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Journal articles on the topic 'Nitroso-glutathione'

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Published: 10 December 2022

Last updated: 28 January 2023

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1

Buca, Beatrice Rozalina, Liliana Mititelu Tartau, Ciprian Rezus, Cristiana Filip, Alin Constantin Pinzariu, Elena Rezus, Gratiela Eliza Popa, et al. "The Effects of Two Nitric Oxide Donors in Acute Inflammation in Rats Experimental data." Revista de Chimie 69, no. 10 (November 15, 2018): 2899–903. http://dx.doi.org/10.37358/rc.18.10.6649.

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We aimed to investigate the effects of two nitric oxide donors in acute inflammation in rats. The experiment was carried out on white Wistar rats, randomly distributed in 4 groups of 5 animals each; the substances were administered intraperitoneally as follows: Group 1 (SS): saline solution 0.1mL/100 g body weight (control); Group 2 (IND): indometacin 150 mg/kg body weight; Group 3 (NEB): nebivolol 1 mg/kg body weight; Group 4 (GSNO): S-nitroso-glutathione 1 mg/kg body weight. An experimental model of acute hind paw inflammation with carrageenan was used for the researches. The influence of the nitric oxide donors on blood parameters, specific inflammatory and immune markers was evaluated 24 h, respectively 72 hours after the injection of irritant agent. The experimental protocol was implemented according to the recommendations of our University Committee for Research and Ethical Issues. The administration of nitric oxide donors nebivolol and S-nitroso-glutathione was accompanied by a substantial diminution of paw edema, as well as by an important decrease in the percent of lymphocytes, a reduction of interleukin 6 and tumor necrosis factor alpha values. The effects of nebivolol were more accentuated than of S-nitroso-glutathione, but less intense than of indomethacin in the experiment. The treatment with nebivolol and S-nitroso-glutathione produced anti-inflammatory effects on local acute inflammation in the carrageenan-induced paw edema test in rats.

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2

Buca, Beatrice Rozalina, Liliana Mititelu-Tartau, Cristiana Filip, Nina Filip, Ciprian Rezus, Cristina Iancu, Elena Rezus, et al. "The Influence of Nitric Oxid Donors Nebivolol and S-Nitrosoglutathion of the Oxidatives Stress and Liver Function in Rats." Revista de Chimie 70, no. 4 (May 15, 2019): 1360–63. http://dx.doi.org/10.37358/rc.19.4.7127.

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We aimed to investigate the influence of two nitric oxide donors on the oxidative stress and the liver function in rats with experimental-induced acute paw inflammation.The experiment was carried out on white male Wistar rats (200-250 g), randomly assigned into 4 groups of 5 animals each, which received the substances intraperitoneal, as follows: group 1 (Control) saline solution 0.1 ml/100 g body weight; group 2 (IND) indomethacin 150 mg/kg body weight (kbw); groups 3 (NEB) and 4 (GSNO) nebivolol 1 mg/kbw, respectively S-nitroso-glutathione 1 mg/kbw. Carrageenan-induced rat�s paw edema test was used for the generation of acute inflammation. The activity of liver enzymes and of some antioxidant parameters was evaluated before the carrageenan injection, after 24 hours and 3 days. The experimental protocol was approved by the University�s Ethic Committee on Research and Ethical Issues.The administration of indomethacin, nebivolol and S-nitroso-glutathione appears to decrease the oxidative stress after 24 h in rats with experimental-induced acute paw inflammation. The nitric oxide donors nebivolol and S-nitroso-glutathione produced moderate functional and structural liver disturbances in rats with acute inflammation.

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3

Tsikas, Dimitrios, Jörg Sandmann, Stefan Rossa, Frank-Mathias Gutzki, and Jürgen C. Frölich. "Gas Chromatographic–Mass Spectrometric Detection of S-Nitroso-cysteine and S-Nitroso-glutathione." Analytical Biochemistry 272, no. 2 (August 1999): 117–22. http://dx.doi.org/10.1006/abio.1999.4177.

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4

Wei, Wei, Raynard Bateman, Daniel Rauh, Bin Li, Kevan M. Shokat, and Limin Liu. "P0119. Pharmacological inhibitors of S-nitroso-glutathione reductase." Nitric Oxide 14, no. 4 (June 2006): 55–56. http://dx.doi.org/10.1016/j.niox.2006.04.185.

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5

Clark, Alan G., and Phillip Debnam. "Inhibition of glutathione S-transferases from rat liver by S-nitroso-L-glutathione." Biochemical Pharmacology 37, no. 16 (August 1988): 3199–201. http://dx.doi.org/10.1016/0006-2952(88)90321-8.

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6

Stomberski, Colin T., Puneet Anand, Nicholas M. Venetos, Alfred Hausladen, Hua-Lin Zhou, Richard T. Premont, and Jonathan S. Stamler. "AKR1A1 is a novel mammalian S-nitroso-glutathione reductase." Journal of Biological Chemistry 294, no. 48 (October 23, 2019): 18285–93. http://dx.doi.org/10.1074/jbc.ra119.011067.

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7

Kazanis, Sophia, and Robert A. McClelland. "Electrophilic intermediate in the reaction of glutathione and nitroso arenes." Journal of the American Chemical Society 114, no. 8 (April 1992): 3052–59. http://dx.doi.org/10.1021/ja00034a043.

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8

Choudhry, Shweta, Limin Liu, and Esteban G. Burchard. "P145. Genetic association of S-nitroso-glutathione reductase with asthma." Nitric Oxide 14, no. 4 (June 2006): 64–65. http://dx.doi.org/10.1016/j.niox.2006.04.212.

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9

Radomski, Marek W., Daryl D. Rees, Alberto Dutra, and Salvador Moncada. "S-nitroso-glutathione inhibits platelet activation in vitro and in vivo." British Journal of Pharmacology 107, no. 3 (November 1992): 745–49. http://dx.doi.org/10.1111/j.1476-5381.1992.tb14517.x.

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10

Ji, Yanbin, Theodorus P. M. Akerboom, Helmut Sies, and James A. Thomas. "S-Nitrosylation and S-Glutathiolation of Protein Sulfhydryls byS-Nitroso Glutathione." Archives of Biochemistry and Biophysics 362, no. 1 (February 1999): 67–78. http://dx.doi.org/10.1006/abbi.1998.1013.

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11

Kashiba-Iwatsuki, Misato, Makiko Yamaguchi, and Masayasu Inoue. "Role of ascorbic acid in the metabolism of S -nitroso-glutathione." FEBS Letters 389, no. 2 (July 1, 1996): 149–52. http://dx.doi.org/10.1016/0014-5793(96)00560-1.

