Detection of S-nitrosothiols in biological fluids: A comparison among the most widely applied methodologies

Giustarini, Daniela; Milzani, Aldo; Dalle‐Donne, Isabella; Rossi, Ranieri

doi:10.1016/j.jchromb.2006.09.031

Cited by 111 publications

(131 citation statements)

References 131 publications

(180 reference statements)

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“…A dwell time of 100 ms was used for each mass transition initial and recent reports, Rudolph et al discussed in their recent paper that ''We and others have detected nitro-oleate in rodents and humans in other instances, as well as metabolites reported herein'' [14]. Unlike other nitrosated and nitrated biomolecules such as S-nitrosothiols [21] and 3-nitrotyrosine [22,23], artifactual formation of nitro-fatty acids is unlikely [13]. We can therefore only hypothesize that mainly analytical factors, such as lack of specificity of the LC-MS/MS method used, have resulted in severe artefacts.…”

Section: Discussionmentioning

confidence: 99%

Nitro‐fatty Acids Occur in Human Plasma in the Picomolar Range: a Targeted Nitro‐lipidomics GC–MS/MS Study

Tsikas

Zoerner

Mitschke

et al. 2009

Lipids

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First studies on the occurrence of nitrated fatty acids in plasma of healthy subjects revealed basal concentrations of 600 nM for free/nonesterified nitro-oleic acid (NO(2)-OA) as measured by liquid chromatography tandem mass spectrometry (LC-MS/MS). We recently showed by a gas chromatography tandem mass spectrometry (GC-MS/MS) method the physiological occurrence of two isomers, i.e., 9-NO(2)-OA and 10-NO(2)-OA, at mean basal plasma concentrations of 880 and 940 pM, respectively. In consideration of this large discrepancy we modified our originally reported method by replacing solid-phase extraction (SPE) by solvent extraction with ethyl acetate and by omitting the high-performance liquid chromatography (HPLC) step for a more direct detection and with the potential for lipidomics studies. Intra-assay imprecision and accuracy of the modified method in human plasma were 1-34% and 91-221%, respectively, for added NO(2)-OA concentrations in the range 0-3,000 pM. This method provided basal plasma concentrations of 306 +/- 44 pM for 9-NO(2)-OA and 316 +/- 33 pM for 10-NO(2)-OA in 15 healthy subjects. Nitro-arachidonic acid and nitro-linolenic acid were not detectable in the plasma samples. In summary, our studies show 9-NO(2)-OA and 10-NO(2)-OA as endogenous nitrated fatty acids in human plasma in the pM range; HPLC is recommendable as a sample clean-up step for reliable quantification of nitro-oleic acids by GC-MS/MS.

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Section: Discussionmentioning

confidence: 99%

Nitro‐fatty Acids Occur in Human Plasma in the Picomolar Range: a Targeted Nitro‐lipidomics GC–MS/MS Study

Tsikas

Zoerner

Mitschke

et al. 2009

Lipids

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“…In order to investigate the relation between the protein S-nitrosylation level of blood and RBCs membrane elasticity change, this paper complete the semi quantitative measurements of Snitrosothiol content of blood based on fluorescent spectrometry during in vitro storage [35,36]. The measurement method can be found in literature [35].…”

