Open Access Review

The Dual Roles of S-Nitrosylation of Proteins in Cancer: Molecular Mechanisms and Recent Advancements

by Yi Wu a,1 Yanqi Li a,1 Tong Wu a  and  Hongmei Yang a,* orcid
The Public Experimental Center, Changchun University of Chinese Medicine, Changchun 130117, China
Author to whom correspondence should be addressed.
CI  2024, 37; 3(2), 37;
Received: 1 January 2024 / Accepted: 27 February 2024 / Published Online: 1 March 2024


Protein S-nitrosylation (SNO), emerging as an important posttranslational modification, involves covalent addition of nitric oxide (NO) to the sulfur atom of cysteine in proteins. Accumulated evidence suggests that protein SNO plays crucial roles in pathophysiological mechanisms in cancer, which is attracting great attention. However, there are still controversies about whether S-nitrosylated proteins act as oncogenic proteins or tumor suppressors in cancer. In this review, we provide an overview of the early and latest evidence regarding the underlying mechanism and dual roles of SNO in cancer, in an effort to clarify its contribution in tumor progression. It has been well established that S-nitrosylated proteins restrain tumor progression in several types of cancer, while they have exhibited activities in promoting cell proliferation and inhibiting apoptosis in some other kinds of cancer. Interestingly, emerging evidence also has highlighted both its anti-cancer and pro-tumorigenic roles in several other cancer diseases. Finally, current limitations and future research prospects are presented. The overview of targeting SNO in cancer will provide new opportunities for drug development through in-depth exploration of SNO-mediated signaling pathways.

Copyright: © 2024 by Wu, Li, Wu and Yang. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY) (Creative Commons Attribution 4.0 International License). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.


the Science and Technology Development Planning Project of Jilin Province (No. 20220508086RC, No. 20230203157SF)

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Wu, Y.; Li, Y.; Wu, T.; Yang, H. The Dual Roles of S-Nitrosylation of Proteins in Cancer: Molecular Mechanisms and Recent Advancements. Cancer Insight, 2024, 3, 37.
AMA Style
Wu Y, Li Y, Wu T, Yang H. The Dual Roles of S-Nitrosylation of Proteins in Cancer: Molecular Mechanisms and Recent Advancements. Cancer Insight; 2024, 3(2):37.
Chicago/Turabian Style
Wu, Yi; Li, Yanqi; Wu, Tong; Yang, Hongmei 2024. "The Dual Roles of S-Nitrosylation of Proteins in Cancer: Molecular Mechanisms and Recent Advancements" Cancer Insight 3, no.2:37.
APA style
Wu, Y., Li, Y., Wu, T., & Yang, H. (2024). The Dual Roles of S-Nitrosylation of Proteins in Cancer: Molecular Mechanisms and Recent Advancements. Cancer Insight, 3(2), 37.

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  1. Deo, SVS., Sharma, J., and Kumar, S. (2022). GLOBOCAN 2020 Report on Global Cancer Burden: Challenges and Opportunities for Surgical Oncologists. Ann Surg Oncol 29(11), 6497-6500.
  2. Sung, H., Ferlay, J., and Siegel, RL. (2021). Global Cancer Statistics 2020: GLOBOCAN Estimates of Incidence and Mortality Worldwide for 36 Cancers in 185 Countries. CA Cancer J Clin 71(3), 209-249.
  3. Maomao, C., He, L., and Dianqin, S. (2022). Current cancer burden in China: epidemiology, etiology, and prevention. Cancer Biol Med 19(8), 1121–38.
  4. Lewandowska, AM., Rudzki, M., and Rudzki, S. (2019). Environmental risk factors for cancer - review paper. Ann Agric Environ Med 26(1), 1-7.
  5. Song, Y., Xu, Y., and Pan, C. (2022). The emerging role of SPOP protein in tumorigenesis and cancer therapy. Mol Cancer 19(1), 2.
  6. Yu, F., Yu, C., and Li, F. (2021). Wnt/β-catenin signaling in cancers and targeted therapies. Signal Transduct Target Ther 6(1),307.
