DA–melanin interactions in secreted ink of possible relevance to the defence mechanism.


2013 ◽  
Vol 179 (2) ◽  
pp. 202
Author(s):  
E.S. Moreira ◽  
T. Moyer ◽  
H. Kassam ◽  
S.I. Stupp ◽  
M.R. Kibbe

2002 ◽  
Vol 124 (41) ◽  
pp. 12182-12191 ◽  
Author(s):  
Pawel G. Parzuchowski ◽  
Megan C. Frost ◽  
Mark E. Meyerhoff

2001 ◽  
Vol 18 (6) ◽  
pp. 849-856 ◽  
Author(s):  
WILLIAM H. BALDRIDGE ◽  
ANDY J. FISCHER

Nitric oxide (NO) activates soluble guanylyl cyclase (sGC) and the resulting increase in cyclic guanosine monophosphate (cGMP) is an important intracellular signalling pathway in the vertebrate retina. Immunocytochemical detection of cGMP following exposure to NO donors has proven an effective method of identifying cells that express sGC. While such an approach has proven useful for the study of several vertebrate retinas, it has not been applied to the well-characterized teleost retina. Therefore, in the present study, we have applied this approach to the retina of the goldfish (Carassius auratus). In the presence of the phosphodiesterase (PDE) inhibitor 3-isobutyl-1-methylxanthine (IBMX), incubation of goldfish eyecups in Ringer's solution containing (±)-S-nitroso-N-acetylpenicillamine (SNAP) increased cGMP-like immunoreactivity (cG-ir) in bipolar, horizontal, amacrine, and ganglion cells and in ganglion cell axons and optic nerve. Weak labeling was observed in horizontal cells but no change in cG-ir was noted within photoreceptors. The NO donor-stimulated increases of cG-ir in horizontal, bipolar, amacrine, and ganglion cells are consistent with known physiological effects of NO on these neurons. The physiological significance of NO action at the level of optic nerve is not known. The lack of an effect of SNAP on cG-ir in photoreceptors was unexpected, as there are known physiological actions of NO, mediated by cGMP, on these neurons. Although this may be due to insufficient sensitivity of immunolabeling, this result may indicate a difference between isoforms of sGC or cGMP PDE in these neurons, compared to neurons where exogenous NO increased cG-ir.


2003 ◽  
Vol 44 (4) ◽  
pp. 395-402
Author(s):  
J. Harnek ◽  
E. Zoucas ◽  
R. Sjuve ◽  
A. Arner ◽  
E. Ekblad ◽  
...  

Purpose: To investigate the development of intimal hyperplasia in response to percutaneous transluminal coronary angioplasty (PTCA) followed by local delivery of the nitric oxide (NO) donor 3-morpholino-sydnonimine (SIN-1). Material and Methods: Overdilation PTCA was performed in coronary arteries in 20 healthy pigs. One of the dilated segments was additionally treated with local delivery of SIN-1 for 10 min. Segments distal to the treated part of the arteries served as controls. Arteries were radiographically depicted and analyzed after 1 and 8 weeks for actin, myosin and intermediate filaments (IF), nitric oxide synthetase (NOS) and histological evaluation. Results: Segments treated with PTCA+SIN-1 showed a significantly ( p = 0.03) larger luminal diameter compared with PTCA only treated segments. The luminal loss after SIN-1 was not significant compared with the diameter prior to treatment. Endothelial NOS content was significantly lower in the PTCA+SIN-1 group compared with the PTCA group after 1 ( p = 0.03) and 8 weeks ( p = 0.013). IF/actin ratio after 1 week was significantly increased in PTCA-treated segments compared with untreated controls ( p = 0.004), and compared with PTCA+SIN-1-treated segments ( p = 0.004). Conclusion: PTCA-induced intimal hyperplasia was potently inhibited by local delivery of the NO donor SIN-1. Momentary events at the time of injury play a significant role in the development of intimal hyperplasia and long-lasting down-regulation of the endothelial NOS expression after SIN-1 exposure is suggested. The IF/actin ratio can be useful as an early marker of intimal hyperplasia.


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