Ascorbic acid modulates immune responses through Jumonji-C domain containing histone demethylases and Ten eleven translocation (TET) methylcytosine dioxygenase.
Ascorbic acid
Epigenetic modifications
Immunomodulation
Jumonji-C domain-containing histone demethylase (JHDM)
Ten eleven translocation (TET) methylcytosine dioxygenase
Journal
BioEssays : news and reviews in molecular, cellular and developmental biology
ISSN: 1521-1878
Titre abrégé: Bioessays
Pays: United States
ID NLM: 8510851
Informations de publication
Date de publication:
11 2023
11 2023
Historique:
revised:
29
08
2023
received:
19
02
2023
accepted:
31
08
2023
medline:
11
10
2023
pubmed:
11
9
2023
entrez:
11
9
2023
Statut:
ppublish
Résumé
Ascorbic acid is a redox regulator in many physiological processes. Besides its antioxidant activity, many intriguing functions of ascorbic acid in the expression of immunoregulatory genes have been suggested. Ascorbic acid acts as a co-factor for the Fe
Identifiants
pubmed: 37694689
doi: 10.1002/bies.202300035
doi:
Substances chimiques
Ascorbic Acid
PQ6CK8PD0R
Jumonji Domain-Containing Histone Demethylases
EC 1.14.11.-
Dioxygenases
EC 1.13.11.-
Histone Demethylases
EC 1.14.11.-
5-Methylcytosine
6R795CQT4H
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2300035Informations de copyright
© 2023 Wiley Periodicals LLC.
Références
Jafari, D., Esmaeilzadeh, A., Mohammadi-Kordkhayli, M., & Rezaei, N. (2019). Vitamin C and the Immune System. In Nutrition and Immunity (pp. 81-102). Springer International Publishing. https://doi.org/10.1007/978-3-030-16073-9_5
McCORMICK, W. J. (1959). Cancer: A collagen disease, secondary to a nutritional deficiency. Archive of Pediatrics, 76(4), 166-171.
Mayland, C. R., Bennett, M. I., & Allan, K. (2005). Vitamin C deficiency in cancer patients. Palliative Medicine, 19(1), 17-20. https://doi.org/10.1191/0269216305pm970oa
Huijskens, M. J. A. J., Wodzig, W. K. W. H., Walczak, M., Germeraad, W. T. V., & Bos, G. M. J. (2016). Ascorbic acid serum levels are reduced in patients with hematological malignancies. Results in Immunology, 6, 8-10. https://doi.org/10.1016/j.rinim.2016.01.001
Das, A. B., Smith-Díaz, C. C., & Vissers, M. C. M. (2021). Emerging epigenetic therapeutics for myeloid leukemia: Modulating demethylase activity with ascorbate. Haematologica, https://doi.org/10.3324/haematol.2020.259283
Bruno, E. J. Jr, Ziegenfuss, T. N., & Landis, J. (2006). Vitamin C: Research update. Current Sports Medicine Reports, 5(4), 177-181. https://doi.org/10.1007/s11932-006-0043-y
Tsukada, Y., Fang, J., Erdjument-Bromage, H., Warren, M. E., Borchers, C. H., Tempst, P., & Zhang, Y. (2006). Histone demethylation by a family of JmjC domain-containing proteins. Nature, 439(7078), 811-816. https://doi.org/10.1038/nature04433
Cloos, P. A., Christensen, J., Agger, K., Maiolica, A., Rappsilber, J., Antal, T., Hansen, K. H., & Helin, K. (2006). The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3. Nature, 442(7100), 307-311. https://doi.org/10.1038/nature04837
Tahiliani, M., Koh, K. P., Shen, Y., Pastor, W. A., Bandukwala, H., Brudno, Y., Agarwal, S., Iyer, L. M., Liu, D. R., Aravind, L., & Rao, A. (2009). Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by MLL partner TET1. Science, 324(5929), 930-935. https://doi.org/10.1126/science.1170116
Reidling, J. C., Subramanian, V. S., Dahhan, T., Sadat, M., & Said, H. M. (2008). Mechanisms and regulation of vitamin C uptake: Studies of the hSVCT systems in human liver epithelial cells. American Journal of Physiology-Gastrointestinal and Liver Physiology, 295(6), G1217-G1227. https://doi.org/10.1152/ajpgi.90399.2008
Nishikimi, M., Fukuyama, R., Minoshima, S., Shimizu, N., & Yagi, K. (1994). Cloning and chromosomal mapping of the human nonfunctional gene for L-gulono-gamma-lactone oxidase, the enzyme for L-ascorbic acid biosynthesis missing in man. The Journal of Biological Chemistry, 269(18), 13685-13688. http://www.ncbi.nlm.nih.gov/pubmed/8175804
Levine, M., Wang, Y., Padayatty, S. J., & Morrow, J. (2001). A new recommended dietary allowance of vitamin C for healthy young women. Proceedings of the National Academy of Sciences, 98(17), 9842-9846. https://doi.org/10.1073/pnas.171318198
Ang, A., Pullar, J. M., Currie, M. J., & Vissers, M. C. M. (2018). Vitamin C and immune cell function in inflammation and cancer. Biochemical Society Transactions, 46(5), 1147-1159. https://doi.org/10.1042/BST20180169
Levine, M., Conry-Cantilena, C., Wang, Y., Welch, R. W., Washko, P. W., Dhariwal, K. R., Park, J. B., Lazarev, A., Graumlich, J. F., King, J., & Cantilena, L. R. (1996). Vitamin C pharmacokinetics in healthy volunteers: Evidence for a recommended dietary allowance. Proceedings of the National Academy of Sciences, 93(8), 3704-3709. https://doi.org/10.1073/pnas.93.8.3704
Rivas, C. I., Zúñiga, F. A., Salas-Burgos, A., Mardones, L., Ormazabal, V., & Vera, J. C. (2008). Vitamin C transporters. Journal of Physiology and Biochemistry, 64(4), 357-375. https://doi.org/10.1007/BF03174092
