Biology:S-Nitrosylation

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Short description: Biochemical reaction; attachment of –NO to cysteine in a protein

In biochemistry, S-Nitrosylation is the covalent attachment of a nitric oxide group (–NO) to a cysteine thiol within a protein to form an S-nitrosothiol (SNO). S-nitrosylation has diverse regulatory roles in bacteria, yeast and plants and in all mammalian cells.[1] It thus operates as a fundamental mechanism for cellular signaling across phylogeny and accounts for the large part of NO bioactivity.

S-nitrosylation is precisely targeted,[2] reversible,[3] spatiotemporally restricted[4][5] and necessary for a wide range of cellular responses,[6] including the prototypic example of red blood cell mediated autoregulation of blood flow that is essential for vertebrate life.[7] Although originally thought to involve multiple chemical routes in vivo, accumulating evidence suggests that S-nitrosylation depends on enzymatic activity, entailing three classes of enzymes (S-nitrosylases) that operate in concert to conjugate NO to proteins, drawing analogy to ubiquitinylation.[8] Beside enzymatic activity, hydrophobicity and low pka values also play a key role in regulating the process.[6]S-Nitrosylation was first described by Stamler et al. and proposed as a general mechanism for control of protein function, including examples of both active and allosteric regulation of proteins by endogenous and exogenous sources of NO.[9][10][11] The redox-based chemical mechanisms for S-nitrosylation in biological systems were also described concomitantly.[12] Important examples of proteins whose activities were subsequently shown to be regulated by S-nitrosylation include the NMDA-type glutamate receptor in the brain.[13][14] Aberrant S-nitrosylation following stimulation of the NMDA receptor would come to serve as a prototypic example of the involvement of S-nitrosylation in disease.[15] S-nitrosylation similarly contributes to physiology and dysfunction of cardiac, airway and skeletal muscle and the immune system, reflecting wide-ranging functions in cells and tissues.[16][17][18] It is estimated that ~70% of the proteome is subject to S-nitrosylation and the majority of those sites are conserved.[19] S-Nitrosylation is also known to show up in mediating pathogenicity in Parkinson's disease systems.[20] S-Nitrosylation is thus established as ubiquitous in biology, having been demonstrated to occur in all phylogenetic kingdoms[21] and has been described as the prototypic redox-based signalling mechanism,[22]

Denitrosylation

The reverse of S-nitrosylation is denitrosylation, principally an enzymically controlled process. Multiple enzymes have been described to date, which fall into two main classes mediating denitrosylation of protein and low molecular weight SNOs, respectively. S-Nitrosoglutathione reductase (GSNOR) is exemplary of the low molecular weight class; it accelerates the decomposition of S-nitrosoglutathione (GSNO) and of SNO-proteins in equilibrium with GSNO. The enzyme is highly conserved from bacteria to humans.[23] Thioredoxin (Trx)-related proteins, including Trx1 and 2 in mammals, catalyze the direct denitrosylation of S-nitrosoproteins[24][25][26] (in addition to their role in transnitrosylation[27]). Aberrant S-nitrosylation (and denitrosylation) has been implicated in multiple diseases, including heart disease,[18] cancer and asthma[28][29][17] as well as neurological disorders, including stroke,[30] chronic degenerative diseases (e.g., Parkinson's and Alzheimer's disease)[31][32][33] and amyotrophic lateral sclerosis (ALS).[34]

Transnitrosylation

Another interesting aspect of S-Nitrosylation includes the protein protein transnitrosylation, which is the transfer of an NO moiety from a SNO to the free thiols in another protein. Thioredoxin(Txn), a protein disulfide oxidoreductase for the cytosol and caspase 3 are a good example where transnitrosylation is significant in regulating cell death.[6] Another example include, the structural changes in mammalian Hb to SNO-Hb under oxygen depleted conditions helps it to bind to AE1 (Anion Exchange, a membrane protein) and in turn gets transnitrosylated the later.[35] Cdk5 (a neuronal-specific kinase) is known get nitrosylated at cysteine 83 and 157 in different neurodegenerative diseases like AD. This SNO-Cdk5 in turn is nitrosylated Drp1, the nitrosylated form of which can be considered as a therapeutic target.[36]

