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• W2168033887 abstract "HomeHypertensionVol. 45, No. 1Role of Circulating S-Nitrosothiols in Control of Blood Pressure Free AccessEditorialPDF/EPUBAboutView PDFView EPUBSections ToolsAdd to favoritesDownload citationsTrack citationsPermissions ShareShare onFacebookTwitterLinked InMendeleyReddit Jump toFree AccessEditorialPDF/EPUBRole of Circulating S-Nitrosothiols in Control of Blood Pressure Matthew W. Foster, John R. Pawloski, David J. Singel and Jonathan S. Stamler Matthew W. FosterMatthew W. Foster From the Howard Hughes Medical Institute (M.W.F., J.S.S.), and Departments of Medicine (J.R.P., J.S.S.) and Biochemistry (J.S.S.), Duke University Medical Center, Durham, NC; and the Department of Chemistry and Biochemistry (D.J.S.), Montana State University, Bozeman, Mont. Search for more papers by this author , John R. PawloskiJohn R. Pawloski From the Howard Hughes Medical Institute (M.W.F., J.S.S.), and Departments of Medicine (J.R.P., J.S.S.) and Biochemistry (J.S.S.), Duke University Medical Center, Durham, NC; and the Department of Chemistry and Biochemistry (D.J.S.), Montana State University, Bozeman, Mont. Search for more papers by this author , David J. SingelDavid J. Singel From the Howard Hughes Medical Institute (M.W.F., J.S.S.), and Departments of Medicine (J.R.P., J.S.S.) and Biochemistry (J.S.S.), Duke University Medical Center, Durham, NC; and the Department of Chemistry and Biochemistry (D.J.S.), Montana State University, Bozeman, Mont. Search for more papers by this author and Jonathan S. StamlerJonathan S. Stamler From the Howard Hughes Medical Institute (M.W.F., J.S.S.), and Departments of Medicine (J.R.P., J.S.S.) and Biochemistry (J.S.S.), Duke University Medical Center, Durham, NC; and the Department of Chemistry and Biochemistry (D.J.S.), Montana State University, Bozeman, Mont. Search for more papers by this author Originally published22 Nov 2004https://doi.org/10.1161/01.HYP.0000150160.41992.71Hypertension. 2005;45:15–17Other version(s) of this articleYou are viewing the most recent version of this article. Previous versions: November 22, 2004: Previous Version 1 The biological effects of nitric oxide (NO) are in large part mediated by S-nitrosylation of peptides and proteins to produce bioactive S-nitrosothiols (SNOs).1–3 The observation of abnormal SNO levels in numerous pathophysiological states2 suggests that dysregulation of SNO homeostasis may contribute to disease pathogenesis. For example, the hypotension of human sepsis is accompanied by increases in circulating levels of vasodilatory SNOs.3 Although such altered SNO levels may simply mirror NO production (eg, induction of inducible NO synthase in sepsis), they may also reflect changes specific to SNO biosynthesis and metabolism. Indeed, mice lacking a SNO-metabolizing enzyme are profoundly hypotensive under anesthesia.3 Thus, blood pressure is evidently regulated by both synthesis and turnover of SNOs. In this issue of Hypertension, Gandley et al4 extend this paradigm by proposing that a defect in SNO turnover contributes to the hypertension of preeclampsia.In the blood, S-nitrosoalbumin (SNO-albumin) and S-nitrosohemoglobin (SNO-Hb) constitute the major conduits for circulating NO bioactivity. Although both SNOs may influence blood pressure, they operate within distinct signaling circuits. SNO-Hb can be viewed as a principal regulator of SNO homeostasis, adaptively modulating NO chemistry to control NO bioactivity. SNO-Hb is formed by transfer of NO from heme-iron to Cysβ93 thiol on T to R structural transition (oxygenation) of the hemoglobin tetramer.5 SNO-Hb associates with the red blood cell (RBC) membrane via an interaction with the cytoplasmic domain of anion-exchanger 1 protein (CDAE1, Band 3); on deoxygenation (R→T) transfer