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12

Guillemard, E., M. Geniteau-Legendre, R. Kergot, G. Lemaire, J. F. Petit, C. Labarre, and A. M. Quero. "Activity of nitric oxide-generating compounds against encephalomyocarditis virus." Antimicrobial Agents and Chemotherapy 40, no. 4 (April 1996): 1057–59. http://dx.doi.org/10.1128/aac.40.4.1057.

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Nitric oxide (NO) generated by two NO donors (sodium nitroprusside or S-nitroso-L-glutathione) was shown to exert a dose-dependent inhibition of encephalomyocarditis virus growth in L-929 cells. This activity was not due to the cytotoxic or direct virucidal effects of NO donors. L-929 cells were shown to produce NO endogenously, but this low level of production did not counter encephalomyocarditis virus replication.

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13

Ramsay, B., M. Radomski, A. Belder, JF Martin, and P. Lopez-Jaramillo. "Systemic effects of S-nitroso-glutathione in the human following intravenous infusion." British Journal of Clinical Pharmacology 40, no. 1 (July 1995): 101–2. http://dx.doi.org/10.1111/j.1365-2125.1995.tb04545.x.

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14

Zeng, Hong, Netanya Y. Spencer, and Neil Hogg. "Metabolism of S-nitrosoglutathione by endothelial cells." American Journal of Physiology-Heart and Circulatory Physiology 281, no. 1 (July 1, 2001): H432—H439. http://dx.doi.org/10.1152/ajpheart.2001.281.1.h432.

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S-nitrosoglutathione (GSNO) is an inhibitor of platelet aggregation and has also been shown to protect the ischemic heart from reperfusion-mediated injury. Although GSNO is often used in cell culture as a source of nitric oxide, the mechanisms of GSNO metabolism are not well established. We show here that GSNO decomposition by bovine aortic endothelial cells has an absolute dependence on the presence of cystine in the cell culture medium. In addition, GSNO decay is inhibited by diethyl maleate, an intracellular glutathione scavenger, but not by buthionine sulfoximine, a glutathione synthesis inhibitor. This indicates that thiols in general, rather than specifically glutathione, are the major factors that influence GSNO decay. Only 40% of the nitroso group of GSNO could be recovered as nitrite/nitrate, suggesting that the primary route of GSNO decay is reductive and that nitric oxide is only a minor product of GSNO decay. We conclude that the intracellular thiol pool causes the reduction of extracellular disulfides to thiols, which then directly reduce GSNO.

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15

Kuo, Eva YuHua, Yi-Lin Chien, Wen-Chyi Dai, Michael Jian-Hao Huang, and Tse-Min Lee. "The Acclimation Mechanisms of Chlamydomonas reinhardtii against Nitrosative Stress: A Role of NADPH Oxidase (RBOL2) in the Regulation of Nitric Oxide-Mediated ER Stress and Glutathione Redox State." Biology and Life Sciences Forum 4, no. 1 (November 30, 2020): 33. http://dx.doi.org/10.3390/iecps2020-08609.

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Nitric oxide (NO) is a signal in the modulation of acclamatory responses to stress in plants. Here, the metabolic shift of Chlamydomonas reinhardtii to sub-lethal NO stress was approached by exposure to 0.1 mM S-nitroso-N-acetylpenicillamine (SNAP), a NO donor, in the presence or the absence of the NO scavenger, 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-l-oxyl-3-oxide (cPTIO). NO did not cause growth impairment but induced a decrease in glutathione (GSH) levels and redox state. NO upregulated the expression of glutathione-associated genes, glutathione synthetase (GSH1), and glutathione reductase (GSHR1) genes while it decreased that of the proteins associated with ER stress-induced unfolded protein response (UPR). Furthermore, the expression of NADPH oxidase isoform, respiratory burst oxygenase-like 2 (RBOL2), instead of RBOL1 increased under NO stress. NO-induced upregulation of GSH1 and GSHR1 upregulation and the downregulation of most UPR genes were not found in rbol2 mutant. The presence of cPTIO suppressed the NO-induced changes in GSH availability, UPR, and RBOL expression. Overall, NADPH oxidase (RBOL2)-dependent and -independent signaling pathways involve in the inhibition of UPR and the enhancement of GSH availability by NO.

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16

Stotz, William, Lou Ann S. Brown, and Lucky Jain. "Elevated Temperature Enhances Release of Nitric Oxide from S-Nitroso-glutathione (GSNO) 351." Pediatric Research 43 (April 1998): 62. http://dx.doi.org/10.1203/00006450-199804001-00372.

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17

Stiborová, Marie, Eva Frei, and Heinz H. Schmeiser. "Study on N-Demethylation of N,N-Dimethyl-4-aminoazobenzene and N-Nitrosamines by Prostaglandin H Synthase." Collection of Czechoslovak Chemical Communications 62, no. 6 (1997): 971–80. http://dx.doi.org/10.1135/cccc19970971.

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The in vitro enzymatic metabolism of carcinogenic N,N-dimethyl-4-aminoazobenzene, N-nitroso-N-methylaniline and N-nitroso-N,N-dimethylamine was investigated using ram seminal vesicle microsomal prostaglandin H synthase. Both N-nitrosamines are not converted by the studied enzyme. Formaldehyde is produced by the prostaglandin H synthase catalyzed reaction from N,N-dimethyl-4-aminoazobenzene. Arachidonic acid and hydrogen peroxide serve as cofactors for the oxidation of N,N-dimethyl-4-aminoazobenzene. The apparent Michaelis constant and the maximal velocity values for N,N-dimethyl-4-aminoazobenzene as a substrate are 64 μmol/l and 51.2 nmol HCHO/min/mg protein, respectively. In addition to formaldehyde, N-methyl-4-aminoazobenzene and 4-aminoazobenzene, two unknown substances are the products of the N,N-dimethyl-4-aminoazobenzene oxidation. The oxidation of N,N-dimethyl-4-aminoazobenzene catalyzed by prostaglandin H synthase is inhibited by glutathione, ascorbate and NADH. The results suggest that prostaglandin H synthase metabolizes N,N-dimethyl-4-aminoazobenzene through a one-electron oxidation mechanism, giving rise to free radicals.

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18

Scorza, Giuseppe, Donatella Pietraforte, and Maurizio Minetti. "Role of Ascorbate and Protein Thiols in the Release of Nitric oxide from S-Nitroso-Albumin and S-Nitroso-Glutathione in Human Plasma." Free Radical Biology and Medicine 22, no. 4 (1997): 633–42. http://dx.doi.org/10.1016/s0891-5849(96)00378-4.