  7. Pan, S., and Chen, R. (2022). Pathological implication of protein post-translational modifications in cancer. Mol Aspects Med 86, 101097.
  8. Plenchette, S., Romagny, S., and Laurens, V. (2016). Itinéraire d'un agent double - NO, S-nitrosylation et cancer [NO and cancer: itinerary of a double agent]. Med Sci (Paris) 32(6-7), 625-33.
  9. Hickok, JR., and Thomas, DD. (2010). Nitric oxide and cancer therapy: the emperor has NO clothes. Curr Pharm Des 16(4), 381-91.
  10. Aranda, E., López-Pedrera, C., and De, La Haba-Rodriguez. (2012). Nitric oxide and cancer: the emerging role of S-nitrosylation. Curr Mol Med 12(1), 50-67.
  11. Sharma, V., Fernando, V., and Letson, J. (2021). S-Nitrosylation in Tumor Microenvironment. Int J Mol Sci 22(9), 4600.
  12. Mishra, D., Patel, V., and Banerjee, D. (2020). Nitric Oxide and S-Nitrosylation in Cancers: Emphasis on Breast Cancer. Breast Cancer (Auckl) 14, 1178223419882688.
  13. Ramírez-Patiño, R., Avalos-Navarro, and G., Figuera, LE. (2022). Influence of nitric oxide signaling mechanisms in cancer. Int J Immunopathol Pharmacol 36, 3946320221135454.
  14. Ye, H., Wu, J., and Liang, Z. (2022). Protein S-Nitrosation: Biochemistry, Identification, Molecular Mechanisms, and Therapeutic Applications. J Med Chem 65(8), 5902-5925.
  15. Zhang, Y., Deng, Y., and Yang, X. (2022). The Relationship Between Protein S-Nitrosylation and Human Diseases: A Review. Neurochem Res 45(12), 2815-2827.
  16. Wynia-Smith, SL., and Smith, BC. (2017). Nitrosothiol formation and S-nitrosation signaling through nitric oxide synthases. Nitric Oxide 63, 52-60.
  17. Numajiri, N., Takasawa, K., and Nishiya, T. (2011). On-off system for PI3-kinase-Akt signaling through S-nitrosylation of phosphatase with sequence homology to tensin (PTEN). Proc Natl Acad Sci U S A 108(25), 10349-54.
  18. Wang, Z. (2012). Protein S-nitrosylation and cancer. Cancer Lett 320(2), 123-9.
  19. Marozkina, NV., and Gaston, B. (2012). S-Nitrosylation signaling regulates cellular protein interactions. Biochim Biophys Acta 1820(6), 722-9.
  20. Khatib, S., Artoul, F., and Gershko, M. (2014). The synthesis and analysis of S-nitorsylated paraoxonase 1. Biochem Biophys Res Commun 444(3), 354-9.
  21. Rizza, S., and Filomeni, G. (2020). Exploiting S-nitrosylation for cancer therapy: facts and perspectives. Biochem J 477(19), 3649-3672.
  22. Peskin, AV., Meotti, FC., and de Souza, LF. (2020). Intra-dimer cooperativity between the active site cysteines during the oxidation of peroxiredoxin 2. Free Radic Biol Med 158, 115-125.
  23. Zhang, Y., Sun, C., and Xiao, G. (2019). S-nitrosylation of the Peroxiredoxin-2 promotes S-nitrosoglutathione-mediated lung cancer cells apoptosis via AMPK-SIRT1 pathway. Cell Death Dis 10(5), 329.
  24. Zhou, S., Han, Q., and Wang, R. (2016). PRDX2 protects hepatocellular carcinoma SMMC-7721 cells from oxidative stress. Oncol Lett 12(3), 2217-2221.
  25. Barnett, SD., and Buxton, ILO. (2017). The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy. Crit Rev Biochem Mol Biol 52(3), 340-354.
  26. Marozkina, NV., Wei, C., and Yemen, S. (2012). S-nitrosoglutathione reductase in human lung cancer. Am J Respir Cell Mol Biol 46(1), 63-70.