of the NO group from SNO-Hb to a cysteine thiol within CDAE1 supports export of RBC vasodilatory activity.6 SNO-Hb thus serves as an O2 sensor and O2-dependent transducer of NO bioactivity. In contrast, it appears that rather than transducing a specific signal, albumin operates as a buffer to maintain NO homeostasis.7S-nitrosylation of albumin occurs at Cys347 via reactions—with NO or nitrosothiols—that are favored by design: specifically, both hydrophobic pockets in albumin (NO/O2 coupling) and bound copper (NO/metal redox coupling) may serve to generate nitrosylating species.8–10 Gandley et al4 make the case that the buffering function of SNO-albumin is impaired in preeclamptic patients, where the thiol of albumin acts as a sink for NO and thus, raises blood pressure. Nudler and colleagues9 have previously demonstrated that albumin can raise blood pressure independently of its oncotic effects: Redistribution of NO, from the tissues into the hydrophobic core of the protein, subserves S-nitrosylation and lowers the steady-state level of vasodilatory NO within the vascular smooth muscle.9Accumulating evidence strongly suggests a role of SNO-albumin in mitigating cardiovascular risk. Elevated (>2 μmol/L) concentrations of plasma SNOs (of which SNO-albumin is the major constituent) portend adverse cardiovascular outcomes in patients with end-stage renal disease and correlate with elevated blood pressures.11 Plasma SNOs are also elevated in patients with hypercholesterolemia.12 Increases in SNO are correlated with an increase in plasma ceruloplasmin, a protein that is known to support SNO synthesis,13 and with a decline in ascorbate, a compound known to promote SNO degradation.14 Gandley et al4 proffer compelling evidence that SNO throughput, not level, is the key measure of NO bioactivity in plasma. They observe elevated levels of SNO-albumin in preeclamptic versus normal pregnancy plasma (7 μmol/L versus 2 μmol/L, respectively) and link reduced levels of ascorbate in preeclampsia to impaired SNO-albumin–dependent vasorelaxation.4 (Notably, SNO-albumin is elevated in preeclampsia despite factors that might be assumed to abrogate the formation of nitrosothiols, including a well characterized oxidative stress and deficit of endothelial-derived NO.)Excessive sequestration of SNOs also occurs in patients with type I diabetes mellitus.15 In this case, however, hemoglobin is the culprit. Accumulation of SNO-Hb in diabetes has been attributed to glycosylation of Hb, which preferentially stabilizes the R structure, thereby impairing NO group release. Reduced vasodilation by diabetic RBCs has been implicated in the microvascular flow impairment associated with the disease. Hypoxic vasodilatory activity of RBCs is also impaired in other disorders of heart, lung, and blood,2,16 consistent with the idea that RBCs regulate blood flow to maximize O2 delivery.16–18 Accumulations of SNO-Hb can also raise blood pressure. This effect, however, occurs through some central action rather than through peripheral vasoconstriction. Comparable levels of plasma hemoglobin (micromolar) have no pressor effects,19 despite the frequent claims to the contrary.20Gandley et al4 add much to address the perpetuated controversy over the concentration of plasma SNOs. They not only report a new set of measurements that are complementary to and consistent with previous work,21 but also provide a confirmatory measure of activity. Levels of plasma SNOs ranging from 10 nmol/L to ≈10 μmol/L (this study) in the literature reflect differences in sample preparation and handling, choice of standards, and detection methods.22 Mass spectrometry of human plasma shows SNO-albumin levels in the 200 nmol/L range,23,24 establishing a lower limit of normal. The idea published by Gladwin25 (and Feelisch26 using the method of