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19

Kumar, Murugaeson R., and Patrick J. Farmer. "Characterization of Polysulfides, Polysulfanes, and Other Unique Species in the Reaction between GSNO and H2S." Molecules 24, no. 17 (August 26, 2019): 3090. http://dx.doi.org/10.3390/molecules24173090.

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Glutathione-based products, GSnX, of the reaction of hydrogen sulfide, H2S, S-nitroso glutathione, and GSNO, at varied stoichiometries have been analyzed by liquid chromatography high-resolution mass spectrometry (LC-HRMS) and chemical trapping experiments. A wide variety of glutathione-based species with catenated sulfur chains have been identified including sulfanes (GSSnG), sulfides (GSSnH), and sulfenic acids (GSnOH); sulfinic (GSnO2H) and sulfonic (GSnO3H) acids are also seen in reactions exposed to air. The presence of each species of GSnX within the original reaction mixtures was confirmed using Single Ion Chromatograms (SICs), to demonstrate the separation on the LC column, and given approximate quantification by the peak area of the SIC. Further, confirmation for different GSnX families was obtained by trapping with species-specific reagents. Several unique GSnX families have been characterized, including bridging mixed di- and tetra-valent polysulfanes and internal trithionitrates (GSNHSnH) with polysulfane branches. Competitive trapping experiments suggest that the polysulfane chains are formed via the intermediacy of sulfenic acid species, GSSnOH. In the presence of radical trap vinylcyclopropane (VCP) the relative distributions of polysulfane speciation are relatively unaffected, suggesting that radical coupling is not a dominant pathway. Therefore, we suggest polysulfane catenation occurs via reaction of sulfides with sulfenic acids.

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20

Adrian, Katrin, Maria Skogby, Lars Goran Friberg, and Karin Mellgren. "The Effect of S-Nitroso-Glutathione on Platelet and Leukocyte Function During Experimental Extracorporeal Circulation." Artificial Organs 27, no. 6 (June 2003): 570–75. http://dx.doi.org/10.1046/j.1525-1594.2003.07106.x.

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21

Lavergne, Sidonie N., Joseph R. Kurian, Sunil U. Bajad, Jennifer E. Maki, Andrea R. Yoder, Margaret V. Guzinski, Frank M. Graziano, and Lauren A. Trepanier. "Roles of endogenous ascorbate and glutathione in the cellular reduction and cytotoxicity of sulfamethoxazole-nitroso." Toxicology 222, no. 1-2 (May 2006): 25–36. http://dx.doi.org/10.1016/j.tox.2006.01.018.

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22

Hart, Terance W. "Some observations concerning the S-nitroso and S-phenylsulphonyl derivatives of L-cysteine and glutathione." Tetrahedron Letters 26, no. 16 (January 1985): 2013–16. http://dx.doi.org/10.1016/s0040-4039(00)98368-0.

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23

Li, JinGui, WenYing Gu, JianPing Tao, and ZongPing Liu. "The effects of S-nitroso-glutathione on the activities of some isoenzymes in Eimeria tenella oocysts." Veterinary Parasitology 162, no. 3-4 (June 2009): 236–40. http://dx.doi.org/10.1016/j.vetpar.2009.03.017.

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24

Eyanagi, Reiko, Akihisa Toda, Masumi Imoto, Hidemori Uchiyama, Yuji Ishii, Hiroaki Kuroki, Yukako Kuramoto, Shinji Soeda, and Hiroshi Shimeno. "Covalent binding of nitroso-sulfonamides to glutathione S-transferase in guinea pigs with delayed type hypersensitivity." International Immunopharmacology 12, no. 4 (April 2012): 694–700. http://dx.doi.org/10.1016/j.intimp.2012.01.017.

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25

Verma, A., C. P. Malik, and V. K. Gupta. "Sodium Nitroprusside-Mediated Modulation of Growth and Antioxidant Defense in the InVitro raised Plantlets of Peanut Genotypes." Peanut Science 41, no. 1 (January 1, 2014): 25–31. http://dx.doi.org/10.3146/ps12-13.1.

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ABSTRACT As a bioactive signaling molecule, nitric oxide (NO) is involved in multiple plant physiological responses. It regulates diverse biochemical processes in a concentration-dependent manner in plants. Different NO generators viz. sodium nitroprusside (SNP), S-nitroso-N-acetyl penicillinamine (SNAP) and S-nitroso-L-glutathione (GSNO) have been reported, but SNP is the most widely used and effective NO donor. Research was conducted to investigate the in vitro effects of an NO donor, SNP, on biochemical and physiological characteristics such as multiple shoots, chlorophyll content, and enzymatic activities of superoxide dismutase (SOD), catalase (CAT), and others in Arachis hypogaea genotypes (M-13 and PBS24030). In vitro impact of SNP on shoot multiplication potential and chlorophyll content increase upto 100 µM SNP alone in peanut cultivars (M-13 and PBS24030). Rhizogenesis was noticed in the presence of SNP alone. Treatment with SNP and 6-Benzyl adenine (BA) was effective in enhancing the antioxidant enzyme activities, total soluble carbohydrates and proteins as compared to SNP alone in for both cultivars. These data indicate that in vitro establishment of peanut cultivars in the presence of SNP alone and in combination with BA will affect various growth promontory physiological and biochemical parameters. A more complete understanding of plant growth regulator (PGR) mediated responses will be instrumental in designing effective strategies for engineering crops for biotic and abiotic stresses.

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26

Kawasaki, Koh, Robert S. Smith, Chung-Ming Hsieh, Jianxin Sun, Julie Chao, and James K. Liao. "Activation of the Phosphatidylinositol 3-Kinase/Protein Kinase Akt Pathway Mediates Nitric Oxide-Induced Endothelial Cell Migration and Angiogenesis." Molecular and Cellular Biology 23, no. 16 (August 15, 2003): 5726–37. http://dx.doi.org/10.1128/mcb.23.16.5726-5737.2003.