Savini, I., Rossi, A., Pierro, C., Avigliano, L., & Catani, M. V. (2008). SVCT1 and SVCT2: Key proteins for vitamin C uptake. Amino Acids, 34(3), 347-355. https://doi.org/10.1007/s00726-007-0555-7
Michie, A. M., Chan, A. C., Ciofani, M., Carleton, M., Lefebvre, J. M., He, Y., Allman, D. M., Wiest, D. L., Zuniga-Pflucker, J. C., & Izon, D. J. (2007). Constitutive Notch signalling promotes CD4-CD8- thymocyte differentiation in the absence of the pre-TCR complex, by mimicking pre-TCR signals. International Immunology, 19(12), 1421-1430. https://doi.org/10.1093/intimm/dxm113
Manning, J., Mitchell, B., Appadurai, D. A., Shakya, A., Pierce, L. J., Wang, H., Nganga, V., Swanson, P. C., May, J. M., Tantin, D., & Spangrude, G. J. (2013). Vitamin C promotes maturation of T-cells. Antioxidants & Redox Signaling, 19(17), 2054-2067. https://doi.org/10.1089/ars.2012.4988
Kouakanou, L., Xu, Y., Peters, C., He, J., Wu, Y., Yin, Z., & Kabelitz, D. (2020). Vitamin C promotes the proliferation and effector functions of human γδ T cells. Cellular & Molecular Immunology, 17(5), 462-473. https://doi.org/10.1038/s41423-019-0247-8
Tsagaratou, A., Lio, C.-W. J., Yue, X., & Rao, A. (2017). TET methylcytosine oxidases in T cell and B cell development and function. Frontiers in Immunology, 8, 220. https://doi.org/10.3389/fimmu.2017.00220
Correa, L. O., Jordan, M. S., & Carty, S. A. (2020). DNA methylation in T-cell development and differentiation. Critical Reviews in Immunology, 40(2), 135-156. https://doi.org/10.1615/CritRevImmunol.2020033728
Watowich, M. B., Gilbert, M. R., & Larion, M. (2023). T cell exhaustion in malignant gliomas. Trends in Cancer, 9(4), 270-292. https://doi.org/10.1016/j.trecan.2022.12.008
Campbell, J. D., Cole, M., Bunditrutavorn, B., & Vella, A. T. (1999). Ascorbic acid is a potent inhibitor of various forms of T cell apoptosis. Cellular Immunology, 194(1), 1-5. https://doi.org/10.1006/cimm.1999.1485
Fraser, R. C., Pavlović, S., Kurahara, C. G., Murata, A., Peterson, N. S., Taylor, K. B., & Feigen, G. A. (1980). The effect of variations in vitamin C intake on the cellular immune response of guinea pigs. The American Journal of Clinical Nutrition, 33(4), 839-847. https://doi.org/10.1093/ajcn/33.4.839
Amin, S., Walsh, M., Wilson, C., Parker, A. E., Oscier, D., Willmore, E., Mann, D., & Mann, J. (2012). Cross-talk between DNA methylation and active histone modifications regulates aberrant expression of ZAP70 in CLL. Journal of Cellular and Molecular Medicine, 16(9), 2074-2084. https://doi.org/10.1111/j.1582-4934.2011.01503.x
Maeng, H. G., Lim, H., Jeong, Y., Woo, A., Kang, J. S., Lee, W. J., & Hwang, Y. (2009). Vitamin C enters mouse T cells as dehydroascorbic acid in vitro and does not recapitulate in vivo vitamin C effects. Immunobiology, 214(4), 311-320. https://doi.org/10.1016/j.imbio.2008.09.003
Eylar, E., Báez, I., Navas, J., & Mercado, C. (1996). Sustained levels of ascorbic acid are toxic and immunosuppressive for human T cells. Puerto Rico Health Sciences Journal, 15(1), 21-26. http://www.ncbi.nlm.nih.gov/pubmed/8744863
Jones, B., & Chen, J. (2006). Inhibition of IFN-gamma transcription by site-specific methylation during T helper cell development. The EMBO Journal, 25(11), 2443-2452. https://doi.org/10.1038/sj.emboj.7601148
Lee, D. U., Agarwal, S., & Rao, A. (2002). Th2 lineage commitment and efficient IL-4 production involves extended demethylation of the IL-4 gene. Immunity, 16(5), 649-660. https://doi.org/10.1016/s1074-7613(02)00314-x
Winders, B. R., Schwartz, R. H., & Bruniquel, D. (2004). A distinct region of the murine IFN-gamma promoter is hypomethylated from early T cell development through mature naive and Th1 cell differentiation, but is hypermethylated in Th2 cells. Journal of Immunology (Baltimore, Md. : 1950), 173(12), 7377-7384. https://doi.org/10.4049/jimmunol.173.12.7377
Schoenborn, J. R., Dorschner, M. O., Sekimata, M., Santer, D. M., Shnyreva, M., Fitzpatrick, D. R., Stamatoyannopoulos, J. A., & Wilson, C. B. (2007). Comprehensive epigenetic profiling identifies multiple distal regulatory elements directing transcription of the gene encoding interferon-gamma. Nature Immunology, 8(7), 732-742. https://doi.org/10.1038/ni1474
Kim, S. T., Fields, P. E., & Flavell, R. A. (2007). Demethylation of a specific hypersensitive site in the Th2 locus control region. Proceedings of the National Academy of Sciences of the United States of America, 104(43), 17052-17057. https://doi.org/10.1073/pnas.0708293104
Ichiyama, K., Chen, T., Wang, X., Yan, X., Kim, B.-S., Tanaka, S., Ndiaye-Lobry, D., Deng, Y., Zou, Y., Zheng, P., Tian, Q., Aifantis, I., Wei, L., & Dong, C. (2015). The methylcytosine dioxygenase Tet2 promotes DNA demethylation and activation of cytokine gene expression in T cells. Immunity, 42(4), 613-626. https://doi.org/10.1016/j.immuni.2015.03.005