Gladwin) that SNOs constitute a negligible to undetectable fraction of bioactive NOx species in plasma and blood should be viewed with skepticism. The discrepancy between multiple methods,16,22 most notably the direct mass spectroscopic approach23,24 and the method of Gladwin,25,27 indicates that the latter is inappropriate for use in complex biological samples. In our experience, the use of acid, thiol blocking agents, and sulfanilamide (to remove contaminating nitrite), destabilizes some SNO (and iron nitrosyl Hb) species, whereas the precipitation that ensues prevents access to others. Disruption of cellular and organellar integrity may also destabilize SNO-proteins by providing unfettered access to various effectors of SNO stability (eg, Ca2+, Mg2+, other proteins).28 Finally, the Gladwin assay does not properly differentiate SNO-Hb from iron nitrosyl Hb or nitrite.16,22 Indeed, measurements of iron nitrosyl Hb in rodents29 by the method of Gladwin are also incompatible with the direct EPR measurements by Kirima et al.30In addition to quantitative measurements using the biotin switch assay4 and 4,5,-diaminofluorescein–based detection,21 Kagan, Gandley, and coworkers also directly measure the liberation of both NO and NO-dependent bioactivity from plasma samples (in healthy controls versus preeclamptic patients) by reaction with exogenous Cu2+ and ascorbate.4 In this assay, ascorbate functions to reduce Cu2+ to Cu+, which in turn reduces nitrosothiol to thiolate and nitric oxide. Taken together, the results of these different methods make a persuasive case for a buildup of SNO in preeclampsia. Nevertheless, we offer a word of caution. Whereas the authors infer from their assays differences in amounts of SNO, some measurements may instead reflect differential reactivity of the various SNOs22 (eg, in health versus disease). Thus, for example, the Cu/ascorbate redox reaction may be favored in preeclamptic versus normal pregnancy plasma and thus yield apparent differences from similar amounts of SNO-albumin. Indeed, Kagan et al have shown that the ascorbate-oxidizing activity of Cu2+ (with formation of Cu+) is greater in preeclamptic than in normal plasma.31 They suggest that this phenomenon is because of an increased fatty acid content of albumin in preeclampsia, as fatty acids modulate both copper-binding to albumin and Cys34 reactivity,31,32 and thus may potentiate Cu/ascorbate-dependent decomposition of SNO-albumin.4The challenge remains to determine the molecular basis for altered SNO-albumin levels in preeclampsia. Plasma ascorbate is 50% lower in preeclampsia versus normals. Gandley et al4 argue for a defect in ascorbate/Cu-mediated release of NO. They find that in the (patho)physiological range of plasma ascorbate concentrations, the rate of NO release from SNO-albumin depends linearly on ascorbate, suggesting that the lower levels of ascorbate in preeclampsia could account for the increase in SNO-albumin. Because these experiments required exogenous copper, identification of the endogenous source of copper would advance the case for physiological relevance. Alternatively, SNO-albumin denitrosylation may be regulated via transnitrosylation with glutathione (GSH) or cysteine, which readily accept NO+ from SNO-proteins. In preeclampsia, plasma GSH levels are low,33 most likely because of oxidative stress. Loss of plasma glutathione could also have profound effects on the NO-dependent vasodilatory activity of RBCs, as GSH may facilitate export of SNOs from RBCs.6,34 Reactive oxygen species (eg, superoxide, O2−), which are also increased in preeclampsia, have been found to potentiate albumin S-nitrosylation,35 providing another possible mechanism for elevated SNOs. Overall, we favor the explanation that redox state influences the equilibria between thiols/nitrosothiols