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ABSTRACT To test the hypothesis that the phosphatidylinositol 3-kinase (PI3 kinase)/protein kinase Akt signaling pathway is involved in nitric oxide (NO)-induced endothelial cell migration and angiogenesis, we treated human and bovine endothelial cells with NO donors, S-nitroso-l-glutathione (GSNO) and S-nitroso-N-penicillamine (SNAP). Both GSNO and SNAP increased Akt phosphorylation and activity, which were blocked by cotreatment with the PI3 kinase inhibitor wortmannin. The mechanism was due to the activation of soluble guanylyl cyclase because 8-bromo-cyclic GMP activated PI3 kinase and the soluble guanylyl cyclase inhibitor 1H-[1,2,4]oxadiazolo[4,3-α]quinoxalin-1-one (ODQ) blocked NO-induced PI3 kinase activity. Indeed, transfection with adenovirus containing endothelial cell NO synthase (eNOS) or protein kinase G (PKG) increased endothelial cell migration, which was inhibited by cotransfection with a dominant-negative mutant of PI3 kinase (dnPI3 kinase). In a rat model of hind limb ischemia, adenovirus-mediated delivery of human eNOS cDNA in adductor muscles resulted in time-dependent expression of recombinant eNOS, which was accompanied by significant increases in regional blood perfusion and capillary density. Coinjection of adenovirus carrying dnPI3 kinase abolished neovascularization in ischemic hind limb induced by eNOS gene transfer. These findings indicate that NO promotes endothelial cell migration and neovascularization via cGMP-dependent activation of PI3 kinase and suggest that this pathway is important in mediating NO-induced angiogenesis.

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27

Belder, A. J. d., R. MacAllister, M. W. Radomski, S. Moncada, and P. J. T. Vallance. "Effects of S-nitroso-glutathione in the human forearm circulation: evidence for selective inhibition of platelet activation." Cardiovascular Research 28, no. 5 (May 1, 1994): 691–94. http://dx.doi.org/10.1093/cvr/28.5.691.

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28

Haddad, I. Y., S. Zhu, J. Crow, E. Barefield, T. Gadilhe, and S. Matalon. "Inhibition of alveolar type II cell ATP and surfactant synthesis by nitric oxide." American Journal of Physiology-Lung Cellular and Molecular Physiology 270, no. 6 (June 1, 1996): L898—L906. http://dx.doi.org/10.1152/ajplung.1996.270.6.l898.

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Alveolar type II (ATII) cells, are often exposed to increased concentration of endogenous and exogenous nitric oxide (.NO). Exposure of freshly isolated rat ATII cells for 2 h to 1-3 microM .NO, generated by S-nitroso-N-penicillamine (SNAP), spermine NONOate, or 3-morpholino-sydnonimine (SIN-1) in the presence of superoxide dismutase, resulted in approximately 60% decrease in the rate of surfactant synthesis, as measured by the rate of incorporation of [methyl-3H]choline into phosphatidylcholine, and 60-80% inhibition of cellular ATP levels, as determined by bioluminescence. Similar results were obtained after incubation of ATII cells with authentic peroxynitrite (0.5 mM) but not SIN-1, a putative generator of peroxynitrite. Addition into the medium of oxyhemoglobin (20 microM), which scavenged .NO, or enhancement of ATII glutathione levels by preincubation with glutathione ester (5 mM) totally prevented the NONOate (100 microM) inhibition of cellular ATP. In contrast to the in vitro findings, normal levels of ATP and lipid synthesis were measured in ATII cells isolated from the lungs of rats that breathed .NO gas (80 ppm) in 21% O2 for 2 h (n = 4). This lack of effect may be due either to the presence of various antioxidants (such as glutathione) in the epithelial lining fluid or to the relatively low concentrations of .NO reaching the alveolar epithelium. We conclude that .NO and peroxynitrite, at concentrations likely to be encountered in vivo during inflammation, decrease ATII cell energy stores and surfactant synthesis, which may lead to derangement of important physiological functions.

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29

VOGT, Ryan N., and Daniel J. STEENKAMP. "The metabolism of S-nitrosothiols in the trypanosomatids: the role of ovothiol A and trypanothione." Biochemical Journal 371, no. 1 (April 1, 2003): 49–59. http://dx.doi.org/10.1042/bj20021649.

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It has recently been established that nitrosoglutathione is the preferred substrate of the glutathione-dependent formaldehyde dehydrogenase from divergent organisms. Trypanosomatids produce not only glutathione, but also glutathionylspermidine, trypanothione and ovothiol A. The formaldehyde dehydrogenase activity of Crithidia fasciculata was independent of these thiols and extracts possessed very low levels of nitrosothiol reductase activity with glutathione or its spermidine conjugates as the thiol component. Although ovothiol A did not form a stable nitrosothiol, it decomposed the S-nitroso groups of nitrosoglutathione (GSNO) and dinitrotrypanothione [T(SNO)2] with second-order rate constants of 19.12M-1·s-1 and 8.67M-1·s-1 respectively. The reaction of T(SNO)2 with ovothiol A, however, accelerated to a rate similar to that seen with GSNO. Ovothiol A can act catalytically to decompose these nitrosothiols, although non-productive mechanisms exist. The catalytic phase of the reaction was dependent on the production of thiyl radicals, since it was abolished in the presence of 5,5-dimethyl-1-pyrroline-N-oxide and the formation of nitric oxide could be detected by means of the conversion of oxyhaemoglobin into methaemoglobin. The rate-limiting step in the catalytic process was the reduction of oxidized ovothiol species and, in this respect, T(SNO)2 is a more efficient substrate than GSNO. Trypanothione decomposed GSNO with a second-order rate constant of 0.786M-1·s-1 and the major nitrogenous end product changed from nitrite to ammonia as the ratio of thiol to nitrosothiol increased. The results indicate that ovothiol A acts in synergy with trypanothione in the decomposition of T(SNO)2.

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30

Buca, B. R., E. G. Popa, N. L. Hilitanu, E. C. Lupusoru, and L. Mititelu-Tartau. "P.113 The nitric oxide donors nebivolol and S-nitroso-glutathione decrease the spontaneous motor behaviour in rats." European Neuropsychopharmacology 29 (December 2019): S95—S96. http://dx.doi.org/10.1016/j.euroneuro.2019.09.168.

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31

JENSEN, David E., George K. BELKA, and Garrett C. Du BOIS. "S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme." Biochemical Journal 331, no. 2 (April 15, 1998): 659–68. http://dx.doi.org/10.1042/bj3310659.