  27. Broniowska, KA., Diers, AR., and Hogg, N. (2013). S-nitrosoglutathione. Biochim Biophys Acta 1830(5), 3173-81.
  28. Wang, Z., Wang, N., and Liu, P. (2016). AMPK and Cancer. Exp Suppl 107, 203-226.
  29. Lee, CW., Wong, LL., and Tse, EY. (2012). AMPK promotes p53 acetylation via phosphorylation and inactivation of SIRT1 in liver cancer cells. Cancer Res 72(17), 4394-404.
  30. Poillet-Perez, L., Despouy, G., and Delage-Mourroux, R. (2010). Interplay between ROS and autophagy in cancer cells, from tumor initiation to cancer therapy. Redox Biol 4, 184-92.
  31. Achard, V., Putora, PM., and Omlin, A. (2012). Metastatic Prostate Cancer: Treatment Options. Oncology 100(1), 48-59.
  32. Hench, IB., Cathomas, R., and Costa, L. (2019). Analysis of AR/ARV7Expression in Isolated Circulating Tumor Cells of Patients with Metastatic Castration-Resistant Prostate Cancer (SAKK 08/14 IMPROVE Trial). Cancers (Basel) 11(8), 1099.
  33. Metcalf, D. (2013). The colony-stimulating factors and cancer. Cancer Immunol Res 1(6), 351-6.
  34. Hamilton, JA., Cook, AD., and Tak, PP. (2016). Anti-colony-stimulating factor therapies for inflammatory and autoimmune diseases. Nat Rev Drug Discov 16(1), 53-70.
  35. Sehgal, A., Irvine, KM., and Hume, DA. (2021). Functions of macrophage colony-stimulating factor (CSF1) in development, homeostasis, and tissue repair. Semin Immunol 54, 101509.
  36. Magkouta, SF., Vaitsi, PC., and Pappas, AG. (2021). CSF1/CSF1R Blockade Limits Mesothelioma and Enhances Efficiency of Anti-PDL1Immunotherapy. Cancers (Basel) 13(11), 2546.
  37. Firdaus, F., Kuchakulla, M., and Qureshi, R. (2022) S-nitrosylation of CSF1 receptor increases the efficacy of CSF1R blockage against prostate cancer. Cell Death Dis 13(10), 859.
  38. Zheng, L., Yang, Q., and Li, F. (2022). The Glycosylation of Immune Checkpoints and Their Applications in Oncology. Pharmaceuticals (Basel) 15(12),1451.
  39. Labianca, R., Beretta, GD., and Kildani, B. (2010). Colon cancer. Crit Rev Oncol Hematol 74(2), 106-33.
  40. Zadoroznyj, A., and Dubrez, L. (2022). Cytoplasmic and Nuclear Functions of cIAP1. Biomolecules 12(2), 322.
  41. Akizuki, Y., Morita, M., and Mori, Y. (2022). cIAP1-based degraders induce degradation via branched ubiquitin architectures. Nat Chem Biol 19(3), 311-322.
  42. Varfolomeev, E., Blankenship, JW., and Wayson, SM. (2007). IAP antagonists induce autoubiquitination of c-IAPs, NF-kappaB activation, and TNFalpha-dependent apoptosis. Cell 131(4), 669-81.
  43. Hira, K., Sajeli, and Begum, A. (2021). Methods for Evaluation of TNF-α Inhibition Effect. Methods Mol Biol 2248:271-279.
  44. Brenner, D., Blaser, H., and Mak, TW. (2015). Regulation of tumour necrosis factor signalling: live or let die. Nat Rev Immunol 15(6), 362-74.
  45. Romagny, S., Bouaouiche, and S., Lucchi, G. (2018). S-Nitrosylation of cIAP1 Switches Cancer Cell Fate from TNFα/TNFR1-Mediated Cell Survival to Cell Death. Cancer Res 78(8), 1948-1957.
  46. Motolani, A., Martin, M., and Sun, M. (2020). Phosphorylation of the Regulators, a Complex Facet of NF-κB Signaling in Cancer. Biomolecules 11(1), 15.