that convey NO bioactivity, rather than the view ascorbate, per se, regulates the amounts of free NO delivered to the vessel wall.Further investigation is needed to address the mechanistic basis and relevance of alterations in SNO-protein levels in disease and to identify therapeutic leads. It would be interesting to know if the preeclamptic state can be controlled through administration of NO or SNO or perhaps even thiols, and whether endogenous SNO-albumin or SNO-hemoglobin transduces the therapeutic effects of these compounds. Finally, ascorbate itself has been shown to improve endothelial dysfunction in atherosclerosis, hypercholesterolemia, and preeclampsia.36 If acute or chronic treatment with ascorbate were to produce a decrease in SNO-albumin commensurate with a fall in blood pressure, then a role for SNO-albumin in control of blood pressure and for ascorbate in modulating its bioactivity would be confirmed.The opinions expressed in this editorial are not necessarily those of the editors or of the American Heart Association.FootnotesCorrespondence to Jonathan S. Stamler, MD, Department of Medicine, Box 2612, Duke University Medical Center, Durham, NC 27710. Email [email protected] References 1 Stamler JS, Lamas S, Fang FC. Nitrosylation: the prototypic redox-based signaling mechanism. Cell. 2001; 106: 675–683.CrossrefMedlineGoogle Scholar2 Foster MW, McMahon TJ, Stamler JS. S-nitrosylation in health and disease. Trends Mol Med. 2003; 9: 160–168.CrossrefMedlineGoogle Scholar3 Liu L, Yan Y, Zeng M, Zhang J, Hanes MA, Ahearn G, McMahon TJ, Dickfeld T, Marshall HE, Que LG, Stamler JS. Essential roles of S-nitrosothiols in vascular homeostasis and endotoxic shock. Cell. 2004; 116: 617–628.CrossrefMedlineGoogle Scholar4 Gandley RE, Tyruin VA, Huang W, Arroyo A. S-nitroso-albumin-mediated relaxation is enhanced by ascorbate and copper: implications for impaired vascular function in preeclampsia. Hypertension. 2005; 45: 21–27.LinkGoogle Scholar5 Jia L, Bonaventura C, Bonaventura J, Stamler JS. S-Nitrosohemoglobin: a dynamic activity of blood involved in vascular control. Nature (London). 1996; 380: 221–226.CrossrefMedlineGoogle Scholar6 Pawloski JR, Hess DT, Stamler JS. Export by red blood cells of nitric oxide bioactivity. Nature. 2001; 409: 622–626.CrossrefMedlineGoogle Scholar7 Stamler JS, Jaraki O, Osborne J, Simon DI, Keaney J, Vita J, Singel D, Valeri CR, Loscalzo J. Nitric oxide circulates in mammalian plasma primarily as an S-nitroso adduct of serum albumin. Proc Natl Acad Sci U S A. 1992; 89: 7674–7677.CrossrefMedlineGoogle Scholar8 Nedospasov A, Rafikov R, Beda N, Nudler E. An autocatalytic mechanism of protein nitrosylation. Proc Natl Acad Sci U S A. 2000; 97: 13543–13548.CrossrefMedlineGoogle Scholar9 Rafikova O, Rafikov R, Nudler E. Catalysis of S-nitrosothiols formation by serum albumin: The mechanism and implication in vascular control. Proc Natl Acad Sci U S A. 2002; 99: 5913–5918.CrossrefMedlineGoogle Scholar10 Stubauer G, Giuffre A, Sarti P. Mechanism of S-nitrosothiol formation and degradation mediated by copper ions. J Biol Chem. 1999; 274: 28128–28133.CrossrefMedlineGoogle Scholar11 Massy ZA, Fumeron C, Borderie D, Tuppin P, Nguyen-Khoa T, Benoit MO, Jacquot C, Buisson C, Drueke TB, Ekindjian OG, Lacour B, Iliou MC. Increased plasma S-nitrosothiol concentrations predict cardiovascular outcomes among patients with end-stage renal disease: a prospective study. J Am Soc Nephrol. 2004; 15: 470–476.CrossrefMedlineGoogle Scholar12 Moriel P, Pereira IR, Bertolami MC, Abdalla DS. Is ceruloplasmin an important catalyst for S-nitrosothiol generation in hypercholesterolemia? Free Radic Biol Med. 2001; 30: 318–326.CrossrefMedlineGoogle Scholar13 Inoue K, Akaike T, Miyamoto Y, Okamoto T, Sawa T, Otagiri M, Suzuki S, Yoshimura T, Maeda H. Nitrosothiol formation catalyzed by ceruloplasmin. Implication for cytoprotective mechanism in vivo. J Biol Chem. 1999; 274: 27069–27075.CrossrefMedlineGoogle Scholar14 Holmes AJ, Williams DLH. Reaction of ascorbic acid with S-nitrosothiols: clear evidence for two distinct reaction pathways. J Chem Soc Perkin 2. 