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An enzyme isolated from rat liver cytosol (native molecular mass 78.3 kDa; polypeptide molecular mass 42.5 kDa) is capable of catalysing the NADH/NADPH-dependent degradation of S-nitrosoglutathione (GSNO). The activity utilizes 1 mol of coenzyme per mol of GSNO processed. The isolated enzyme has, as well, several characteristics that are unique to alcohol dehydrogenase (ADH) class III isoenzyme: it is capable of catalysing the NAD+-dependent oxidations of octanol (insensitive to inhibition by 4-methylpyrazole), methylcrotyl alcohol (stimulated by added pentanoate) and 12-hydroxydodecanoic acid, and also the NADH/NADPH-dependent reduction of octanal. Methanol and ethanol oxidation activity is minimal. The enzyme has formaldehyde dehydrogenase activity in that it is capable of catalysing the NAD+/NADP+-dependent oxidation of S-hydroxymethylglutathione. Treatment with the arginine-specific reagent phenylglyoxal prevents the pentanoate stimulation of methylcrotyl alcohol oxidation and markedly diminishes the enzymic activity towards octanol, 12-hydroxydodecanoic acid and S-hydroxymethylglutathione; the capacity to catalyse GSNO degradation is also checked. Additionally, limited peptide sequencing indicates 100% correspondence with known ADH class III isoenzyme sequences. Kinetic studies demonstrate that GSNO is an exceptionally active substrate for this enzyme. S-Nitroso-N-acetylpenicillamine and S-nitrosated human serum albumin are not substrates; the activity towards S-nitrosated glutathione mono- and di-ethyl esters is minimal. Product analysis suggests that glutathione sulphinamide is the major stable product of enzymic GSNO processing, with minor yields of GSSG and NH3; GSH, hydroxylamine, nitrite, nitrate and nitric oxide accumulations are minimal. Inclusion of GSH in the reaction mix decreases the yield of the supposed glutathione sulphinamide in favor of GSSG and hydroxylamine.

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32

Langford, Edward J., Andrew Parfitt, Adam J. de Beider, Michael T. Marrinan, and John F. Martin. "A Study of Platelet Activation during Human Cardiopulmonary Bypass and the Effect of S-Nitrosoglutathione." Thrombosis and Haemostasis 78, no. 06 (1997): 1516–19. http://dx.doi.org/10.1055/s-0038-1665444.

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SummaryCardiac surgery is complicated by the occurrence of post-operative bleeding due to platelet dysfunction. This is largely caused by platelet activation and consumption during cardiopulmonary bypass. Patients undergoing cardiac surgery requiring cardiopulmonary bypass were studied to determine whether early platelet changes due to bypass could be inhibited using the platelet-selective nitric oxide donor S-nitroso-glutathione (GSNO). Flow cytometry was used to measure platelet surface expression of P-selectin (an α-granule protein) and glycoproteins (GP) IIb/IIIa and Ib (mediators of aggregation and adhesion) before and 5 and 10 min after commencing cardiopulmonary bypass, in 6 controls and 6 patients receiving GSNO 50 μg/min. Platelet P-selectin expression increased during bypass both in controls and patients receiving GSNO. Glycoproteins IIb/IIIa and Ib fell during bypass in control and GSNO-treated patients. There was no difference between control and GSNO-treated groups. Thus no significant platelet inhibition by S-nitrosoglutathione was demonstrated under these conditions.

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33

Igarashi, Junsuke, Masashi Nishida, Shiro Hoshida, Nobushige Yamashita, Hiroaki Kosaka, Masatsugu Hori, Tsunehiko Kuzuya, and Michihiko Tada. "Inducible nitric oxide synthase augments injury elicited by oxidative stress in rat cardiac myocytes." American Journal of Physiology-Cell Physiology 274, no. 1 (January 1, 1998): C245—C252. http://dx.doi.org/10.1152/ajpcell.1998.274.1.c245.

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The effects of nitric oxide (NO) produced by cardiac inducible NO synthase (iNOS) on myocardial injury after oxidative stress were examined. Interleukin-1β induced cultured rat neonatal cardiac myocytes to express iNOS. After induction of iNOS,l-arginine enhanced NO production in a concentration-dependent manner. Glutathione peroxidase (GPX) activity in myocytes was attenuated by elevated iNOS activity and by an NO donor, S-nitroso- N-acetyl-penicillamine (SNAP). Although NO production by iNOS did not induce myocardial injury, NO augmented release of lactate dehydrogenase from myocyte cultures after addition of H2O2(0.1 mM, 1 h). Inhibition of iNOS with Nω-nitro-l-arginine methyl ester ameliorated the effects of NO-enhancing treatments on myocardial injury and GPX activity. SNAP augmented the myocardial injury induced by H2O2. Inhibition of GPX activity with antisense oligodeoxyribonucleotide for GPX mRNA increased myocardial injury by H2O2. Results suggest that the induction of cardiac iNOS promotes myocardial injury due to oxidative stress via inactivation of the intrinsic antioxidant enzyme, GPX.

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Li, JinGui, Tao Xing, Lin Wang, JianPing Tao, and ZongPing Liu. "Inhibitory effect of S-nitroso-glutathione on Eimeria tenella oocysts was mainly limited to the early stages of sporogony." Veterinary Parasitology 173, no. 1-2 (October 2010): 64–69. http://dx.doi.org/10.1016/j.vetpar.2010.06.022.

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35

Liu, Yang, Yichao Yuan, Zhuoke Jiang, and Songheng Jin. "Nitric Oxide Improves Salt Tolerance of Cyclocarya paliurus by Regulating Endogenous Glutathione Level and Antioxidant Capacity." Plants 11, no. 9 (April 25, 2022): 1157. http://dx.doi.org/10.3390/plants11091157.

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Cyclocarya paliurus is commonly used to treat diabetes in China. However, the natural habitats of C. paliurus are typically affected by salt stress. Previous studies showed that nitric oxide (NO) level was related to salt tolerance of C. paliurus, and its synthesis was induced by exogenous hydrogen sulfide. However, the effects of different NO donors in alleviating the negative effect of salt stress are still unclear. In the present study, C. paliurus seedlings pretreated with three NO donors (S-nitroso-N-acetylpenicillamine, SNAP and S-nitrosoglutathione, GSNO and sodium nitroprusside, SNP) were exposed to salt stress, and then, the total biomass, chlorophyll fluorescence parameters, NO and glutathione levels, oxidative damage, and antioxidant enzyme activities were investigated. The results showed that pretreatment of NO donors maintained chlorophyll fluorescence and attenuated the loss of plant biomass under salt stress, and the best performance was observed in C. paliurus under SNP treatment. We also found that pretreatment of NO donors further increased the endogenous NO content and nitrate reductase (NR) activity compared with salt treatment. Moreover, pretreatment with NO donors, especially SNP, alleviated salt-induced oxidative damage, as indicated by lowered lipid peroxidation, through an enhanced antioxidant system including glutathione accumulation and increased antioxidant enzyme activities. The supply of NO donors is an interesting strategy for alleviating the negative effect of salt on C. paliurus. Our data provide new evidence contributing to the current understanding of NO-induced salt stress tolerance.