Qin, X., Liu, J., Du, Y., Li, Y., Zheng, L., Chen, G., & Cao, Y. (2019). Different doses of vitamin C supplementation enhances the Th1 immune response to early Plasmodium yoelii 17XL infection in BALB/c mice. International Immunopharmacology, 70, 387-395. https://doi.org/10.1016/j.intimp.2019.02.031
Song, M. H., Nair, V. S., & Oh, K. I. (2017). Vitamin C enhances the expression of IL17 in a Jmjd2-dependent manner. BMB Reports, 50(1), 49-54. https://doi.org/10.5483/BMBRep.2017.50.1.193
Abbas, A. K., Benoist, C., Bluestone, J. A., Campbell, D. J., Ghosh, S., Hori, S., Jiang, S., Kuchroo, V. K., Mathis, D., Roncarolo, M. G., Rudensky, A., Sakaguchi, S., Shevach, E. M., Vignali, D. A. A., & Ziegler, S. F. (2013). Regulatory T cells: Recommendations to simplify the nomenclature. Nature Immunology, 14(4), 307-308. https://doi.org/10.1038/ni.2554
Josefowicz, S. Z., Lu, L.-F., & Rudensky, A. Y. (2012). Regulatory T cells: Mechanisms of differentiation and function. Annual Review of Immunology, 30(1), 531-564. https://doi.org/10.1146/annurev.immunol.25.022106.141623
Huehn, J., & Beyer, M. (2015). Epigenetic and transcriptional control of Foxp3+ regulatory T cells. Seminars in Immunology, 27(1), 10-18. https://doi.org/10.1016/j.smim.2015.02.002
Sasidharan Nair, V., Song, M. H., & Oh, K. I. (2016). Vitamin C facilitates demethylation of the Foxp3 enhancer in a Tet-dependent manner. Journal of Immunology, 196(5), 2119-2131. https://doi.org/10.4049/jimmunol.1502352
Vignali, D. A. A., Collison, L. W., & Workman, C. J. (2008). How regulatory T cells work. Nature Reviews Immunology, 8(7), 523-532. https://doi.org/10.1038/nri2343
Sojka, D. K., Huang, Y.-H., & Fowell, D. J. (2008). Mechanisms of regulatory T-cell suppression - a diverse arsenal for a moving target. Immunology, 124(1), 13-22. https://doi.org/10.1111/j.1365-2567.2008.02813.x
Wang, W., He, W., Ruan, Y., & Geng, Q. (2022). First pig-to-human heart transplantation. The Innovation, 3(2), 100223. https://doi.org/10.1016/j.xinn.2022.100223
Lio, C.-W., Zhang, J., González-Avalos, E., Hogan, P. G., Chang, X., & Rao, A. (2016). Tet2 and Tet3 cooperate with B-lineage transcription factors to regulate DNA modification and chromatin accessibility. Elife, 5, e18290. https://doi.org/10.7554/eLife.18290
Orlanski, S., Labi, V., Reizel, Y., Spiro, A., Lichtenstein, M., Levin-Klein, R., Koralov, S. B., Skversky, Y., Rajewsky, K., Cedar, H., & Bergman, Y. (2016). Tissue-specific DNA demethylation is required for proper B-cell differentiation and function. Proceedings of the National Academy of Sciences, 113(18), 5018-5023. https://doi.org/10.1073/pnas.1604365113
Lio, C.-W. J., Shukla, V., Samaniego-Castruita, D., González-Avalos, E., Chakraborty, A., Yue, X., Schatz, D. G., Ay, F., & Rao, A. (2019). TET enzymes augment activation-induced deaminase (AID) expression via 5-hydroxymethylcytosine modifications at the Aicda superenhancer. Science Immunology, 4(34), eaau7523. https://doi.org/10.1126/sciimmunol.aau7523
Schoeler, K., Aufschnaiter, A., Messner, S., Derudder, E., Herzog, S., Villunger, A., Rajewsky, K., & Labi, V. (2019). <scp>TET</scp>enzymes control antibody production and shape the mutational landscape in germinal centre B cells. The FEBS Journal, 286(18), 3566-3581. https://doi.org/10.1111/febs.14934
Fujii, K., Tanaka, S., Hasegawa, T., Narazaki, M., Kumanogoh, A., Koseki, H., Kurosaki, T., & Ise, W. (2020). Tet DNA demethylase is required for plasma cell differentiation by controlling expression levels of IRF4. International Immunology, 32(10), 683-690. https://doi.org/10.1093/intimm/dxaa042
Ise, W., Kohyama, M., Schraml, B. U., Zhang, T., Schwer, B., Basu, U., Alt, F. W., Tang, J., Oltz, E. M., Murphy, T. L., & Murphy, K. M. (2011). The transcription factor BATF controls the global regulators of class-switch recombination in both B cells and T cells. Nature Immunology, 12(6), 536-543. https://doi.org/10.1038/ni.2037
Qi, T., Sun, M., Zhang, C., Chen, P., Xiao, C., & Chang, X. (2020). Ascorbic acid promotes plasma cell differentiation through enhancing TET2/3-mediated DNA demethylation. Cell reports, 33(9), 108452. https://doi.org/10.1016/j.celrep.2020.108452
Chen, H.-Y., Almonte-Loya, A., Lay, F.-Y., Hsu, M., Johnson, E., González-Avalos, E., Yin, J., Bruno, R. S., Ma, Q., Ghoneim, H. E., Wozniak, D. J., Harrison, F. E., & Lio, C.-W. J. (2022). Epigenetic remodeling by vitamin C potentiates plasma cell differentiation. Elife, 11, e73754. https://doi.org/10.7554/eLife.73754
Rauch, P. J., Chudnovskiy, A., Robbins, C. S., Weber, G. F., Etzrodt, M., Hilgendorf, I., Tiglao, E., Figueiredo, J.-L., Iwamoto, Y., Theurl, I., Gorbatov, R., Waring, M. T., Chicoine, A. T., Mouded, M., Pittet, M. J., Nahrendorf, M., Weissleder, R., & Swirski, F. K. (2012). Innate response activator B cells protect against microbial sepsis. Science, 335(6068), 597-601. https://doi.org/10.1126/science.1215173