2000; 1639–1644.Google Scholar15 James PE, Lang D, Tufnell-Barret T, Milsom AB, Frenneaux MP. Vasorelaxation by red blood cells and impairment in diabetes: reduced nitric oxide and oxygen delivery by glycated hemoglobin. Circ Res. 2004; 94: 976–983.LinkGoogle Scholar16 Singel DJ, Stamler JS. Chemical physiology of blood flow regulation by red blood cells: the role of nitric oxide and S-nitrosohemoglobin. Ann Rev Physiol. 2005;67: in press.Google Scholar17 Pawloski JR, Stamler JS. Nitric oxide in RBCs. Transfusion. 2002; 42: 1603–1609.CrossrefMedlineGoogle Scholar18 Singel DJ, Stamler JS. Blood traffic control. Nature. 2004; 430: 297.CrossrefMedlineGoogle Scholar19 Sonveaux P, McMahon TJ, JSS, Dewhirst MW. (unpublished observation).Google Scholar20 Reiter CD, Wang X, Tanus-Santos JE, Hogg N, Cannon RO, 3rd, Schechter AN, Gladwin MT. Cell-free hemoglobin limits nitric oxide bioavailability in sickle-cell disease. Nat Med. 2002; 8: 1383–1389.CrossrefMedlineGoogle Scholar21 Tyurin VA, Liu SX, Tyurina YY, Sussman NB, Hubel CA, Roberts JM, Taylor RN, Kagan VE. Elevated levels of S-nitrosoalbumin in preeclampsia plasma. Circ Res. 2001; 88: 1210–1215.CrossrefMedlineGoogle Scholar22 Stamler JS. S-nitrosothiols in the blood: roles, amounts, and methods of analysis. Circ Res. 2004; 94: 414–417.LinkGoogle Scholar23 Tsikas D, Sandmann J, Gutzki FM, Stichtenoth DO, Frolich JC. Measurement of S-nitrosoalbumin by gas chromatography-mass spectrometry. II. Quantitative determination of S-nitrosoalbumin in human plasma using S-[15N]nitrosoalbumin as internal standard. J Chromatogr B Biomed Sci Appl. 1999; 726: 13–24.CrossrefMedlineGoogle Scholar24 Tsikas D, Sandmann J, Frolich JC. Measurement of S-nitrosoalbumin by gas chromatography–mass spectrometry. III. Quantitative determination in human plasma after specific conversion of the S-nitroso group to nitrite by cysteine and Cu(2+) via intermediate formation of S-nitrosocysteine and nitric oxide. J Chromatogr B Analyt Technol Biomed Life Sci. 2002; 772: 335–346.CrossrefMedlineGoogle Scholar25 Wang X, Tanus-Santos JE, Reiter CD, Dejam A, Shiva S, Smith RD, Hogg N, Gladwin MT. Biological activity of nitric oxide in the plasmatic compartment. Proc Natl Acad Sci U S A. 2004; 101: 11477–11482.CrossrefMedlineGoogle Scholar26 Bryan NS, Rassaf T, Maloney RE, Rodriguez CM, Saijo F, Rodriguez JR, Feelisch M. Cellular targets and mechanisms of nitros(yl)ation: an insight into their nature and kinetics in vivo. Proc Natl Acad Sci U S A. 2004; 101: 4308–4313.CrossrefMedlineGoogle Scholar27 Gladwin MT, Shelhamer JH, Schechter AN, Pease-Fye ME, Waclawiw MA, Panza JA, Ognibene FP, Cannon RO, 3rd. Role of circulating nitrite and S-nitrosohemoglobin in the regulation of regional blood flow in humans. Proc Natl Acad Sci U S A. 2000; 97: 11482–11487.CrossrefMedlineGoogle Scholar28 Lai TS, Hausladen A, Slaughter TF, Eu JP, Stamler JS, Greenberg CS. Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase. Biochemistry. 2001; 40: 4904–4910.CrossrefMedlineGoogle Scholar29 Rassaf T, Bryan NS, Maloney RE, Specian V, Kelm M, Kalyanaraman B, Rodriguez J, Feelisch M. NO adducts in mammalian red blood cells: too much or too little? Nat Med. 2003; 9: 481–482.CrossrefMedlineGoogle Scholar30 Kirima K, Tsuchiya K, Sei H, Hasegawa T, Shikishima M, Motobayashi Y, Morita K, Yoshizumi M, Tamaki T. Evaluation of systemic blood NO dynamics by EPR spectroscopy: HbNO as an endogenous index of NO. Am J Physiol Heart Circ Physiol. 