References

  1. ↑ "Enzymatic mechanisms regulating protein S-nitrosylation: implications in health and disease". Journal of Molecular Medicine 90 (3): 233–244. March 2012. doi:10.1007/s00109-012-0878-z. PMID 22361849. 
  2. ↑ "Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO". Proceedings of the National Academy of Sciences of the United States of America 98 (20): 11158–11162. September 2001. doi:10.1073/pnas.201289098. PMID 11562475. Bibcode: 2001PNAS...9811158S. 
  3. ↑ "S-nitrosoglutathione reversibly inhibits GAPDH by S-nitrosylation". The American Journal of Physiology 269 (3 Pt 1): C739–C749. September 1995. doi:10.1152/ajpcell.1995.269.3.C739. PMID 7573405. 
  4. ↑ "Dexras1: a G protein specifically coupled to neuronal nitric oxide synthase via CAPON". Neuron 28 (1): 183–193. October 2000. doi:10.1016/s0896-6273(00)00095-7. PMID 11086993. 
  5. ↑ "Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking". Proceedings of the National Academy of Sciences of the United States of America 103 (52): 19777–19782. December 2006. doi:10.1073/pnas.0605907103. PMID 17170139. Bibcode: 2006PNAS..10319777I. 
  6. ↑ 6.0 6.1 6.2 "Protein S-nitrosylation: purview and parameters". Nature Reviews. Molecular Cell Biology 6 (2): 150–166. February 2005. doi:10.1038/nrm1569. PMID 15688001. 
  7. ↑ "Hemoglobin βCys93 is essential for cardiovascular function and integrated response to hypoxia". Proceedings of the National Academy of Sciences of the United States of America 112 (20): 6425–6430. May 2015. doi:10.1073/pnas.1502285112. PMID 25810253. Bibcode: 2015PNAS..112.6425Z. 
  8. ↑ "A Multiplex Enzymatic Machinery for Cellular Protein S-nitrosylation". Molecular Cell 69 (3): 451–464.e6. February 2018. doi:10.1016/j.molcel.2017.12.025. PMID 29358078. 
  9. ↑ "S-nitrosylation of proteins with nitric oxide: synthesis and characterization of biologically active compounds". Proceedings of the National Academy of Sciences of the United States of America 89 (1): 444–448. January 1992. doi:10.1073/pnas.89.1.444. PMID 1346070. Bibcode: 1992PNAS...89..444S. 
  10. ↑ "S-nitrosylation of tissue-type plasminogen activator confers vasodilatory and antiplatelet properties on the enzyme". Proceedings of the National Academy of Sciences of the United States of America 89 (17): 8087–8091. September 1992. doi:10.1073/pnas.89.17.8087. PMID 1325644. Bibcode: 1992PNAS...89.8087S. 
  11. ↑ "Comparison of properties of nitric oxide". The biology of nitric oxide: proceedings of the 2nd International Meeting on the Biology of Nitric Oxide, London. London: Portland Press. 1992. pp. 20–23. OCLC 29356699. 
  12. ↑ "Biochemistry of nitric oxide and its redox-activated forms". Science 258 (5090): 1898–1902. December 1992. doi:10.1126/science.1281928. PMID 1281928. Bibcode: 1992Sci...258.1898S. 
  13. ↑ "Effect of nitric oxide production on the redox modulatory site of the NMDA receptor-channel complex". Neuron 8 (6): 1087–1099. June 1992. doi:10.1016/0896-6273(92)90130-6. PMID 1376999. 
  14. ↑ "A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds". Nature 364 (6438): 626–632. August 1993. doi:10.1038/364626a0. PMID 8394509. Bibcode: 1993Natur.364..626L. 
  15. ↑ "Aberrant protein S-nitrosylation contributes to the pathophysiology of neurodegenerative diseases". Neurobiology of Disease 84: 99–108. December 2015. doi:10.1016/j.nbd.2015.03.017. PMID 25796565. 
  16. ↑ "A SNO storm in skeletal muscle". Cell 133 (1): 33–35. April 2008. doi:10.1016/j.cell.2008.03.013. PMID 18394987. 
  17. ↑ 17.0 17.1 "Protein S-nitrosylation in health and disease: a current perspective". Trends in Molecular Medicine 15 (9): 391–404. September 2009. doi:10.1016/j.molmed.2009.06.007. PMID 19726230. 
  18. ↑ 18.0 18.1 "Identification of novel S-nitrosation sites in soluble guanylyl cyclase, the nitric oxide receptor". Journal of Proteomics 138: 40–47. April 2016. doi:10.1016/j.jprot.2016.02.009. PMID 26917471. 