  47. Varfolomeev, E., and Vucic, D. (2022). RIP1 post-translational modifications. Biochem J 479(9), 929-951.
  48. Nakamura, T., Wang, L., and Wong, CC. (2010). Transnitrosylation of XIAP regulates caspase-dependent neuronal cell death. Mol Cell 39(2), 184-95.
  49. Brigle, K., and Rogers, B. (2017). Pathobiology and Diagnosis of Multiple Myeloma. Semin Oncol Nurs 33(3), 225-236.
  50. Kim, J., Choi, S., and Saxena, N. (2017). Regulation of STAT3 and NF-κB activations by S-nitrosylation in multiple myeloma. Free Radic Biol Med 106, 245-253.
  51. Zou, S., Tong, Q., and Liu, B. (2020). Targeting STAT3 in Cancer Immunotherapy. Mol Cancer 19(1), 145.
  52. Guanizo, AC., Fernando, CD., and Garama, DJ. (2018). STAT3: a multifaceted oncoprotein. Growth Factors 36(1-2), 1-14.
  53. Manni, S., Brancalion, A., and Mandato, E. (2013). Protein kinase CK2 inhibition down modulates the NF-κB and STAT3 survival pathways, enhances the cellular proteotoxic stress and synergistically boosts the cytotoxic effect of bortezomib on multiple myeloma and mantle cell lymphoma cells. PLoS One 8(9), e75280.
  54. Ma, J., Gong, W., and Liu, S. (2018). Ibrutinib targets microRNA-21 in multiple myeloma cells by inhibiting NF-κB and STAT3. Tumour Biol 40(1), 1010428317731369.
  55. Kannaiyan, R., Hay, HS., and Rajendran, P. (2011). Celastrol inhibits proliferation and induces chemosensitization through down-regulation of NF-κB and STAT3 regulated gene products in multiple myeloma cells. Br J Pharmacol 164(5), 1506-21.
  56. Bharti, AC., Shishodia, S., and Reuben, JM. (2004). Nuclear factor-kappaB and STAT3 are constitutively active in CD138+ cells derived from multiple myeloma patients, and suppression of these transcription factors leads to apoptosis. Blood 103(8), 3175-84.
  57. Bommert, K., Bargou, RC., and Stühmer, T. (2006). Signalling and survival pathways in multiple myeloma. Eur J Cancer 42(11), 1574-80.
  58. Kim, J., Choi, S., and Saxena, N. (2017). Regulation of STAT3 and NF-κB activations by S-nitrosylation in multiple myeloma. Free Radic Biol Med 106, 245-253.
  59. Bhattacharya, S., Ray, RM., and Johnson, LR. (2005). STAT3-mediated transcription of Bcl-2, Mcl-1 and c-IAP2 prevents apoptosis in polyamine-depleted cells. Biochem J 392(Pt 2), 335-44.
  60. Siegel RL, Miller KD, Jemal A. (2018). Cancer statistics,2018. CA: a cancer journal for clinicians 68, 7-30.
  61. Theoharides TC, Kempuraj D. (2023). Potential Role of Moesin in Regulating Mast Cell Secretion. International Journal of Molecular Sciences 24(15):12081.
  62. Solinet S, Mahmud K, Stewman SF, Ben El Kadhi K, Decelle B, Talje L, et al. (2013). The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex. International Journal of Molecular Sciences 202(2) 251-260.
  63. Blanchoin L, Boujemaa-Paterski R, Sykes C, Plastino J. (2014). Actin dynamics, architecture, and mechanics in cell motility. Physiological Reviews 94: 235-63.
  64. Bouchet, BP., and Akhmanova, A. (2017). Microtubules in 3D cell motility. J Cell Sci 130(1), 39-50.
  65. Succony, L., Rassl, DM., and Barker, AP. (2021). Adenocarcinoma spectrum lesions of the lung: Detection, pathology and treatment strategies. Cancer Treat Rev 99, 102237.
  66. Apte, RS., Chen, DS., and Ferrara, N. (2019). VEGF in Signaling and Disease: Beyond Discovery and Development. Cell 176(6), 1248-1264.
  67. Zhang, C., Li, T., and Yin, S. (2022). Monocytes deposit migrasomes to promote embryonic angiogenesis. Nat Cell Biol 24(12), 1726-1738.