Section: Resultsmentioning

confidence: 99%

Study of in vitro RBCs membrane elasticity with AOD scanning optical tweezers

Song¹,

Liu²,

Zhang³

et al. 2016

Biomed. Opt. Express

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Abstract:The elasticity of red cell membrane is a critical physiological index for the activity of RBC. Study of the inherent mechanism for RBCs membrane elasticity transformation is attention-getting all along. This paper proposes an optimized measurement method of erythrocytes membrane shear modulus incorporating acousto-optic deflector (AOD) scanning optical tweezers system. By use of this method, both membrane shear moduli and sizes of RBCs with different in vitro times were determined. The experimental results reveal that the RBCs membrane elasticity and size decline with in vitro time extension. In addition, semi quantitative measurements of S-nitrosothiol content in blood using fluorescent spectrometry during in vitro storage show that RBCs membrane elasticity change is positively associated with the S-nitrosylation level of blood. The analysis considered that the diminished activity of the nitric oxide synthase makes the S-nitrosylation of in vitro blood weaker gradually. The main reason for worse elasticity of the in vitro RBCs is that S-nitrosylation effect of spectrin fades. These results will provide a guideline for further study of in vitro cells activity and other clinical applications. References and links1. N. Hamasaki and M. Yamamoto, "Red blood cell function and blood storage," Vox Sang. 79(4), 191-197 (2000). 2. M. Whirter, J. Liam, H. Noguchi, and G. Gompper, "Ordering and arrangement of deformed red blood cells in flow through microcapillaries," New J. Phys. 14(8), 6709-6717 (2012). 3. M. Musielak, "Red blood cell-deformability measurement: review of techniques," Clin. Hemorheol. Microcirc.42(1), 47-64 (2009). 4. S. Svetina, G. Kokot, T. S. Kebe, B. Žekš, and R. E. Waugh, "A novel strain energy relationship for red blood cell membrane skeleton based on spectrin stiffness and its application to micropipette deformation," Biomech. Model. Mechanobiol. 15(3), 745-758 (2016). 5. G. J. Streekstra, J. G. G. Dobbe, and A. G. Hoekstra, "Quantification of the fraction poorly deformable red blood cells using ektacytometry," Opt. Express 18(13), 14173-14182 (2010). 6. L. Dintenfass, "Internal viscosity of the red cell and a blood viscosity equation," Nature 219(5157), 956-958 (1968). 649-652 (1986). 37. Z. Peng, X. Li, I. V. Pivkin, M. Dao, G. E. Karniadakis, and S. Suresh, "Lipid bilayer and cytoskeletal interactions in a red blood cell," Proc. Natl. Acad. Sci. U.S.A. 110(33), 13356-13361 (2013). 38. M. Grau, P. Friederichs, S. Krehan, C. Koliamitra, F. Suhr, and W. Bloch, "Decrease in red blood cell deformability is associated with a reduction in RBC-NOS activation during storage," Clin. Hemorheol. Microcirc. 60(2), 215-229 (2015).

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“…Its beneficial effects in the vasculature extend to cardiac left ventricular function and systemic vasodilation (Rassaf et al, 2002), and preeclampsia (Lees et al, 1996) (Table 1). Although with some discrepancies related to the analytical method used (Giustarini et al, 2006;Bramanti et al, 2009), GSNO was found at nanoto low micromolar concentrations in extracellular fluids and tissues (Gaston et al, 1993;Kluge et al, 1997;Giustarini et al, 2006), and due to its nature of endogenous compound and its important role in NO signaling and S-nitrosation, it has been considered an attractive candidate for therapeutic applications (Snyder et al, 2002;Corti et al, 2014). However, despite its powerful antiplatelet activity, vasodilator effects, antimicrobial and antithrombotic effects, this molecule is not yet present in any pharmaceutical composition for the treatment of vascular diseases.…”

Section: S-nitrosoglutathione (Gsno): the Main Endogenous No Donormentioning

confidence: 99%

Regulation of protein function by S-nitrosation and S-glutathionylation: processes and targets in cardiovascular pathophysiology

Belcastro

Gaucher

Corti

et al. 2017

Biological Chemistry

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Decades of chemical, biochemical and pathophysiological research have established the relevance of post-translational protein modifications induced by processes related to oxidative stress, with critical reflections on cellular signal transduction pathways. A great deal of the so-called 'redox regulation' of cell function is in fact mediated through reactions promoted by reactive oxygen and nitrogen species on more or less specific aminoacid residues in proteins, at various levels within the cell machinery. Modifications involving cysteine residues have received most attention, due to the critical roles they play in determining the structure/function correlates in proteins. The peculiar reactivity of these residues results in two major classes of modifications, with incorporation of NO moieties (S-nitrosation, leading to formation of protein S-nitrosothiols) or binding of low molecular weight thiols (S-thionylation, i.e . in particular S-glutathionylation, S-cysteinylglycinylation and S-cysteinylation).A wide array of proteins have been thus analyzed in detail as far as their susceptibility to either modification or both, and the resulting functional changes have been described in a number of experimental settings. The present review aims to provide an update of available knowledge in the field, with a special focus on the respective (sometimes competing and antagonistic) roles played by protein S-nitrosations and S-thionylations in biochemical and cellular processes specifically pertaining to pathogenesis of cardiovascular diseases.

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Detection of S-nitrosothiols in biological fluids: A comparison among the most widely applied methodologies

Cited by 111 publications

References 131 publications

Nitro‐fatty Acids Occur in Human Plasma in the Picomolar Range: a Targeted Nitro‐lipidomics GC–MS/MS Study

Nitro‐fatty Acids Occur in Human Plasma in the Picomolar Range: a Targeted Nitro‐lipidomics GC–MS/MS Study

Study of in vitro RBCs membrane elasticity with AOD scanning optical tweezers

Regulation of protein function by S-nitrosation and S-glutathionylation: processes and targets in cardiovascular pathophysiology

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