Shen, P., Roch, T., Lampropoulou, V., O'Connor, R. A., Stervbo, U., Hilgenberg, E., Ries, S., Dang, V. D., Jaimes, Y., Daridon, C., Li, R., Jouneau, L., Boudinot, P., Wilantri, S., Sakwa, I., Miyazaki, Y., Leech, M. D., McPherson, R. C., Wirtz, S., …, Fillatreau, S. (2014). IL-35-producing B cells are critical regulators of immunity during autoimmune and infectious diseases. Nature, 507(7492), 366-370. https://doi.org/10.1038/nature12979
Rodriguez, R. M., Suarez-Alvarez, B., Lavín, J. L., Ascensión, A. M., Gonzalez, M., Lozano, J. J., Raneros, A. B., Bulnes, P. D., Vidal-Castiñeira, J. R., Huidobro, C., Martin-Martin, C., Sanz, A. B., Ruiz-Ortega, M., Puig-Kröger, A., Corbí, A. L., Araúzo-Bravo, M. J., Aransay, A. M., & Lopez-Larrea, C. (2019). Signal integration and transcriptional regulation of the inflammatory response mediated by the GM-/M-CSF signaling axis in human monocytes. Cell Reports, 29(4), 860-872.e5. https://doi.org/10.1016/j.celrep.2019.09.035
Vento-Tormo, R., Company, C., Rodríguez-Ubreva, J., de la Rica, L., Urquiza, J. M., Javierre, B. M., Sabarinathan, R., Luque, A., Esteller, M., Aran, J. M., Álvarez-Errico, D., & Ballestar, E. (2016). IL-4 orchestrates STAT6-mediated DNA demethylation leading to dendritic cell differentiation. Genome Biology, 17(1), 4. https://doi.org/10.1186/s13059-015-0863-2
de la Rica, L., Rodríguez-Ubreva, J., García, M., Islam, A. B., Urquiza, J. M., Hernando, H., Christensen, J., Helin, K., Gómez-Vaquero, C., & Ballestar, E. (2013). PU.1 target genes undergo Tet2-coupled demethylation and DNMT3b-mediated methylation in monocyte-to-osteoclast differentiation. Genome Biology, 14(9), R99. https://doi.org/10.1186/gb-2013-14-9-r99
Mendes, K., Schmidhofer, S., Minderjahn, J., Glatz, D., Kiesewetter, C., Raithel, J., Wimmer, J., Gebhard, C., & Rehli, M. (2021). The epigenetic pioneer EGR2 initiates DNA demethylation in differentiating monocytes at both stable and transient binding sites. Nature Communications, 12(1), 1556. https://doi.org/10.1038/s41467-021-21661-y
Morante-Palacios, O., Ciudad, L., Micheroli, R., de la Calle-Fabregat, C., Li, T., Barbisan, G., Houtman, M., Edalat, S. G., Frank-Bertoncelj, M., Ospelt, C., & Ballestar, E. (2022). Coordinated glucocorticoid receptor and MAFB action induces tolerogenesis and epigenome remodeling in dendritic cells. Nucleic Acids Research, 50(1), 108-126. https://doi.org/10.1093/nar/gkab1182
Català-Moll, F., Ferreté-Bonastre, A. G., Godoy-Tena, G., Morante-Palacios, O., Ciudad, L., Barberà, L., Fondelli, F., Martínez-Cáceres, E. M., Rodríguez-Ubreva, J., Li, T., & Ballestar, E. (2022). Vitamin D receptor, STAT3, and TET2 cooperate to establish tolerogenesis. Cell Reports, 38(3), 110244. https://doi.org/10.1016/j.celrep.2021.110244
De Santa, F., Narang, V., Yap, Z. H., Tusi, B. K., Burgold, T., Austenaa, L., Bucci, G., Caganova, M., Notarbartolo, S., Casola, S., Testa, G., Sung, W.-K., Wei, C.-L., & Natoli, G. (2009). Jmjd3 contributes to the control of gene expression in LPS-activated macrophages. The EMBO Journal, 28(21), 3341-3352. https://doi.org/10.1038/emboj.2009.271
Yan, Q., Sun, L., Zhu, Z., Wang, L., Li, S., & Ye, R. D. (2014). Jmjd3-mediated epigenetic regulation of inflammatory cytokine gene expression in serum amyloid A-stimulated macrophages. Cellular Signalling, 26(9), 1783-1791. https://doi.org/10.1016/j.cellsig.2014.03.025
Medzhitov, R., & Horng, T. (2009). Transcriptional control of the inflammatory response. Nature Reviews Immunology, 9(10), 692-703. https://doi.org/10.1038/nri2634
Smale, S. T. (2010). Selective transcription in response to an inflammatory stimulus. Cell, 140(6), 833-844. https://doi.org/10.1016/j.cell.2010.01.037
Natoli, G., Ghisletti, S., & Barozzi, I. (2011). The genomic landscapes of inflammation. Genes & Development, 25(2), 101-106. https://doi.org/10.1101/gad.2018811
Zhu, Y., van Essen, D., & Saccani, S. (2012). Cell-type-specific control of enhancer activity by H3K9 trimethylation. Molecular Cell, 46(4), 408-423. https://doi.org/10.1016/j.molcel.2012.05.011
van Essen, D., Zhu, Y., & Saccani, S. (2010). A feed-forward circuit controlling inducible NF-κB target gene activation by promoter histone demethylation. Molecular Cell, 39(5), 750-760. https://doi.org/10.1016/j.molcel.2010.08.010
Stender, J. D., Pascual, G., Liu, W., Kaikkonen, M. U., Do, K., Spann, N. J., Boutros, M., Perrimon, N., Rosenfeld, M. G., & Glass, C. K. (2012). Control of proinflammatory gene programs by regulated trimethylation and demethylation of histone H4K20. Molecular Cell, 48(1), 28-38. https://doi.org/10.1016/j.molcel.2012.07.020
Kruidenier, L., Chung, C., Cheng, Z., Liddle, J., Che, K., Joberty, G., Bantscheff, M., Bountra, C., Bridges, A., Diallo, H., Eberhard, D., Hutchinson, S., Jones, E., Katso, R., Leveridge, M., Mander, P. K., Mosley, J., Ramirez-Molina, C., Rowland, P., …, Wilson, D. M. (2012). A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response. Nature, 488(7411), 404-408. https://doi.org/10.1038/nature11262
