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• W2000942575 abstract "EDITORIAL FOCUSNO and nitrosothiols: spatial confinement and free diffusionJack R. Lancaster Jr., and Benjamin GastonJack R. Lancaster Jr., and Benjamin GastonPublished Online:01 Sep 2004https://doi.org/10.1152/ajplung.00151.2004MoreSectionsPDF (19 KB)Download PDF ToolsExport citationAdd to favoritesGet permissionsTrack citations ShareShare onFacebookTwitterLinkedInWeChat nitric oxide (NO, nitrogen monoxide) affects a multitude of physiological systems. It can react with metal centers, oxygen, and superoxide in tissues. The report from Zhang and Hogg, one of the current articles in focus (Ref. 13, see p. L467 in this issue), confirms that one cellular target of oxidized form(s) of NO is thiol groups (RSH) (13). Nitrosothiols (RSNO) are formed from peptide or protein RSH (cysteine) residues in the presence of an electron acceptor such as copper (i.e., in ceruloplasmin), iron, or oxygen (5, 11, 13). Recent reports suggest that different cysteine thiols in proteins exhibit different extents of nitrosation (4, 9, 11). Here, Zhang and Hogg confirm previous data (3) that cellular RSNOs are formed under physiological conditions and that this synthesis is increased in association with nitric oxide synthase (NOS) activation. However, the role of RSNO formation in cell signaling remains controversial in part because 1) the mechanisms and kinetics of cellular S-NO bond formation and cleavage in situ are not well defined; and 2) assaying for specific cellular RSNO remains cumbersome, complex, and controversial. For this reason, we propose criteria (Table 1) to help to guide research regarding whether a bioactivity results from the S-nitrosation (or denitrosation) of a specific protein.Zhang and Hogg (13) describe important properties of the formation of RSNO inside and outside the murine macrophage cell line, RAW 264.7, pretreated with lipopolysaccharide (LPS). They show that LPS treatment increases cytosolic and extracellular RSNO and that this increase is substantially inhibited in the presence of a NOS inhibitor. Furthermore, addition of nitrite to cells in the absence of endogenous NO formation does not increase cytosolic RSNO formation. This indicates that the RSNOs are not formed from nitrite in RAW 264.7 cell cytosol.When Zhang and Hogg (13) stopped NO synthesis with a NOS inhibitor, the intracellular RSNO levels declined only slowly, by 50% after 3 h. This result demonstrates that certain protein thiols denitrosate relatively slowly. However, specific protein thiols that may be functionally regulated by nitrosation may well turn over (both nitrosation and denitrosation) rapidly and would not be detected by the methods applied here.Zhang and Hogg (13) also found that addition of extracellular oxyhemoglobin for 2 h halved the amount of LPS-induced intracellular RSNO protein in cytosolic extracts. Hemoglobin is an efficient NO scavenger that will increase the rate at which NO is lost from the hemoglobin-free side of a membrane (7, 8, 12). It does this by decreasing the probability (to virtually 0) that a molecule introduced to the nonhemoglobin side will, after it diffuses to the hemoglobin side, diffuse back. Therefore, the difference in intracellular RSNO concentration in the presence of extracellular hemoglobin is accounted for by loss of NO molecules that diffused out, but not back (7, 8). It is proposed (Lancaster) that this observation demonstrates that all RSNO formation must be accounted for by NO that diffuses out and back across the cell membrane because this diffusion is more rapid than any NO oxidation process that would form RSNO; thus, rapid diffusion suggests that RSNO formation is not spatially constrained (2) by the location of NOS isoforms, electron acceptors, or target thiols. Indeed, this accounts for data in hepatocytes (2, 10).On the other hand, it can be argued (Gaston) that RSNO synthesis may be spatially constrained in that 1) it is most likely to occur in membranes and organelles (9), which were not analyzed in the cytosolic extracts prepared by Zhang and Hogg (13); 2) the establishment of a transmembrane pressure/concentration gradient, and consequent increased net transmembrane flow, does not demonstrate that NO must leave and return to react, particularly in the context of rapid intracellular reactions with superoxide, metal-containing proteins, and redox-active amino acid groups; and 3) in any event, spatial constraint of RSNO formation does not necessarily imply spatial confinement of NO. As is the case with all reactions in biology, spatial constraint must not