2003; 285: H589–596.CrossrefMedlineGoogle Scholar31 Kagan VE, Tyurin VA, Borisenko GG, Fabisiak JP, Hubel CA, Ness RB, Gandley R, McLaughlin MK, Roberts JM. Mishandling of copper by albumin: role in redox-cycling and oxidative stress in preeclampsia plasma. Hypertens Pregnancy. 2001; 20: 221–241.CrossrefMedlineGoogle Scholar32 Gryzunov YA, Arroyo A, Vigne JL, Zhao Q, Tyurin VA, Hubel CA, Gandley RE, Vladimirov YA, Taylor RN, Kagan VE. Binding of fatty acids facilitates oxidation of cysteine-34 and converts copper-albumin complexes from antioxidants to prooxidants. Arch Biochem Biophys. 2003; 413: 53–66.CrossrefMedlineGoogle Scholar33 Raijmakers MT, Zusterzeel PL, Steegers EA, Hectors MP, Demacker PN, Peters WH. Plasma thiol status in preeclampsia. Obstet Gynecol. 2000; 95: 180–184.MedlineGoogle Scholar34 Lipton AJ, Johnson MA, Macdonald T, Lieberman MW, Gozal D, Gaston B. S-nitrosothiols signal the ventilatory response to hypoxia. Nature. 2001; 413: 171–174.CrossrefMedlineGoogle Scholar35 Ng ES, Jourd’heuil D, McCord JM, Hernandez D, Yasui M, Knight D, Kubes P. Enhanced S-nitroso-albumin formation from inhaled NO during ischemia/reperfusion. Circ Res. 2004; 94: 559–565.LinkGoogle Scholar36 May JM. How does ascorbic acid prevent endothelial dysfunction? Free Radic Biol Med. 2000; 28: 1421–1429.CrossrefMedlineGoogle Scholar Previous Back to top Next FiguresReferencesRelatedDetailsCited By Getsy P, Young A, Bates J, Baby S, Seckler J, Grossfield A, Hsieh Y, Lewis T, Jenkins M, Gaston B and Lewis S (2022) S-nitroso-L-cysteine stereoselectively blunts the adverse effects of morphine on breathing and arterial blood gas chemistry while promoting analgesia, Biomedicine & Pharmacotherapy, 10.1016/j.biopha.2022.113436, 153, (113436), Online publication date: 1-Sep-2022. Rezeck Nunes P, Cezar Pinheiro L, Zanetoni Martins L, Alan Dias-Junior C, Carolina Taveiros Palei A and Cristina Sandrim V (2022) A new look at the role of nitric oxide in preeclampsia: Protein S-nitrosylation, Pregnancy Hypertension, 10.1016/j.preghy.2022.05.008, 29, (14-20), Online publication date: 1-Aug-2022. Getsy P, Baby S, Gruber R, Gaston B, Lewis T, Grossfield A, Seckler J, Hsieh Y, Bates J and Lewis S (2022) S-Nitroso-L-Cysteine Stereoselectively Blunts the Deleterious Effects of Fentanyl on Breathing While Augmenting Antinociception in Freely-Moving Rats, Frontiers in Pharmacology, 10.3389/fphar.2022.892307, 13 Kulandavelu S, Dulce R, Murray C, Bellio M, Fritsch J, Kanashiro‐Takeuchi R, Arora H, Paulino E, Soetkamp D, Balkan W, Van Eyk J and Hare J (2022) S‐Nitrosoglutathione Reductase Deficiency Causes Aberrant Placental S‐Nitrosylation and Preeclampsia, Journal of the American Heart Association, 11:5, Online publication date: 1-Mar-2022. Zoanni B, Brioschi M, Mallia A, Gianazza E, Eligini S, Carini M, Aldini G and Banfi C (2021) Novel insights about albumin in cardiovascular diseases: Focus on heart failure, Mass Spectrometry Reviews, 10.1002/mas.21743 Oliver A, Guillory R, Flom K, Morath L, Kolesar T, Mostaed E, Sikora-Jasinska M, Drelich J and Goldman J (2020) Analysis of Vascular Inflammation against Bioresorbable Zn–Ag-Based Alloys, ACS Applied Bio Materials, 10.1021/acsabm.0c00740, 3:10, (6779-6789), Online publication date: 19-Oct-2020. Sakaki J, Melough M, Lee S, Pounis G and Chun O (2019) Polyphenol-Rich Diets in Cardiovascular Disease Prevention Analysis in Nutrition Research, 10.1016/B978-0-12-814556-2.00010-5, (259-298), . Ayoobi N, Jafarirad S, Haghighizadeh M and Jahanshahi A (2017) Protective Effect of Dark Chocolate on Cardiovascular Disease Factors and Body Composition in Type 2 Diabetes: A Parallel, Randomized, Clinical Trial, Iranian Red Crescent Medical Journal, 10.5812/ircmj.21644, 19:8 Yan J, Huang X, Zhu D and Lou Y (2017) Enhanced Aerobic Glycolysis by S-Nitrosoglutathione via HIF-1α Associated GLUT1/Aldolase A Axis in Human Endothelial