Suebsaard, P., & Charerntantanakul, W. (2021). Rutin, α-tocopherol, and l-ascorbic acid up-regulate type I interferon-regulated gene and type I and II interferon expressions and reduce inflammatory cytokine expressions in monocyte-derived macrophages infected with highly pathogenic porcine reproductiv. Veterinary Immunology and Immunopathology, 235, 110231. https://doi.org/10.1016/j.vetimm.2021.110231
Zhong, C., Tao, B., Yang, F., Xia, K., Yang, X., Chen, L., Peng, T., Xia, X., Li, X., & Peng, L. (2021). Histone demethylase JMJD1C promotes the polarization of M1 macrophages to prevent glioma by upregulating miR-302a. Clinical and Translational Medicine, 11(9), e424. https://doi.org/10.1002/ctm2.424
Lee, H., Hwang, S. J., Kim, H. R., Shin, C. H., Choi, K. H., Joung, J.-G., & Kim, H. H. (2016). Neurofibromatosis 2 (NF2) controls the invasiveness of glioblastoma through YAP-dependent expression of CYR61/CCN1 and miR-296-3p. Biochimica et Biophysica Acta (BBA)-Gene Regulatory Mechanisms, 1859(4), 599-611. https://doi.org/10.1016/j.bbagrm.2016.02.010
Spence, S., Fitzsimons, A., Boyd, C. R., Kessler, J., Fitzgerald, D., Elliott, J., Gabhann, J. N., Smith, S., Sica, A., Hams, E., Saunders, S. P., Jefferies, C. A., Fallon, P. G., McAuley, D. F., Kissenpfennig, A., & Johnston, J. A. (2013). RETRACTED: Suppressors of cytokine signaling 2 and 3 diametrically control macrophage polarization. Immunity, 38(1), 66-78. https://doi.org/10.1016/j.immuni.2012.09.013
Zhou, D., Chen, L., Yang, K., Jiang, H., Xu, W., & Luan, J. (2017). SOCS molecules: The growing players in macrophage polarization and function. Oncotarget, 8(36), 60710-60722. https://doi.org/10.18632/oncotarget.19940
Rogers, S. L., Rouhi, A., Takei, F., & Mager, D. L. (2006). A role for DNA hypomethylation and histone acetylation in maintaining allele-specific expression of mouse NKG2A in developing and mature NK cells. The Journal of Immunology, 177(1), 414-421. https://doi.org/10.4049/jimmunol.177.1.414
Zhao, N.-H., Qian, Y., Wu, C.-S., Wang, J.-W., Fang, Y., Fan, X.-P., Gao, S., Fan, Y.-C., & Wang, K. (2019). Diagnostic value of NKG2D promoter methylation in hepatitis B virus-associated hepatocellular carcinoma. Biomarkers in Medicine, 13(13), 1093-1105. https://doi.org/10.2217/bmm-2019-0102
Luetke-Eversloh, M., Cicek, B. B., Siracusa, F., Thom, J. T., Hamann, A., Frischbutter, S., Baumgrass, R., Chang, H.-D., Thiel, A., Dong, J., & Romagnani, C. (2014). NK cells gain higher IFN-γ competence during terminal differentiation. European Journal of Immunology, 44(7), 2074-2084. https://doi.org/10.1002/eji.201344072
Cribbs, A., Hookway, E. S., Wells, G., Lindow, M., Obad, S., Oerum, H., Prinjha, R. K., Athanasou, N., Sowman, A., Philpott, M., Penn, H., Soderstrom, K., Feldmann, M., & Oppermann, U. (2018). Inhibition of histone H3K27 demethylases selectively modulates inflammatory phenotypes of natural killer cells. Journal of Biological Chemistry, 293(7), 2422-2437. https://doi.org/10.1074/jbc.RA117.000698
Zhao, D., Zhang, Q., Liu, Y., Li, X., Zhao, K., Ding, Y., Li, Z., Shen, Q., Wang, C., Li, N., & Cao, X. (2016). H3K4me3 demethylase Kdm5a is required for NK cell activation by associating with p50 to suppress SOCS1. Cell Reports, 15(2), 288-299. https://doi.org/10.1016/j.celrep.2016.03.035
Huijskens, M. J., Walczak, M., Sarkar, S., Atrafi, F., Senden-Gijsbers, B. L., Tilanus, M. G., Bos, G. M., Wieten, L., & Germeraad, W. T. (2015). Ascorbic acid promotes proliferation of natural killer cell populations in culture systems applicable for natural killer cell therapy. Cytotherapy, 17(5), 613-620. https://doi.org/10.1016/j.jcyt.2015.01.004
Wu, C.-Y., Zhang, B., Kim, H., Anderson, S. K., Miller, J. S., & Cichocki, F. (2020). Ascorbic acid promotes KIR demethylation during early NK cell differentiation. The Journal of Immunology, 205(6), 1513-1523. https://doi.org/10.4049/jimmunol.2000212
Kim, J.-E., Cho, H.-S., Yang, H.-S., Jung, D.-J., Hong, S.-W., Hung, C.-F., Lee, W. J., & Kim, D. (2012). Depletion of ascorbic acid impairs NK cell activity against ovarian cancer in a mouse model. Immunobiology, 217(9), 873-881. https://doi.org/10.1016/j.imbio.2011.12.010
Atasever, B., Ertan, N. Z., Erdem-Kuruca, S., & Karakas, Z. (2006). IN vitro effects of vitamin C and selenium on NK activity of patients with β -thalassemia major. Pediatric Hematology and Oncology, 23(3), 187-197. https://doi.org/10.1080/08880010500506420
Toliopoulos, I. K., Simos, Y. V, Daskalou, T. A., Verginadis, I. I., Evangelou, A. M., & Karkabounas, S. C. (2011). Inhibition of platelet aggregation and immunomodulation of NK lymphocytes by administration of ascorbic acid. Indian Journal of Experimental Biology, 49(12), 904-908. http://www.ncbi.nlm.nih.gov/pubmed/22403863
Hyun, K., Jeon, J., Park, K., & Kim, J. (2017). Writing, erasing and reading histone lysine methylations. Experimental & Molecular Medicine, 49(4), e324-e324. https://doi.org/10.1038/emm.2017.11
Black, J. C., Van Rechem, C., & Whetstine, J. R. (2012). Histone lysine methylation dynamics: Establishment, regulation, and biological impact. Molecular Cell, 48(4), 491-507. https://doi.org/10.1016/j.molcel.2012.11.006