violate the laws of diffusion, but the two principles are not necessarily mutually exclusive: for example, NO diffusing out of the cell can be “spatially constrained” by hemoglobin not to diffuse back. Interestingly, inducible NOS upregulation in the lung, associated with a general increase in nitrotyrosine immunostaining, is associated with localized decreases in RSNO immunostaining, suggesting that RSNO formation is localized and/or metabolically regulated (1). We propose that this differential localization of reactivity might be called “spatial confinement” as opposed to “spatial constraint.” Certainly, an important finding of Zhang and Hogg is that NO diffusion affects cellular RSNO concentrations and that RSNO metabolism is best studied in the physiological context in which the cell would find itself in vivo. For example, cellular RSNO metabolism might be expected to be different in a cell exposed to continuous blood flow than in a cell in the center of an abscess.The cytosolic RSNO in lysates identified by Zhang and Hogg (13) were primarily composed of high-molecular-weight species (>3 kDa). It would have been of interest to know which specific cytosolic proteins were S-nitrosated in the RAW 264.7 cells following LPS exposure. One of us (Gaston, unpublished observations) has found that when assaying protein RSNOs in biological samples, several variables can affect the signal readout; these include preassay protein preparation, position and reactivity of the RSNO bond in the protein, autocapture of NO by metal centers, and other competing reactions of NO. Thus standard curves using S-nitrosoglutathione or S-nitrosated albumin may under- or overestimate the concentration of specific RSNO proteins immunoprecipitated or otherwise isolated from cells or tissues, and quantitative validation by three different, independent assays is ideal at this stage of the science. In this regard, it is of interest that Zhang and Hogg report cytosolic RSNO proteins in greater abundance and having greater stability in RAW 264.7 cells than have previously been reported in other cells (4, 9, 11). Additional work will be required to carefully dissect the specific proteins involved using immunoprecipitation, site-directed mutagenesis, and proteomic techniques (4, 6, 9).So, three major take-home messages from the work of Zhang and Hogg (13) are that 1) confirming previous studies, protein RSNOs are formed in macrophage cell line cytosolic extracts following LPS stimulation; 2) these protein RSNOs can be quite stable, despite the cytosolic “reducing environment”; and 3) intracellular RSNO metabolism needs to be studied in the physiological context because of the powerful effects of tissue/environmental reactive species, such as hemoglobin, on NO diffusion. It will be of great interest to see 1) if their results are relevant to specific “sequestered” cell compartments; 2) which specific proteins are S-nitrosated in response to LPS stimulation; and 3) what the specific mechanism(s) might be for this S-nitrosation. Table 1. Proposed criteria to establish that a specific bioacivity is associated with S-nitrosation or denitrosation of a specific proteinThe altered bioactivity of the target protein is associated with increased (or decreased) activity of a nitric oxide synthase (NOS) isoform.S-Nitrosation of the target protein isolated from cells (and/or in situ) following NOS activation can be demonstrated by more than one independent assay (ideally 3 assays). In addition, the extent of nitrosation from endogenous nitric oxide formation is sufficient in magnitude to affect the activity of the protein, and nitrosation/denitrosation occurs rapidly enough to account for regulated changes in activity.Mutation of a specific cysteine in the target protein results in 1) loss of the NOS-responsive bioactivity and 2) inability to identify the S-nitrosated protein following NOS activation.In association with termination of the bioactivity, loss of the cellular protein S-nitrosation is demonstrated.Alteration of the function of the purified protein can be demonstrated in association with S-nitrosation under conditions relevant to the protein's cellular environment (i.e., in the presence of a nitrogen oxide at concentrations measured in the specifically relevant tissue or cell compartment at the appropriate Po2, pH, etc.).Pharmacological experiments demonstrate that cGMP is not exclusively involved in mediating the bioactivity.Pharmacological experiments suggest that a thiol modification is involved (i.e., the altered bioactivity is blocked by pretreatment with N-ethylmaleimide and/or reversed by