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36

Liu, Yang, Yichao Yuan, Zhuoke Jiang, and Songheng Jin. "Nitric Oxide Improves Salt Tolerance of Cyclocarya paliurus by Regulating Endogenous Glutathione Level and Antioxidant Capacity." Plants 11, no. 9 (April 25, 2022): 1157. http://dx.doi.org/10.3390/plants11091157.

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Cyclocarya paliurus is commonly used to treat diabetes in China. However, the natural habitats of C. paliurus are typically affected by salt stress. Previous studies showed that nitric oxide (NO) level was related to salt tolerance of C. paliurus, and its synthesis was induced by exogenous hydrogen sulfide. However, the effects of different NO donors in alleviating the negative effect of salt stress are still unclear. In the present study, C. paliurus seedlings pretreated with three NO donors (S-nitroso-N-acetylpenicillamine, SNAP and S-nitrosoglutathione, GSNO and sodium nitroprusside, SNP) were exposed to salt stress, and then, the total biomass, chlorophyll fluorescence parameters, NO and glutathione levels, oxidative damage, and antioxidant enzyme activities were investigated. The results showed that pretreatment of NO donors maintained chlorophyll fluorescence and attenuated the loss of plant biomass under salt stress, and the best performance was observed in C. paliurus under SNP treatment. We also found that pretreatment of NO donors further increased the endogenous NO content and nitrate reductase (NR) activity compared with salt treatment. Moreover, pretreatment with NO donors, especially SNP, alleviated salt-induced oxidative damage, as indicated by lowered lipid peroxidation, through an enhanced antioxidant system including glutathione accumulation and increased antioxidant enzyme activities. The supply of NO donors is an interesting strategy for alleviating the negative effect of salt on C. paliurus. Our data provide new evidence contributing to the current understanding of NO-induced salt stress tolerance.

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37

Khan, S., M. Kayahara, U. Joashi, N. D. Mazarakis, C. Sarraf, A. D. Edwards, M. N. Hughes, and H. Mehmet. "Differential induction of apoptosis in Swiss 3T3 cells by nitric oxide and the nitrosonium cation." Journal of Cell Science 110, no. 18 (September 15, 1997): 2315–22. http://dx.doi.org/10.1242/jcs.110.18.2315.

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We have investigated the effect of nitric oxide (NO) on apoptosis in Swiss 3T3 fibroblasts and compared it to the effect of the nitrosonium cation (NO+). Both species induced apoptosis, confirmed by electron microscopy, propidium iodide staining, DNA laddering and activation of caspases. The kinetics of triggering apoptosis were different for the two redox species: NO+ required only a 2 hour exposure, whereas NO required 24 hours. Three sources of NO were used: aqueous solutions of NO and two NO donors, S-nitrosoglutathione and S-nitroso-N-acetylpenicillamine. The time course of apoptosis induced by these two S-nitrosothiols correlated with their rate of decomposition to NO. The apoptotic effect of NO was reduced in the presence of the NO scavenger oxyhaemoglobin, or the antioxidants N-acetylcysteine and ascorbic acid, whereas in the case of NO+ these antioxidants potentiated apoptosis. Glutathione also had a potentiating effect on the cytotoxicity of NO+. This suggests that cellular antioxidants may play a role in protecting the cell from NO-induced apoptosis while NO+ may trigger apoptosis independently of oxidative stress mechanisms.

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Veleeparampil, Manoj M., Usha K. Aravind, and C. T. Aravindakumar. "Decomposition of S-Nitrosothiols Induced by UV and Sunlight." Advances in Physical Chemistry 2009 (January 17, 2009): 1–5. http://dx.doi.org/10.1155/2009/890346.

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Photochemical release of nitric oxide (NO) from the S-nitroso derivatives of glutathione, L-cysteine, N-acetyl-L-cysteine, L-cysteinemethylester, D,L-penicillamine, N-acetyl-D,L-penicillamine, and N-acetylcysteamine has been investigated at neutral and acidic pH. The release of NO from RSNO is one of the key reactions that could be utilized in photodynamic therapy. The UV-VIS and HPLC analyses have shown that under argon saturated conditions, disulfide (RSSR) is the major product of UV as well as sunlight induced decomposition. While in aerated conditions, nitirite—the end product of the oxidation of NO—was also observed along with disulfide. The formation of thiyl radical as the intermediate was reconfirmed by laser flash photolysis. The initial rate of formation of NO was on the order of 10−10dm3mol−1s−1. The quantum yields of these reactions were in the range of 0.2–0.8. The high quantum yields observed in the photo induced release of NO from RSNO using both UV and sunlight demonstrate the potential application of these reactions in photodynamic therapy.

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Ravi Kumar, Murugaeson, Tara Clover, and Patrick Farmer. "Sulfomics and Nitromics: Characterizations of S- and N-Based Speciation in Reactions of S-nitroso-glutathione (GSNO) with Hydrogen Sulfide (H2S)." Free Radical Biology and Medicine 87 (October 2015): S79—S80. http://dx.doi.org/10.1016/j.freeradbiomed.2015.10.210.

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40

White, Thomas A., Timothy F. Walseth, and Mathur S. Kannan. "Nitric oxide inhibits ADP-ribosyl cyclase through a cGMP-independent pathway in airway smooth muscle." American Journal of Physiology-Lung Cellular and Molecular Physiology 283, no. 5 (November 1, 2002): L1065—L1071. http://dx.doi.org/10.1152/ajplung.00064.2002.

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There is evidence for a role of cyclic ADP-ribose (cADPR) in intracellular Ca2+ regulation in smooth muscle. cADPR is synthesized and degraded by ADP-ribosyl cyclase and cADPR hydrolase, respectively, by a bifunctional protein, CD38. Nitric oxide (NO) inhibits intracellular Ca2+mobilization in airway smooth muscle. The present study was designed to determine whether this inhibition is due to regulation of ADP-ribosyl cyclase and/or cADPR hydrolase activity. Sodium nitroprusside (SNP) and S-nitroso- N-acetylpenicillamine, NO donors, produced a concentration-dependent decrease in ADP-ribosyl cyclase, but not cADPR hydrolase, activity. The NO scavenger carboxy-PTIO prevented and reversed, and reduced glutathione prevented, the inhibition of ADP-ribosyl cyclase by SNP, suggesting S-nitrosylation by NO as a mechanism. N-ethylmaleimide, which covalently modifies protein sulfhydryl groups, making them incapable of nitrosylation, produced a marked inhibition of ADP-ribosyl cyclase, but not cADPR hydrolase, activity. SNP and N-ethylmaleimide significantly inhibited the ADP-ribosyl cyclase activity in recombinant human CD38 without affecting the cADPR hydrolase activity. These results provide a novel mechanism for differential regulation of CD38 by NO through a cGMP-independent pathway involving S-nitrosylation of thiols.