Rothbart, S. B., Krajewski, K., Nady, N., Tempel, W., Xue, S., Badeaux, A. I., Barsyte-Lovejoy, D., Martinez, J. Y., Bedford, M. T., Fuchs, S. M., Arrowsmith, C. H., & Strahl, B. D. (2012). Association of UHRF1 with methylated H3K9 directs the maintenance of DNA methylation. Nature Structural & Molecular Biology, 19(11), 1155-1160. https://doi.org/10.1038/nsmb.2391
Rothbart, S. B., Dickson, B. M., Ong, M. S., Krajewski, K., Houliston, S., Kireev, D. B., Arrowsmith, C. H., & Strahl, B. D. (2013). Multivalent histone engagement by the linked tandem Tudor and PHD domains of UHRF1 is required for the epigenetic inheritance of DNA methylation. Genes & Development, 27(11), 1288-1298. https://doi.org/10.1101/gad.220467.113
Liu, X., Gao, Q., Li, P., Zhao, Q., Zhang, J., Li, J., Koseki, H., & Wong, J. (2013). UHRF1 targets DNMT1 for DNA methylation through cooperative binding of hemi-methylated DNA and methylated H3K9. Nature Communications, 4(1), 1563. https://doi.org/10.1038/ncomms2562
Bicocca, V. T., Ormsby, T., Adhvaryu, K. K., Honda, S., & Selker, E. U. (2018). ASH1-catalyzed H3K36 methylation drives gene repression and marks H3K27me2/3-competent chromatin. Elife, 7, e41497. https://doi.org/10.7554/eLife.41497
Santos-Rosa, H., Schneider, R., Bannister, A. J., Sherriff, J., Bernstein, B. E., Emre, N. C. T., Schreiber, S. L., Mellor, J., & Kouzarides, T. (2002). Active genes are tri-methylated at K4 of histone H3. Nature, 419(6905), 407-411. https://doi.org/10.1038/nature01080
Satoh, T., Takeuchi, O., Vandenbon, A., Yasuda, K., Tanaka, Y., Kumagai, Y., Miyake, T., Matsushita, K., Okazaki, T., Saitoh, T., Honma, K., Matsuyama, T., Yui, K., Tsujimura, T., Standley, D. M., Nakanishi, K., Nakai, K., & Akira, S. (2010). The Jmjd3-Irf4 axis regulates M2 macrophage polarization and host responses against helminth infection. Nature Immunology, 11(10), 936-944. https://doi.org/10.1038/ni.1920
Yıldırım-Buharalıoğlu, G., Bond, M., Sala-Newby, G. B., Hindmarch, C. C. T., & Newby, A. C. (2017). Regulation of epigenetic modifiers, including KDM6B, by interferon-γ and interleukin-4 in human macrophages. Frontiers in Immunology, 8, 92. https://doi.org/10.3389/fimmu.2017.00092
Ptaschinski, C., Mukherjee, S., Moore, M. L., Albert, M., Helin, K., Kunkel, S. L., & Lukacs, N. W. (2015). RSV-induced H3K4 demethylase KDM5B leads to regulation of dendritic cell-derived innate cytokines and exacerbates pathogenesis in vivo. PLOS Pathogens, 11(6), e1004978. https://doi.org/10.1371/journal.ppat.1004978
Northrup, D., Yagi, R., Cui, K., Proctor, W. R., Wang, C., Placek, K., Pohl, L. R., Wang, R., Ge, K., Zhu, J., & Zhao, K. (2017). Histone demethylases UTX and JMJD3 are required for NKT cell development in mice. Cell & Bioscience, 7(1), 25. https://doi.org/10.1186/s13578-017-0152-8
An, J., Rao, A., & Ko, M. (2017). TET family dioxygenases and DNA demethylation in stem cells and cancers. Experimental & Molecular Medicine, 49(4), e323-e323. https://doi.org/10.1038/emm.2017.5
Shen, L., Song, C.-X., He, C., & Zhang, Y. (2014). Mechanism and function of oxidative reversal of DNA and RNA methylation. Annual Review of Biochemistry, 83(1), 585-614. https://doi.org/10.1146/annurev-biochem-060713-035513
He, Y.-F., Li, B.-Z., Li, Z., Liu, P., Wang, Y., Tang, Q., Ding, J., Jia, Y., Chen, Z., Li, L., Sun, Y., Li, X., Dai, Q., Song, C.-X., Zhang, K., He, C., & Xu, G.-L. (2011). Tet-mediated formation of 5-carboxylcytosine and its excision by TDG in mammalian DNA. Science, 333(6047), 1303-1307. https://doi.org/10.1126/science.1210944
Ito, S., Shen, L., Dai, Q., Wu, S. C., Collins, L. B., Swenberg, J. A., He, C., & Zhang, Y. (2011). Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine. Science, 333(6047), 1300-1303. https://doi.org/10.1126/science.1210597
Monfort, A., & Wutz, A. (2013). Breathing-in epigenetic change with vitamin C. EMBO Reports, 14(4), 337-346. https://doi.org/10.1038/embor.2013.29
Lio, C.-W. J., & Rao, A. (2019). TET enzymes and 5hmC in adaptive and innate immune systems. Frontiers in Immunology, 10, 210. https://doi.org/10.3389/fimmu.2019.00210
Ficz, G., & Gribben, J. G. (2014). Loss of 5-hydroxymethylcytosine in cancer: Cause or consequence? Genomics, 104(5), 352-357. https://doi.org/10.1016/j.ygeno.2014.08.017
Huang, Y., & Rao, A. (2014). Connections between TET proteins and aberrant DNA modification in cancer. Trends in Genetics, 30(10), 464-474. https://doi.org/10.1016/j.tig.2014.07.005
Sakata-Yanagimoto, M., Enami, T., Yoshida, K., Shiraishi, Y., Ishii, R., Miyake, Y., Muto, H., Tsuyama, N., Sato-Otsubo, A., Okuno, Y., Sakata, S., Kamada, Y., Nakamoto-Matsubara, R., Tran, N. B., Izutsu, K., Sato, Y., Ohta, Y., Furuta, J., Shimizu, S., …, Chiba, S. (2014). Somatic RHOA mutation in angioimmunoblastic T cell lymphoma. Nature Genetics, 46(2), 171-175. https://doi.org/10.1038/ng.2872