Cells, Journal of Cellular Biochemistry, 10.1002/jcb.25911, 118:8, (2443-2453), Online publication date: 1-Aug-2017. Nagababu E (2016) Ferriheme catalyzes nitric oxide reaction with glutathione to form S-nitrosoglutathione: A novel mechanism for formation of S-nitrosothiols, Free Radical Biology and Medicine, 10.1016/j.freeradbiomed.2016.09.015, 101, (296-304), Online publication date: 1-Dec-2016. McCarthy C, Guillory R, Goldman J and Frost M (2016) Transition-Metal-Mediated Release of Nitric Oxide (NO) from S -Nitroso- N -acetyl- d -penicillamine (SNAP): Potential Applications for Endogenous Release of NO at the Surface of Stents Via Corrosion Products , ACS Applied Materials & Interfaces, 10.1021/acsami.6b00145, 8:16, (10128-10135), Online publication date: 27-Apr-2016. Corpas F, Chaki M, Begara-Morales J, Valderrama R, Sánchez-Calvo B and Barroso J (2016) Functional Implications of S-Nitrosothiols under Nitrooxidative Stress Induced by Abiotic Conditions Nitric Oxide and Signaling in Plants, 10.1016/bs.abr.2015.10.004, (79-96), . Bohlen H (2015) Nitric Oxide and the Cardiovascular System Comprehensive Physiology, 10.1002/cphy.c140052, (803-828) Rifkind J, Nagababu E, Dobrosielski D, Salgado M, Lima M, Ouyang P and Silber H (2014) The effect of intermittent pneumatic compression of legs on the levels of nitric oxide related species in blood and on arterial function in the arm, Nitric Oxide, 10.1016/j.niox.2014.06.007, 40, (117-122), Online publication date: 1-Aug-2014. Nagababu E and Rifkind J (2011) Routes for Formation of S-Nitrosothiols in Blood, Cell Biochemistry and Biophysics, 10.1007/s12013-011-9321-2, 67:2, (385-398), Online publication date: 1-Nov-2013. Roche C, Cassera M, Dantsker D, Hirsch R and Friedman J (2013) Generating S-Nitrosothiols from Hemoglobin, Journal of Biological Chemistry, 10.1074/jbc.M113.482679, 288:31, (22408-22425), Online publication date: 1-Aug-2013. Lima B, Forrester M, Hess D and Stamler J (2010) S-Nitrosylation in Cardiovascular Signaling, Circulation Research, 106:4, (633-646), Online publication date: 5-Mar-2010. Roche C and Friedman J (2010) NO reactions with sol–gel and solution phase samples of the ferric nitrite derivative of HbA, Nitric Oxide, 10.1016/j.niox.2009.11.003, 22:2, (180-190), Online publication date: 1-Feb-2010. Lippi G, Franchini M, Montagnana M, Favaloro E, Guidi G and Targher G (2008) Dark chocolate: consumption for pleasure or therapy?, Journal of Thrombosis and Thrombolysis, 10.1007/s11239-008-0273-3, 28:4, (482-488), Online publication date: 1-Nov-2009. Bohlen H, Zhou X, Unthank J, Miller S and Bills R (2009) Transfer of nitric oxide by blood from upstream to downstream resistance vessels causes microvascular dilation, American Journal of Physiology-Heart and Circulatory Physiology, 10.1152/ajpheart.00171.2009, 297:4, (H1337-H1346), Online publication date: 1-Oct-2009. Loke W, Hodgson J, Proudfoot J, McKinley A, Puddey I and Croft K (2008) Pure dietary flavonoids quercetin and (−)-epicatechin augment nitric oxide products and reduce endothelin-1 acutely in healthy men, The American Journal of Clinical Nutrition, 10.1093/ajcn/88.4.1018, 88:4, (1018-1025), Online publication date: 1-Oct-2008. Zhu J, Li S, Marshall Z and Whorton A (2008) A cystine-cysteine shuttle mediated by xCT facilitates cellular responses to S -nitrosoalbumin , American Journal of Physiology-Cell Physiology, 10.1152/ajpcell.00411.2007, 294:4, (C1012-C1020), Online publication date: 1-Apr-2008. Angelo M, Hausladen A, Singel D and Stamler J (2008) Interactions of NO with Hemoglobin: From Microbes to Man Globins and Other Nitric Oxide-Reactive Proteins, Part A, 10.1016/S0076-6879(08)36008-X, (131-168), . Balzer J, Rassaf T and Kelm M (2007) Reductase activity of polyphenols?: A commentary on “Red wine-dependent reduction of nitrite to nitric