  68. Byzova, TV., Goldman, CK., and Jankau, J. (2002). Adenovirus encoding vascular endothelial growth factor-D induces tissue-specific vascular patterns in vivo. Blood 99(12). 4434-42.
  69. Ehrenfeld, P., Cordova, F., and Duran, WN. (2019). S-nitrosylation and its role in breast cancer angiogenesis and metastasis. Nitric Oxide 87, 52-59.
  70. Kowalczuk, O., Laudanski, J., and Laudanski, W. (2018). Lymphatics-associated genes are downregulated at transcription level in non-small cell lung cancer. Oncol Lett 15(5), 6752-6762.
  71. He, Q., Qu, M., and Shen, T. (2022). Suppression of VEGFD expression by S-nitrosylation promotes the development of lung adenocarcinoma. J Exp Clin Cancer Res 41(1), 239.
  72. Dhillon, J., and Betancourt, M. (2020). Pancreatic Ductal Adenocarcinoma. Monogr Clin Cytol 26, 74-91.
  73. Adamska, A., Domenichini, A., and Falasca, M. (2017). Pancreatic Ductal Adenocarcinoma: Current and Evolving Therapies. Int J Mol Sci 18(7), 1338.
  74. Vincent, A., Herman, J., and Schulick, R. (2011). Pancreatic cancer. Lancet 378(9791), 607-20.
  75. Cheng, H., Wang, L., and Mollica, M. (2014). Nitric oxide in cancer metastasis. Cancer Lett 353(1), 1-7.
  76. Salimian, Rizi, B., Achreja, A., and Nagrath, D. (2017). Nitric Oxide: The Forgotten Child of Tumor Metabolism. Trends Cancer 3(9), 659-672.
  77. Seth, D., and Stamler, JS. (2011). The SNO-proteome: causation and classifications. Curr Opin Chem Biol 15(1), 129-36.
  78. Tan, C., Li, Y., and Huang, X. (2019). Extensive protein S-nitrosylation associated with human pancreatic ductal adenocarcinoma pathogenesis. Cell Death Dis 10(12), 914.
  79. Lim, KH., Ancrile, BB., and Kashatus, DF. (2008). Tumour maintenance is mediated by eNOS. Nature 452(7187), 646-9.
  80. Jin, UH., Karki, K., and Kim, SB. (2018). Inhibition of pancreatic cancer Panc1 cellmigration by omeprazole is dependent on aryl hydrocarbon receptor activation of JNK. Biochem Biophys Res Commun 501(3), 751-757.
  81. Aimé, S., Hichami, S., and Wendehenne, D. (2018). Analysis of Recombinant Protein S-Nitrosylation Using the Biotin-Switch Technique. Methods Mol Biol 1747, 131-141.
  82. Li, X., Ramadori, P., and Pfister, D. (2021). The immunological and metabolic landscape in primary and metastatic liver cancer. Nat Rev Cancer 21(9), 541-557.
  83. Perz, JF., Armstrong, GL., and Farrington, LA. (2006). The contributions of hepatitis B virus and hepatitis C virus infections to cirrhosis and primary liver cancer worldwide. J Hepatol 45(4), 529-38.
  84. Farazi, PA., and DePinho, RA. (2006). Hepatocellular carcinoma pathogenesis: from genes to environment. Nat Rev Cancer 6(9), 674-87.
  85. Rizza, S., Montagna, C., and Cardaci, S. (2006). S-nitrosylation of the Mitochondrial Chaperone TRAP1 Sensitizes Hepatocellular Carcinoma Cells to Inhibitors of Succinate Dehydrogenase. Cancer Res 76(14), 4170-82.
  86. Liu, Q., Gu, T., and Su, LY. (2021). GSNOR facilitates antiviral innate immunity by restricting TBK1 cysteine S-nitrosation. Redox Biol 47, 102172.
  87. Barnett, SD., and Buxton, ILO. (2017). The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy. Crit Rev Biochem Mol Biol 52(3), 340-354.