Yue, X., & Rao, A. (2020). TET family dioxygenases and the TET activator vitamin C in immune responses and cancer. Blood, 136(12), 1394-1401. https://doi.org/10.1182/blood.2019004158
Wang, T., Chen, K., Zeng, X., Yang, J., Wu, Y., Shi, X., Qin, B., Zeng, L., Esteban, M. A., Pan, G., & Pei, D. (2011). The histone demethylases jhdm1a/1b enhance somatic cell reprogramming in a vitamin-C-dependent manner. Cell Stem Cell, 9(6), 575-587. https://doi.org/10.1016/j.stem.2011.10.005
Liu, X., Khan, A., Li, H., Wang, S., Chen, X., & Huang, H. (2022). Ascorbic acid in epigenetic reprogramming. Current Stem Cell Research & Therapy, 17(1), 13-25. https://doi.org/10.2174/1574888X16666210714152730
Peng, D., He, A., He, S., Ge, G., Wang, S., Ci, W., Li, X., Xia, D., & Zhou, L. (2022). Ascorbic acid induced TET2 enzyme activation enhances cancer immunotherapy efficacy in renal cell carcinoma. International Journal of Biological Sciences, 18(3), 995-1007. https://doi.org/10.7150/ijbs.67329
Coker, S. J., Smith-Díaz, C. C., Dyson, R. M., Vissers, M. C. M., & Berry, M. J. (2022). The epigenetic role of vitamin C in neurodevelopment. International Journal of Molecular Sciences, 23(3), 1208. https://doi.org/10.3390/ijms23031208
Chen, Z., Zang, J., Whetstine, J., Hong, X., Davrazou, F., Kutateladze, T. G., Simpson, M., Mao, Q., Pan, C.-H., Dai, S., Hagman, J., Hansen, K., Shi, Y., & Zhang, G. (2006). Structural insights into histone demethylation by JMJD2 family members. Cell, 125(4), 691-702. https://doi.org/10.1016/j.cell.2006.04.024
Anand, R., & Marmorstein, R. (2007). Structure and mechanism of lysine-specific demethylase enzymes. Journal of Biological Chemistry, 282(49), 35425-35429. https://doi.org/10.1074/jbc.R700027200
Iyer, L. M., Tahiliani, M., Rao, A., & Aravind, L. (2009). Prediction of novel families of enzymes involved in oxidative and other complex modifications of bases in nucleic acids. Cell Cycle, 8(11), 1698-1710. https://doi.org/10.4161/cc.8.11.8580
Hu, L., Li, Z., Cheng, J., Rao, Q., Gong, W., Liu, M., Shi, Y. G., Zhu, J., Wang, P., & Xu, Y. (2013). Crystal structure of TET2-DNA complex: Insight into TET-mediated 5mC oxidation. Cell, 155(7), 1545-1555. https://doi.org/10.1016/j.cell.2013.11.020
Bedhiafi, T., Inchakalody, V. P., Fernandes, Q., Mestiri, S., Billa, N., Uddin, S., Merhi, M., & Dermime, S. (2022). The potential role of vitamin C in empowering cancer immunotherapy. Biomedicine & Pharmacotherapy, 146, 112553. https://doi.org/10.1016/j.biopha.2021.112553
Luchtel, R. A., Bhagat, T., Pradhan, K., Jacobs, W. R., Levine, M., Verma, A., & Shenoy, N. (2020). High-dose ascorbic acid synergizes with anti-PD1 in a lymphoma mouse model. Proceedings of the National Academy of Sciences, 117(3), 1666-1677. https://doi.org/10.1073/pnas.1908158117
Magrì, A., Germano, G., Lorenzato, A., Lamba, S., Chilà, R., Montone, M., Amodio, V., Ceruti, T., Sassi, F., Arena, S., Abrignani, S., D'Incalci, M., Zucchetti, M., Di Nicolantonio, F., & Bardelli, A. (2020). High-dose vitamin C enhances cancer immunotherapy. Science Translational Medicine, 12(532), eaay8707. https://doi.org/10.1126/scitranslmed.aay8707
Salomão, R., Ferreira, B. L., Salomão, M. C., Santos, S. S., Azevedo, L. C. P., & Brunialti, M. K. C. (2019). Sepsis: Evolving concepts and challenges. Brazilian Journal of Medical and Biological Research, 52(4), e8595. https://doi.org/10.1590/1414-431x20198595
Zhang, Y., & Ning, B. (2021). Signaling pathways and intervention therapies in sepsis. Signal Transduction and Targeted Therapy, 6(1), 407. https://doi.org/10.1038/s41392-021-00816-9
Torres, L. K., Pickkers, P., & van der Poll, T. (2022). Sepsis-induced immunosuppression. Annual Review of Physiology, 84(1), 157-181. https://doi.org/10.1146/annurev-physiol-061121-040214
Ruenjaiman, V., Butta, P., Leu, Y.-W., Pongpanich, M., Leelahavanichkul, A., Kueanjinda, P., & Palaga, T. (2020). Profile of Histone H3 Lysine 4 trimethylation and the effect of lipopolysaccharide/immune complex-activated macrophages on endotoxemia. Frontiers in Immunology, 10, 2956. https://doi.org/10.3389/fimmu.2019.02956
Pieterse, E., Hofstra, J., Berden, J., Herrmann, M., Dieker, J., & van der Vlag, J. (2014). Acetylated histones contribute to the immunostimulatory potential of neutrophil extracellular traps in systemic lupus erythematosus. Clinical and Experimental Immunology, 179(1), 68-74. https://doi.org/10.1111/cei.12359
Liu, C., Tangsombatvisit, S., Rosenberg, J. M., Mandelbaum, G., Gillespie, E. C., Gozani, O. P., Alizadeh, A. A., & Utz, P. J. (2012). Specific post-translational histone modifications of neutrophil extracellular traps as immunogens and potential targets of lupus autoantibodies. Arthritis Research & Therapy, 14(1), R25. https://doi.org/10.1186/ar3707
OʼSullivan, S. T., Lederer, J. A., Horgan, A. F., Chin, D. H. L., Mannick, J. A., & Rodrick, M. L. (1995). Major Injury leads to predominance of the T helper-2 lymphocyte phenotype and diminished interleukin-12 production associated with decreased resistance to infection. Annals of Surgery, 222(4), 482-492. https://doi.org/10.1097/00000658-199522240-00006