excess DTT).Pharmacological modifications of specific SNO metabolic enzymes relevant to the putative signaling process (such as γ-glutamyl transpeptidase or glutathione-dependent formaldehyde dehydrogenase) appropriately alter the bioactivity, and/or the bioactivity is caused by S-nitroso-l-cysteine-containing compounds but not S-nitroso-d-cysteine-containing compounds.REFERENCES1 Atochina EN, Beers MF, Hawgood S, Poulain F, Davis C, Fusaro T, and Gow AJ. Surfactant protein-D, a mediator of innate lung immunity, alters the products of nitric oxide metabolism. Am J Respir Cell Mol Biol 30: 271–279, 2004.Crossref | PubMed | ISI | Google Scholar2 Barouch LA, Harrison RW, Skaf MW, Rosas GO, Cappola TP, Kobeissi ZA, Hobai IA, Lemmon CA, Burnett AL, O'Rourke B, Rodriguez ER, Huang PL, Lima JA, Berkowitz DE, and Hare JM. Nitric oxide regulates the heart by spatial confinement of nitric oxide synthase isoforms. Nature 416: 337–339, 2002.Crossref | PubMed | ISI | Google Scholar3 Gow A, Chen Q, Hess D, Day B, Ischiropoulos H, and Stamler J. Basal and stimulated protein S-nitrosylation in multiple cell types and tissues. J Biol Chem 277: 9637–9640, 2002.Crossref | PubMed | ISI | Google Scholar4 Haendeler J, Hoffmann J, Tischler V, Berk B, Zeiher AM, and Dimmler S. Redox regulatory and anti-apoptotic function of thioredoxin depends on S-nitrosylation at cysteine 69. Nat Cell Biol 4: 743–749, 2002.Crossref | PubMed | ISI | Google Scholar5 Inoue K, Akaike T, Miyamoto Y, Okamoto T, Sawa T, Otagiri M, Suzuki S, Yoshimura T, and Maeda H. Nitrosothiol formation catalyzed by ceruloplasmin. Implication for cytoprotective mechanism in vivo. J Biol Chem 274: 27069–27075, 1999.Crossref | PubMed | ISI | Google Scholar6 Jaffrey SR, Erdjument-Bromage H, Ferris CD, Temps P, and Snyder SH. Protein S-nitrosylation: a physiological signal for neuronal nitric oxide. Nat Cell Biol 3: 193–198, 2001.Crossref | PubMed | ISI | Google Scholar7 Lancaster JR Jr. Diffusion of free nitric oxide. Methods Enzymol 268: 31–50, 1996.Crossref | PubMed | ISI | Google Scholar8 Lancaster JR Jr. The physical properties of nitric oxide. Determinants of the dynamics of NO in tissue. In: Nitric Oxide: Biology and Pathobiology, edited by Ignarro LJ. San Diego, CA: Academic, 2000, p. 209–224.Google Scholar9 Mannick J, Schonhoff C, Papeta N, Ghafourifar P, Szibor M, Fang K, and Gaston B. S-nitrosylation of mitochondrial caspases. J Cell Biol 154: 1111–1116, 2001.Crossref | PubMed | ISI | Google Scholar10 Stadler J, Bergonia HA, Di Silvio M, Sweetland MA, Billiar TR, Simmons RL, and Lancaster JR Jr. Nonheme iron-nitrosyl complex formation in rat hepatocytes: detection by electron paramagnetic resonance spectroscopy. Arch Biochem Biophys 302: 4–11, 1993.Crossref | PubMed | ISI | Google Scholar11 Stamler JS, Lamas S, and Fang FC. Nitrosylation, the prototypic redox-based signaling mechanism. Cell 106: 675–683, 2001.Crossref | PubMed | ISI | Google Scholar12 Thomas D, Liu X, Kantrow S, and Lancaster JR Jr. The biological lifetime of nitric oxide: implications for the perivascular dynamics of NO and O2. Proc Natl Acad Sci USA 98: 355–360, 2001.Crossref | PubMed | ISI | Google Scholar13 Zhang Y and Hogg N. Formation and stability of S-nitrosothiols in RAW 264.7 cells. Am J Physiol Lung Cell Mol Physiol 287: L467–L474, 2004.Link | ISI | Google ScholarAUTHOR NOTESAddress for reprint requests and other correspondence: B. Gaston, Univ. of Virginia School of Medicine, Pediatric Respiratory Medicine, PO Box 800386, Charlottesville, VA 22908 (E-mail: [email protected]) Download PDF Previous Back to Top Next FiguresReferencesRelatedInformationCited ByS-nitrosothiols signaling in cystic fibrosis airways1 December 2021 | Journal of Biosciences, Vol. 46, No. 4Influence of hemoglobin and albumin on the NO donation effect of tetranitrosyl iron complex with thiosulfateNitric Oxide, Vol. 94Winner of the society for biomaterials young investigator award for the annual meeting of the society for biomaterials, April 11-14, 2018, Atlanta, GA: S-nitrosated poly(propylene sulfide) nanoparticles for enhanced nitric oxide delivery to lymphatic tiss5 March 2018 | Journal of Biomedical Materials Research Part A, Vol. 106, No. 6Augmentation of CFTR maturation by S-nitrosoglutathione reductaseKhalequz Zaman, Victoria Sawczak, Atiya Zaidi, Maya Butler, Deric Bennett, Paulina Getsy, Maryam Zeinomar, Zivi Greenberg, Michael Forbes, Shagufta Rehman, Vinod Jyothikumar, Kim DeRonde, Abdus Sattar, Laura Smith, Deborah Corey, Adam Straub, Fei Sun, Lisa Palmer, Ammasi Periasamy, Scott Randell, Thomas J. 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