  88. Rizza, S., Di, Leo., and L, Pecorari. (2023). GSNOR deficiency promotes tumor growth via FAK1 S-nitrosylation. Cell Rep 42(1), 111997.
  89. Hess, DT., Matsumoto, A., and Kim, SO. (2005). Protein S-nitrosylation: purview and parameters. Nat Rev Mol Cell Biol 6(2), 150-66.
  90. Wei, W., Li, B., and Hanes, MA. (2010). S-nitrosylation from GSNOR deficiency impairs DNA repair and promotes hepatocarcinogenesis. Sci Transl Med 2(19), 19ra13.
  91. Lu, H., Cassis, LA., and Kooi, CW. (2016). Structure and functions of angiotensinogen. Hypertens Res 39(7), 492-500.
  92. Tubbs, JL., Pegg, AE., and Tainer, JA. (2007). DNA binding, nucleotide flipping, and the helix-turn-helix motif in base repair by O6-alkylguanine-DNA alkyltransferase and its implications for cancer chemotherapy. DNA Repair (Amst) 6(8), 1100-15.
  93. Wei, W., Yang, Z., and Tang, CH. (2011). Targeted deletion of GSNOR inhepatocytes of mice causes nitrosative inactivation of O6-alkylguanine-DNA alkyltransferase and increased sensitivity to genotoxic diethylnitrosamine. Carcinogenesis 32(7), 973-7.
  94. Lv, H., Zhu, C., and Wei, W. (2020). Enhanced Keap1-Nrf2/Trx-1 axis by daphnetin protects against oxidative stress-driven hepatotoxicity via inhibiting ASK1/JNK and Txnip/NLRP3 inflammasome activation. Phytomedicine 71, 153241.
  95. Yu, C., and Xiao, JH. (2021). The Keap1-Nrf2 System: A Mediator between Oxidative Stress and Aging. Oxid Med Cell Longev, 6635460.
  96. Quinti, L., Dayalan, Naidu S., Träger, U. (2017). KEAP1-modifying small molecule reveals muted NRF2 signaling responses in neural stem cells from Huntington's disease patients. Proc Natl Acad Sci U S A 114(23), E4676-E4685.
  97. Xinastle-Castillo, LO., and Landa, A. (2022). Physiological and modulatory role of thioredoxins in the cellular function. Open Med (Wars) 17(1), 2021-2035.
  98. González, R., Rodríguez-Hernández, MA., and Negrete, M. (2020). Downregulation of thioredoxin-1-dependent CD95 S-nitrosation by Sorafenib reduces liver cancer. Redox Biol 34, 101528.
  99. Oberacker, T., Kraft, L., and Schanz, M. (2023). The Importance of Thioredoxin-1 in Health and Disease. Antioxidants (Basel) 12(5), 1078.
  100. Chen, W., Wei, W., and Yu, L. (2021). Mammary Development and Breast Cancer: a Notch Perspective. J Mammary Gland Biol Neoplasia 26(3), 309-320.
  101. Shao, S., Zhao, X., and Zhang, X. (2015). Notch1 signaling regulates the epithelial-mesenchymal transition and invasion of breast cancer in a Slug-dependent manner. Mol Cancer 14(1), 28.
  102. Mishra, D., Patel, V., and Banerjee, D. (2020). Nitric Oxide and S-Nitrosylation in Cancers: Emphasis on Breast Cancer. Breast Cancer (Auckl) 14, 1178223419882688.
  103. Buggy, Y., Maguire, TM., and McGreal, G. (2004). Overexpression of the Ets-1 transcription factor in human breast cancer. Br J Cancer 91(7), 1308-15.
  104. Mylona, EE., Alexandrou, PT., and Giannopouloum IA. (2006). Study of the topographic distribution of ets-1 protein expression in invasive breast carcinomas in relation to tumor phenotype. Cancer Detect Prev 30(2), 111-7.
  105. Switzer, CH., Cheng, RY., and Ridnour, LA. (2012). Ets-1 is a transcriptional mediator of oncogenic nitric oxide signaling in estrogen receptor-negative breast cancer. Breast Cancer Res 14(5), R125.