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41

Jahnová, Jana, Lenka Luhová, and Marek Petřivalský. "S-Nitrosoglutathione Reductase—The Master Regulator of Protein S-Nitrosation in Plant NO Signaling." Plants 8, no. 2 (February 21, 2019): 48. http://dx.doi.org/10.3390/plants8020048.

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S-nitrosation has been recognized as an important mechanism of protein posttranslational regulations, based on the attachment of a nitroso group to cysteine thiols. Reversible S-nitrosation, similarly to other redox-base modifications of protein thiols, has a profound effect on protein structure and activity and is considered as a convergence of signaling pathways of reactive nitrogen and oxygen species. In plant, S-nitrosation is involved in a wide array of cellular processes during normal development and stress responses. This review summarizes current knowledge on S-nitrosoglutathione reductase (GSNOR), a key enzyme which regulates intracellular levels of S-nitrosoglutathione (GSNO) and indirectly also of protein S-nitrosothiols. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions have been uncovered. Extensive studies of plants with down- and upregulated GSNOR, together with application of transcriptomics and proteomics approaches, seem promising for new insights into plant S-nitrosothiol metabolism and its regulation.

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42

Nassi, Achille, Loan To Thi Kim, Aurélie Girard, Laurent Griscom, Florence Razan, Sophie Griveau, Laurent Thouin, and Fethi Bedioui. "Comparison of three different configurations of dual ultramicroelectrodes for the decomposition of S-Nitroso-L-glutathione and the direct detection of nitric oxide." Microchimica Acta 179, no. 3-4 (July 11, 2012): 337–43. http://dx.doi.org/10.1007/s00604-012-0860-z.

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43

Triquigneaux, Mathilde, Béatrice Tuccio, Robert Lauricella, and Laurence Charles. "Nucleophile addition of reduced glutathione on 2-methyl-2-nitroso compound: A combined electron paramagnetic resonance spectroscopy and electrospray tandem mass spectrometry study." Journal of the American Society for Mass Spectrometry 20, no. 11 (November 2009): 2013–20. http://dx.doi.org/10.1016/j.jasms.2009.07.018.

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44

Tullett, Jayne M., Daryl D. Rees, David E. G. Shuker, and Andreas Gescher. "Lack of correlation between the observed stability and pharmacological properties of S-nitroso derivatives of glutathione and cysteine-related peptides11Abbreviations: NO, nitric oxide; RSNO, S-nitrosothiol; CysH, cysteine; SNOGSH, S-nitrosoglutathione; SNOCys, S-nitrosocysteine; SNOGluCys, S-nitroso-l-γ-glutamyl-l-cysteine; SNOCysGly, S-nitroso-l-cysteinylglycine; SNOPROPA, S-nitroso-3-mercaptopropionic acid; SNONAC, S-nitroso-N-acetyl-l-cysteine; DTPA, diethylenetriaminpentaacetic acid; and MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide." Biochemical Pharmacology 62, no. 9 (November 2001): 1239–47. http://dx.doi.org/10.1016/s0006-2952(01)00750-x.

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45

Li, Chung-Yu, Ting-Yu Chin, and Sheau-Huei Chueh. "Rat cerebellar granule cells are protected from glutamate-induced excitotoxicity by S-nitrosoglutathione but not glutathione." American Journal of Physiology-Cell Physiology 286, no. 4 (April 2004): C893—C904. http://dx.doi.org/10.1152/ajpcell.00127.2003.

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In cultured rat cerebellar granule cells, glutamate or N-methyl-d-aspartate (NMDA) activation of the NMDA receptor caused a sustained increase in cytosolic Ca2+ levels ([Ca2+]i), reactive oxygen species (ROS) generation, and cell death (respective EC50 values for glutamate were 12, 30, and 38 μM) but no increase in caspase-3 activity. Removal of extracellular Ca2+ blocked all three glutamate-induced effects, whereas pretreatment with an ROS scavenger inhibited glutamate-induced cell death but had no effect on the [Ca2+]i increase. This indicates that glutamate-induced cell death is attributable to [Ca2+]i increase and ROS generation, and the [Ca2+]i increase precedes ROS generation. Apoptotic cell death was not seen until 24 h after exposure of cells to glutamate. S-nitrosoglutathione abolished glutamate-induced ROS generation and cell death, and only a transient [Ca2+]i increase was seen; similar results were observed with another nitric oxide (NO) donor, S-nitroso- N-acetylpenicillamine, but not with glutathione, which suggests that the effects were caused by NO. The transient [Ca2+]i increase and the abolishment of ROS generation induced by glutamate and S-nitrosoglutathione were still seen in the presence of an ROS scavenger. Glial cells, which were present in the cultures used, showed no [Ca2+]i increase in the presence of glutamate, and glutamate-induced granule cell death was independent of the percentage of glial cells. In conclusion, NO donors protect cultured cerebellar granule cells from glutamate-induced cell death, which is mediated by ROS generated by a sustained [Ca2+]i increase, and glial cells provide negligible protection against glutamate-induced excitotoxicity.

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Fernandes, Ana B., Maria P. Guarino, and M. Paula Macedo. "Understanding the in-vivo relevance of S-nitrosothiols in insulin action." Canadian Journal of Physiology and Pharmacology 90, no. 7 (July 2012): 887–94. http://dx.doi.org/10.1139/y2012-090.

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Insulin sensitivity is maximal in the postprandial state, decreasing with a fasting period through a mechanism that is dependent on the integrity of the hepatic parasympathetic nerves/nitric oxide (NO) production and increased hepatic glutathione (GSH) levels. GSH and NO react to form S-nitrosoglutathione (GSNO), an S-nitrosothiol (RSNO) for which the in-vivo effects are still being determined. The goal of this study was to test the hypothesis that in-vivo administration of RSNOs, GSNO, or S-nitroso-N-acetylpenicillamine (SNAP) increases insulin sensitivity in fasted or fed-denervated animals, but not in fed animals, where full postprandial insulin sensitivity is achieved. Fasted, fed, or fed-denervated male Wistar rats were used as models for different insulin sensitivity conditions. The rapid insulin sensitivity test (RIST) was used to measure insulin-stimulated glucose disposal before and after drug administration (GSNO, SNAP, or 3-morpholinosydnonimine (SIN-1), intravenous (i.v.) or to the portal vein (i.p.v.)). Fast insulin sensitivity was not altered by administration of SIN-1 (neither i.v. nor i.p.v.). Intravenous infusion of RSNOs in fasted and fed hepatic denervated rats increased insulin sensitivity by 126.35% ± 35.43% and 82.7% ± 12.8%, respectively. In fed animals, RSNOs decreased insulin sensitivity indicating a negative feedback mechanism. These results suggest that RSNOs incremental effect on insulin sensitivity represent a promising therapeutical tool in insulin resistance states.

