S-Nitrosothiol measurements in biological systems

Gow, Andrew J.; Doctor, Allan; Mannick, Joan B.; Gaston, Benjamin

doi:10.1016/j.jchromb.2007.01.052

Cited by 109 publications

(121 citation statements)

References 50 publications

Supporting

Mentioning

118

Contrasting

Order By: Relevance

“…Curiously, a recent report described activation of MMP-9 by selected concentrations of SPER-NO, which appears to counter our observations, although the mechanism of activation was not addressed (28). First, only high concentrations of an exceptionally reactive S-nitrosothiol, CSNO (29), were found to weakly activate proMMP9, consistent with earlier findings (4), but the biological significance of this is questionable because biological concentrations of SNO are in the nanomolar range (30). Second, although several diverse NO donors and S-nitro-sothiols are similarly capable of inducing S-nitrosylation within a peptide that represents the Cys-containing prodomain region of proMMP-9, the fact that most of these agents cannot activate proMMP-9 would suggest that S-nitrosylation may not be responsible for MMP-9 activation by CSNO or by other RNS (4,9).…”

Section: Discussionsupporting

confidence: 58%

Nitric Oxide Regulation of MMP-9 Activation and Its Relationship to Modifications of the Cysteine Switch

et al. 2008

View full text Add to dashboard Cite

Matrix metalloproteases (MMPs) are Zn-containing endopeptidases involved in the degradation of extracellular matrix components and are typically secreted in a latent (pro-MMP) form and activated either by proteolytic or oxidative disruption of a conserved cysteine switch. Several recent studies have suggested that nitric oxide (NO) can contribute to the activation of MMPs, but the mechanisms involved are incompletely understood. We investigated the ability of NO to regulate the activation of (pro)MMP-9 using a variety of NO-donor compounds and characterized modifications of the cysteine switch using a synthetic peptide (PRCGVPDLGR) representing the cysteine switch domain of MMP-9. Among the NO-donors used, only S-nitrosocysteine (SNOC) was found to be capable of modest activation of proMMP-9, but S-nitrosoglutathione (GSNO) or the NONOates, DEA-NO, SPER-NO, or DETA-NO, were ineffective. In fact, high concentrations of DETA-NO were found to inhibit MMP-9 activity, presumably by direct interaction with the active-site Zn 2+ . Analysis of chemical modifications within the Cys-containing peptide, PRCGVPDLGR, revealed rapid and transient S-nitrosylation by SNOC and GSNO, and formation of mixed disulfides and dimerized peptide as major final products. Similarly, NONOates induced transient S-nitrosylation and primarily peptide dimerization. Coordination of the peptide Cys with a synthetic Zn 2+ complex, to more closely mimic the structure of the active site in proMMP-9, reduced peptide nitrosylation and oxidation by NONOates, but enhanced peptide nitrosylation by SNOC and GSNO. Collectively, our results demonstrate that NO is incapable of directly activating proMMP-9 and that S-nitrosylation of MMP-9 propeptide by NO-donors is unrelated to their ability to regulate MMP-9 activity.Matrix metalloproteinases (MMPs) comprise a family of zinc-containing endopeptidases and play important roles in development, inflammation, tissue injury and repair, and tumor biology (1,2). The MMP family consists of at least 26 members that share several structural characteristics including a highly conserved Cys-containing pro-peptide domain and a catalytic domain containing three His residues bound to a Zn(II) metal ion. MMPs are typically expressed at low levels in normal tissues, but in conditions of inflammation and/or tissue injury, MMP expression is generally increased by the action of pro-inflammatory † This work was supported by NIH research grants R01 HL074295 and R01 HL068865 (to A.vdV.), T32 ES07122 (training fellowship to S.M.M.), and P20 RR16462 (to the Vermont Genetics Network). Several recent studies have suggested that NO contributes to the activation of MMPs or related metalloproteinases by S-nitrosylation (often also referred to as S-nitrosation) of the pro-domain Cys residue. For example, MMP-9 activation in vivo was found to be associated with increased NOS activity, and the nitrosothiol S-nitrosocysteine is capable of activating pro-MMP-9 by a mechanism that appears to involve transnitrosylation (4,11). Similar...

show abstract

Section: Discussionsupporting

confidence: 58%

Nitric Oxide Regulation of MMP-9 Activation and Its Relationship to Modifications of the Cysteine Switch

et al. 2008

View full text Add to dashboard Cite

show abstract

“…At present, most techniques to measure blood RSNOs require the preparation of plasma by centrifugation and subsequent treatment of the plasma samples with various reagents to liberate NO (6 ). During these processes, exposure to ambient light is difficult to completely eliminate, and most methods reported to date do not take any precautions in this regard.…”