  106. Marshall, HE., and Foster, MW. (2012). S-nitrosylation of Ras in breast cancer. Breast Cancer Res 14(6), 113.
  107. Switzer, CH., Glynn, SA., and Cheng, RY. (2012). S-nitrosylation of EGFR and Src activates an oncogenic signaling network in human basal-like breast cancer. Mol Cancer Res 10(9), 1203-15.
  108. Rashid, M., Zadeh, LR., and Baradaran, B. (2021). Up-down regulation of HIF-1α in cancer progression. Gene 798, 145796.
  109. Li, F., Sonveaux, P., and Rabbani, ZN. (2007). Regulation of HIF-1alpha stability through S-nitrosylation. Mol Cell 26(1), 63-74.
  110. Mittal, K., Ebos, J., and Rini, B. (2014). Angiogenesis and the tumor microenvironment: vascular endothelial growth factor and beyond. Semin Oncol 41(2), 235-51.
  111. Kobayashi, M., Narumi, K., and Furugen, A. (2021). Transport function, regulation, and biology of human monocarboxylate transporter 1 (hMCT1) and 4 (hMCT4). Pharmacol Ther 226, 107862.
  112. Stewart, C., Ralyea, C., and Lockwood, S. (2019). Ovarian Cancer: An Integrated Review. Semin Oncol Nurs 35(2), 151-156.
  113. Ganapathy-Kanniappan, S., and Geschwind, JF. (2013). Tumor glycolysis as a target for cancer therapy: progress and prospects. Mol Cancer 12, 152.
  114. Yi, W., Clark, PM., and Mason, DE. (2012). Phosphofructokinase 1 glycosylation regulates cell growth and metabolism. Science 337(6097), 975-80.
  115. Firestein, BL., and Bredt, DS. (1999). Interaction of neuronal nitric-oxide synthase and phosphofructokinase-M. J Biol Chem 274(15), 10545-50.
  116. Gao, W., Huang, M., and Chen, X. (2021). The role of S-nitrosylation of PFKM in regulation of glycolysis in ovarian cancer cells. Cell Death Dis 12(4), 408.
  117. Sawa, T., and Ohshima, H. (2006). Nitrative DNA damage in inflammation and its possible role in carcinogenesis. Nitric Oxide 14(2), 91-100.
  118. Burke, AJ., Garrido, P., and Johnson, C. (2017). Inflammation and Nitrosative Stress Effects in Ovarian and Prostate Pathology and Carcinogenesis. Antioxid Redox Signal 26(18), 1078-1090.
  119. Furuhashi, S., Sugita, H., Takamori, H. (2012). NO donor and MEK inhibitor synergistically inhibit proliferation and invasion of cancer cells. Int J Oncol 40(3), 807-15.
  120. Giri, S., Rattan, R., and Deshpande, M. (2014). Preclinical therapeutic potential of a nitrosylating agent in the treatment of ovarian cancer. PLoS One 9(6), e97897.
  121. Liu, M., Wang, F., and Wen, Z. (2014). Blockage of STAT3 signaling pathway with a decoy oligodeoxynucleotide inhibits growth of human ovarian cancer cells. Cancer Invest 32(1), 8-12.
  122. Altomare, DA., Wang, HQ., and Skele, KL. (2004). AKT and mTOR phosphorylation is frequently detected in ovarian cancer and can be targeted to disrupt ovarian tumor cell growth. Oncogene 23(34), 5853-7.
  123. Qin, Y., Dey, A., and Daaka, Y. (2013). Protein s-nitrosylation measurement. Methods Enzymol 522:409-25.
  124. Glish, GL., Vachet, RW. (2003). The basics of mass spectrometry in the twenty-first century. Nat Rev Drug Discov 2(2):140-50.
  125. Raju, K., Doulias, PT., and Tenopoulou, M. (2012). Strategies and tools to explore protein S-nitrosylation. Biochim Biophys Acta 1820(6):684-8.
  126. Bhattacharyya, C., Chakraborty, S., and Sengupta, R. (2022). NO news: S-(de)nitrosylation of cathepsins and their relationship with cancer. Anal Biochem 655:114872.