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FRANK, Stefan, Birgit STALLMEYER, Heiko KÄMPFER, Christian SCHAFFNER, and Josef PFEILSCHIFTER. "Differential regulation of vascular endothelial growth factor and its receptor fms-like-tyrosine kinase is mediated by nitric oxide in rat renal mesangial cells." Biochemical Journal 338, no. 2 (February 22, 1999): 367–74. http://dx.doi.org/10.1042/bj3380367.

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Under conditions associated with local and systemic inflammation, mesangial cells and invading immune cells are likely to be responsible for the release of large amounts of nitric oxide (NO) in the glomerulus. To further define the mechanisms of NO action in the glomerulus, we attempted to identify genes which are regulated by NO in rat glomerular mesangial cells. We identified vascular endothelial growth factor (VEGF) and its receptor fms-like tyrosine kinase (FLT-1) to be under the regulatory control of exogenously applied NO in these cells. Using S-nitroso-glutathione (GSNO) as an NO-donating agent, VEGF expression was strongly induced, whereas expression of its FLT-1 receptor simultaneously decreased. Expressional regulation of VEGF and FLT-1 mRNA was transient and occurred rapidly within 1–3 h after GSNO treatment. Expression of a second VEGF-specific receptor, fetal liver kinase-1 (FLK-1/KDR), could not be detected. The inflammatory cytokine interleukin-1β mediated a moderate increase in VEGF expression after 24 h and had no influence on FLT-1 expression. In contrast, platelet-derived growth factor–BB and basic fibroblast growth factor had no effect on VEGF expression, but strongly induced FLT-1 mRNA levels. Obviously, there is a differential regulation of VEGF and its receptor FLT-1 by NO, cytokines and growth factors in rat mesangial cells.

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Sharma, A., K. Kolanjiappan, D. McDonald, C. Yount, and I. Singh. "7 CHEMOTHERAPEUTIC ACTIVITY OF S-NITROSO-GLUTATHIONE ALONE AND IN COMBINATION WITH CISPLATIN AND RADIATION IN HEAD AND NECK CANCER CELLS AND MOUSE XENOGRAFT MODEL." Radiotherapy and Oncology 102 (March 2012): S1. http://dx.doi.org/10.1016/s0167-8140(12)70001-4.

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49

Khan, Muhammad Aaqil, Abdul Latif Khan, Qari Muhammad Imran, Sajjad Asaf, Sang-Uk Lee, Byung-Wook Yun, Muhammad Hamayun, Tae-Han Kim, and In-Jung Lee. "Exogenous application of nitric oxide donors regulates short-term flooding stress in soybean." PeerJ 7 (October 8, 2019): e7741. http://dx.doi.org/10.7717/peerj.7741.

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Short-term water submergence to soybean (Glycine max L.) create hypoxic conditions hindering plant growth and productivity. Nitric oxide (NO) is considered a stress-signalling and stress-evading molecule, however, little is known about its role during flooding stress. We elucidated the role of sodium nitroprusside (SNP) and S-nitroso L-cysteine (CySNO) as NO donor in modulation of flooding stress-related bio-chemicals and genetic determinants of associated nitrosative stress to Daewon and Pungsannamul soybean cultivars after 3 h and 6 h of flooding stress. The results showed that exogenous SNP and CysNO induced glutathione activity and reduced the resulting superoxide anion contents during short-term flooding in Pungsannamul soybean. The exo- SNP and CysNO triggered the endogenous S-nitrosothiols, and resulted in elevated abscisic acid (ABA) contents in both soybean cultivars overtime. To know the role of ABA and NO related genes in short-term flooding stress, the mRNA expression of S-nitrosoglutathione reductase (GSNOR1), NO overproducer1 (NOX1) and nitrate reductase (NR), Timing of CAB expression1 (TOC1), and ABA-receptor (ABAR) were assessed. The transcripts accumulation of GSNOR1, NOX1, and NR being responsible for NO homeostasis, were significantly high in response to early or later phases of flooding stress. ABAR and TOC1 showed a decrease in transcript accumulation in both soybean plants treated with exogenous SNP and CySNO. The exo- SNP and CySNO could impinge a variety of biochemical and transcriptional programs that can mitigate the negative effects of short-term flooding stress in soybean.

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Merial, Christelle, Anne Bouloumie, Véronique Trocheris, Max Lafontan, and Jean Galitzky. "Nitric oxide-dependent downregulation of adipocyte UCP-2 expression by tumor necrosis factor-α." American Journal of Physiology-Cell Physiology 279, no. 4 (October 1, 2000): C1100—C1106. http://dx.doi.org/10.1152/ajpcell.2000.279.4.c1100.

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Uncoupling protein-2 (UCP-2) is a mitochondrial protein expressed in adipocytes and has recently been involved in the control of energy dissipation. Because obesity is characterized by an imbalance between energy intake and expenditure and by an enhanced adipocyte-derived secretion of tumor necrosis factor-α (TNF-α), we asked whether TNF-α could directly influence UCP-2 expression in adipocytes. Experiments performed in differentiated 3T3F442A preadipocytes showed that TNF-α (10 ng/ml) induced a reduction of UCP-2 trancripts, assessed by Northern blot analysis. A significant decrease in UCP-2 expression (40%) was observed after 12 and 24 h of TNF-α stimulation of the cells. The characterization of the mechanisms responsible for the TNF-α effect on UCP-2 expression demonstrates an involvement of the TNF-α-induced inducible (i) nitric oxide synthase (NOS) expression. Cell treatment with the NOS inhibitor N G-nitro-l-arginine methyl ester (l-NAME; 1 mmol/l) significantly diminished the TNF-α-mediated sustained downregulation of UCP-2 expression, whereas cell treatment with a nitric oxide (NO) donor (10−3 mol/l S-nitroso-l-glutathione) mimicked the TNF-α effect on UCP-2 expression. Moreover, Western blot analysis clearly showed that TNF-α alone induces the expression of iNOS after 12–24 h treatment of differentiated 3T3F442A cells. These experiments demonstrate that TNF-α directly downregulates UCP-2 expression via NO-dependent pathways that involve the induction of iNOS expression.

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