Section: Discussionmentioning

confidence: 99%

Photoinstability of S-Nitrosothiols during Sampling of Whole Blood: A Likely Source of Error and Variability in S-Nitrosothiol Measurements

Zhang

Wang

et al. 2008

Clinical Chemistry

View full text Add to dashboard Cite

BACKGROUND:The determination of reference intervals for the concentration of total S-nitrosothiols (RSNOs) in blood is a highly controversial topic, likely because of the inherent instability of these species. Most currently available techniques to quantify RSNOs in blood require considerable sample handling and multiple pretreatment steps during which light exposure is difficult to completely eliminate. We investigated the effect of brief light exposure on the stability of RSNO species in blood during the initial sampling process.

show abstract

“…To distinguish RSNO from RNNO, mercuric chloride can be used to cleave RSNO to form nitrite, but leaving RNNO intact, which is known as the Saville reaction (12). Sensitivity of the original colorimetric method for the Griess assay was ϳ0.5 M for S-nitrosothiols, which is not low enough for detecting biological levels (33). However, combining the Griess assay with HPLC, flow injection analysis, and microgas analysis system, the detection range has been improved significantly and now these analyses are routinely applied to measuring biological sample.…”

Section: No and H 2 S Measurementsmentioning

confidence: 99%

Working with nitric oxide and hydrogen sulfide in biological systems

Yuan

Patel

Kevil

2015

American Journal of Physiology-Lung Cellular and Molecular Phys

View full text Add to dashboard Cite

(H 2S) are gasotransmitter molecules important in numerous physiological and pathological processes. Although these molecules were first known as environmental toxicants, it is now evident that that they are intricately involved in diverse cellular functions with impact on numerous physiological and pathogenic processes. NO and H 2S share some common characteristics but also have unique chemical properties that suggest potential complementary interactions between the two in affecting cellular biochemistry and metabolism. Central among these is the interactions between NO, H 2S, and thiols that constitute new ways to regulate protein function, signaling, and cellular responses. In this review, we discuss fundamental biochemical principals, molecular functions, measurement methods, and the pathophysiological relevance of NO and H 2S. thiol; oxidation; redox; pulmonary; cardiovascular HISTORICALLY CONSIDERED ONLY as industrial pollutants, nitric oxide (NO) and hydrogen sulfide (H 2 S) are now appreciated as two key physiologically produced signaling molecules that control multiple cellular functions. Appreciation that dysfunction in how these solvated gases affect these functions, through either deficient formation or downstream reactivity, has opened up new therapeutic avenues for a host of diseases in all major organ systems including the lung. Our understanding of NO homeostasis mechanisms are relatively advanced compared with H 2 S, primarily because of the latter's discovery as a biologically relevant entity being postdated by a decade or more compared with NO. Although they are chemically distinct, there are intriguing parallel mechanisms/concepts in NO and H 2 S biology that include overlapping functions, technical challenges in how each of these gases are measured in biological milieu, appreciation of the mechanisms and factors that modulate how metabolism of each of these is regulated, and therapeutic potential for either inhibiting or repleting NO or H 2 S. In this article, and within the framework outlined above, we provide a general overview of NO and H 2 S biology. Nitric Oxide Formation: Enzymatic and Nonenzymatic SourcesEnzymatic sources. Nitric oxide is synthesized by one of three different isoforms of nitric oxide synthase (NOS) that differ in enzymatic activity, in how they are regulated (transcriptional, translational, and posttranslational mechanisms), and in how they are expressed/compartmentalized in tissues as well as the subcellular level. These are called NOS I, II, and III, corresponding to the inducible (iNOS), neuronal (nNOS), and endothelial (eNOS) isoforms, typically with high, mid, and low activities, respectively. In the systemic and pulmonary vasculature, eNOS plays a key role in controlling blood flow and maintaining an antithrombotic and anti-inflammatory luminal surface. On the other hand, iNOS is induced by inflammatory stimuli in leukocytes, airway epithelial cells, and alveolar macrophages to mediate pathogen killing. However, production of NO at higher concentrations in ...

show abstract

S-Nitrosothiol measurements in biological systems

Cited by 109 publications

References 50 publications

Nitric Oxide Regulation of MMP-9 Activation and Its Relationship to Modifications of the Cysteine Switch

Nitric Oxide Regulation of MMP-9 Activation and Its Relationship to Modifications of the Cysteine Switch

Photoinstability of S-Nitrosothiols during Sampling of Whole Blood: A Likely Source of Error and Variability in S-Nitrosothiol Measurements

Working with nitric oxide and hydrogen sulfide in biological systems

Contact Info

Product

Resources

About