oxide in the stomach”, Free Radical Biology and Medicine, 10.1016/j.freeradbiomed.2007.07.018, 43:9, (1226-1228), Online publication date: 1-Nov-2007. Marsden P (2007) Low-molecular-weight S-nitrosothiols and blood vessel injury, Journal of Clinical Investigation, 10.1172/JCI33136, 117:9, (2377-2380), Online publication date: 4-Sep-2007. Shumaev K, Gubkin A, Gubkina S, Gudkov L, Lakomkin V, Topunov A, Vanin A and Ruuge E (2007) Interaction between albumin-bound dinitrosyl iron complexes and reactive oxygen species, Biophysics, 10.1134/S0006350907030141, 52:3, (336-339), Online publication date: 1-Jun-2007. Lu D, Nadas J, Zhang G, Johnson W, Zweier J, Cardounel A, Villamena F and Wang P (2007) 4-Aryl-1,3,2-oxathiazolylium-5-olates as pH-Controlled NO-Donors: The Next Generation of S -Nitrosothiols , Journal of the American Chemical Society, 10.1021/ja0682226, 129:17, (5503-5514), Online publication date: 1-May-2007. Li S and Whorton A (2007) Functional characterization of two S -nitroso- l -cysteine transporters, which mediate movement of NO equivalents into vascular cells , American Journal of Physiology-Cell Physiology, 10.1152/ajpcell.00382.2006, 292:4, (C1263-C1271), Online publication date: 1-Apr-2007. Hausladen A, Rafikov R, Angelo M, Singel D, Nudler E and Stamler J (2007) Assessment of nitric oxide signals by triiodide chemiluminescence, Proceedings of the National Academy of Sciences, 10.1073/pnas.0611191104, 104:7, (2157-2162), Online publication date: 13-Feb-2007. Varonka M and Warren T (2007) S-nitrosothiol and nitric oxide reactivity at β-diketiminato zinc thiolates, Inorganica Chimica Acta, 10.1016/j.ica.2006.07.049, 360:1, (317-328), Online publication date: 1-Jan-2007. Balzer J, Heiss C, Schroeter H, Brouzos P, Kleinbongard P, Matern S, Lauer T, Rassaf T and Kelm M (2006) Flavanols and Cardiovascular Health: Effects on the circulating NO Pool in Humans, Journal of Cardiovascular Pharmacology, 10.1097/00005344-200606001-00006, 47:Supplement 2, (S122-S127), Online publication date: 1-Jun-2006. Heiss C, Lauer T, Dejam A, Kleinbongard P, Hamada S, Rassaf T, Matern S, Feelisch M and Kelm M (2006) Plasma Nitroso Compounds Are Decreased in Patients With Endothelial Dysfunction, Journal of the American College of Cardiology, 10.1016/j.jacc.2005.06.089, 47:3, (573-579), Online publication date: 1-Feb-2006. Lewis S, Owen J and Bates J (2006) S-nitrosocysteine elicits hemodynamic responses similar to those of the Bezold–Jarisch reflex via activation of stereoselective recognition sites, European Journal of Pharmacology, 10.1016/j.ejphar.2005.11.027, 531:1-3, (254-258), Online publication date: 1-Feb-2006. Orie N, Vallance P, Jones D and Moore K (2005) S -nitroso-albumin carries a thiol-labile pool of nitric oxide, which causes venodilation in the rat , American Journal of Physiology-Heart and Circulatory Physiology, 10.1152/ajpheart.01014.2004, 289:2, (H916-H923), Online publication date: 1-Aug-2005. Miller W, Brosnan M, Graham D, Nicol C, Morecroft I, Channon K, Danilov S, Reynolds P, Baker A and Dominiczak A (2005) Targeting endothelial cells with adenovirus expressing nitric oxide synthase prevents elevation of blood pressure in stroke-prone spontaneously hypertensive rats, Molecular Therapy, 10.1016/j.ymthe.2005.02.025, 12:2, (321-327), Online publication date: 1-Aug-2005. Rogers S, Khalatbari A, Gapper P, Frenneaux M and James P (2005) Detection of Human Red Blood Cell-bound Nitric Oxide, Journal of Biological Chemistry, 10.1074/jbc.M501179200, 280:29, (26720-26728), Online publication date: 1-Jul-2005. January 2005Vol 45, Issue 1 Advertisement Article InformationMetrics https://doi.org/10.1161/01.HYP.0000150160.41992.71PMID: 15557388 Originally publishedNovember 22, 2004 PDF download Advertisement" @default.
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