  19. ↑ "Protein S-Nitrosylation: Determinants of Specificity and Enzymatic Regulation of S-Nitrosothiol-Based Signaling". Antioxidants & Redox Signaling 30 (10): 1331–1351. April 2019. doi:10.1089/ars.2017.7403. PMID 29130312. 
  20. ↑ "Neurodegeneration: Impact of S-nitrosylated Parkin, DJ-1 and PINK1 on the pathogenesis of Parkinson's disease". Archives of Biochemistry and Biophysics 704: 108869. June 2021. doi:10.1016/j.abb.2021.108869. PMID 33819447. 
  21. ↑ "Endogenous protein S-Nitrosylation in E. coli: regulation by OxyR". Science 336 (6080): 470–473. April 2012. doi:10.1126/science.1215643. PMID 22539721. Bibcode: 2012Sci...336..470S. 
  22. ↑ "Balancing reactivity against selectivity: the evolution of protein S-nitrosylation as an effector of cell signaling by nitric oxide". Cardiovascular Research 75 (2): 210–219. July 2007. doi:10.1016/j.cardiores.2007.04.023. PMID 17524376. 
  23. ↑ "A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans". Nature 410 (6827): 490–494. March 2001. doi:10.1038/35068596. PMID 11260719. 
  24. ↑ "Thioredoxin and lipoic acid catalyze the denitrosation of low molecular weight and protein S-nitrosothiols". Journal of the American Chemical Society 127 (45): 15815–15823. November 2005. doi:10.1021/ja0529135. PMID 16277524. 
  25. ↑ "Thioredoxin catalyzes the denitrosation of low-molecular mass and protein S-nitrosothiols". Biochemistry 46 (28): 8472–8483. July 2007. doi:10.1021/bi700449x. PMID 17580965. 
  26. ↑ "Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins". Science 320 (5879): 1050–1054. May 2008. doi:10.1126/science.1158265. PMID 18497292. Bibcode: 2008Sci...320.1050B. 
  27. ↑ "Biotin Switch Processing and Mass Spectrometry Analysis of S-Nitrosated Thioredoxin and Its Transnitrosation Targets". Nitric Oxide. Methods in Molecular Biology. 1747. 2018. pp. 253–266. doi:10.1007/978-1-4939-7695-9_20. ISBN 978-1-4939-7694-2. 
  28. ↑ "Nitric oxide and cancer: the emerging role of S-nitrosylation". Current Molecular Medicine 12 (1): 50–67. January 2012. doi:10.2174/156652412798376099. PMID 22082481. 
  29. ↑ "S-nitrosylation of EGFR and Src activates an oncogenic signaling network in human basal-like breast cancer". Molecular Cancer Research 10 (9): 1203–1215. September 2012. doi:10.1158/1541-7786.MCR-12-0124. PMID 22878588. 
  30. ↑ "S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death". Science 297 (5584): 1186–1190. August 2002. doi:10.1126/science.1073634. PMID 12183632. Bibcode: 2002Sci...297.1186G. 
  31. ↑ "Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity". Proceedings of the National Academy of Sciences of the United States of America 101 (29): 10810–10814. July 2004. doi:10.1073/pnas.0404161101. PMID 15252205. Bibcode: 2004PNAS..10110810Y. 
  32. ↑ "S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration". Nature 441 (7092): 513–517. May 2006. doi:10.1038/nature04782. PMID 16724068. Bibcode: 2006Natur.441..513U. 
  33. ↑ "S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury". Science 324 (5923): 102–105. April 2009. doi:10.1126/science.1171091. PMID 19342591. Bibcode: 2009Sci...324..102C. 
  34. ↑ "S-nitrosothiol depletion in amyotrophic lateral sclerosis". Proceedings of the National Academy of Sciences of the United States of America 103 (7): 2404–2409. February 2006. doi:10.1073/pnas.0507243103. PMID 16461917. Bibcode: 2006PNAS..103.2404S. 
  35. ↑ "Export by red blood cells of nitric oxide bioactivity". Nature 409 (6820): 622–626. February 2001. doi:10.1038/35054560. PMID 11214321. 
  36. ↑ "Emerging role of protein-protein transnitrosylation in cell signaling pathways". Antioxidants & Redox Signaling 18 (3): 239–249. January 2013. doi:10.1089/ars.2012.4703. PMID 22657837. 



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