Roth, G., Moser, B., Krenn, C., Brunner, M., Haisjackl, M., Almer, G., Gerlitz, S., Wolner, E., Boltz-Nitulescu, G., & Ankersmit, H. J. (2003). Susceptibility to programmed cell death in T-lymphocytes from septic patients: A mechanism for lymphopenia and Th2 predominance. Biochemical and Biophysical Research Communications, 308(4), 840-846. https://doi.org/10.1016/S0006-291X(03)01482-7
Boretti, A., & Banik, B. K. (2020). Intravenous vitamin C for reduction of cytokines storm in acute respiratory distress syndrome. PharmaNutrition, 12, 100190. https://doi.org/10.1016/j.phanu.2020.100190
Schmidt, T., Kahn, R., & Kahn, F. (2022). Ascorbic acid attenuates activation and cytokine production in sepsis-like monocytes. Journal of Leukocyte Biology, 112(3), 491-498. https://doi.org/10.1002/JLB.4AB0521-243R
Ni, Y., Wu, G.-H., Cai, J.-J., Zhang, R., Zheng, Y., Liu, J.-Q., Yang, X.-H., Yang, X., Shen, Y., Lai, J.-M., Ye, X.-M., & Mo, S.-J. (2022). Tubule-mitophagic secretion of SerpinG1 reprograms macrophages to instruct anti-septic acute kidney injury efficacy of high-dose ascorbate mediated by NRF2 transactivation. International Journal of Biological Sciences, 18(13), 5168-5184. https://doi.org/10.7150/ijbs.74430
Williams Roberson, S., Nwosu, S., Collar, E. M., Kiehl, A. L., Harrison, F. E., Bastarache, J., Wilson, J. E., Mart, M. F., Sevransky, J. E., Ely, E. W., Lindsell, C. J., Jackson, J. C., & VICTAS Investigators. (2023). Association of vitamin c, thiamine, and hydrocortisone infusion with long-term cognitive, psychological, and functional outcomes in sepsis survivors: A secondary analysis of the vitamin c, thiamine, and steroids in sepsis randomized clinical trial. JAMA Network Open, 6(2), e230380. https://doi.org/10.1001/jamanetworkopen.2023.0380
Lamontagne, F., Masse, M.-H., Menard, J., Sprague, S., Pinto, R., Heyland, D. K., Cook, D. J., Battista, M.-C., Day, A. G., Guyatt, G. H., Kanji, S., Parke, R., McGuinness, S. P., Tirupakuzhi Vijayaraghavan, B.-K., Annane, D., Cohen, D., Arabi, Y. M., Bolduc, B., Marinoff, N., …, Adhikari, N. K. J. (2022). Intravenous vitamin C in adults with sepsis in the intensive care unit. New England Journal of Medicine, 386(25), 2387-2398. https://doi.org/10.1056/NEJMoa2200644
Wacker, D. A., Burton, S. L., Berger, J. P., Hegg, A. J., Heisdorffer, J., Wang, Q., Medcraft, E. J., & Reilkoff, R. A. (2022). Evaluating vitamin C in septic shock: A randomized controlled trial of vitamin C monotherapy*. Critical Care Medicine, 50(5), e458-e467. https://doi.org/10.1097/CCM.0000000000005427
Montazersaheb, S., Hosseiniyan Khatibi, S. M., Hejazi, M. S., Tarhriz, V., Farjami, A., Ghasemian Sorbeni, F., Farahzadi, R., & Ghasemnejad, T. (2022). COVID-19 infection: an overview on cytokine storm and related interventions. Virology Journal, 19(1), 92. https://doi.org/10.1186/s12985-022-01814-1
Liu, Y., Zhang, C., Huang, F., Yang, Y., Wang, F., Yuan, J., Zhang, Z., Qin, Y., Li, X., Zhao, D., Li, S., Tan, S., Wang, Z., Li, J., Shen, C., Li, J., Peng, L., Wu, W., Cao, M., …, & Jiang, C. (2020). Elevated plasma levels of selective cytokines in COVID-19 patients reflect viral load and lung injury. National Science Review, 7(6), 1003-1011. https://doi.org/10.1093/nsr/nwaa037
Coomes, E. A., & Haghbayan, H. (2020). Interleukin-6 in Covid-19: A systematic review and <scp>meta-analysis</scp>. Reviews in Medical Virology, 30(6), 1-9. https://doi.org/10.1002/rmv.2141
Rostamian, A., Ghazanfari, T., Arabkheradmand, J., Edalatifard, M., Ghaffarpour, S., Salehi, M. R., Raeeskarami, S. R., Mahmoodi Aliabadi, M., Rajabnia Chenary, M., Mirsharif, E. S., Jamali, D., Sattarian, M. R., Najafizadeh, R., Hosseinieselki Sari, S., Jafarpour, S., Nezhadseifi, E., Movasseghi, S., Baharvand, E., Beiranvand, S., …, Naghizadeh, M. M. (2020). Interleukin-6 as a potential predictor of COVID-19 disease severity in hospitalized patients and its association with clinical laboratory routine tests. Immunoregulation, 3, 29-36. https://doi.org/10.32598/IMMUNOREGULATION.3.1.4
Liu, F., Zhu, Y., Zhang, J., Li, Y., & Peng, Z. (2020). Intravenous high-dose vitamin C for the treatment of severe COVID-19: Sstudy protocol for a multicentre randomised controlled trial. BMJ Open, 10, e039519. https://doi.org/10.1136/bmjopen-2020-039519
Shakoor, H., Feehan, J., Al Dhaheri, A. S., Ali, H. I., Platat, C., Ismail, L. C., Apostolopoulos, V., & Stojanovska, L. (2021). Immune-boosting role of vitamins D, C, E, zinc, selenium and omega-3 fatty acids: Could they help against COVID-19? Maturitas, 143, 1-9. https://doi.org/10.1016/j.maturitas.2020.08.003
Krishnan, S., Patel, K., Desai, R., Sule, A., Paik, P., Miller, A., Barclay, A., Cassella, A., Lucaj, J., Royster, Y., Hakim, J., Ahmed, Z., & Ghoddoussi, F. (2020). Clinical comorbidities, characteristics, and outcomes of mechanically ventilated patients in the State of Michigan with SARS-CoV-2 pneumonia. Journal of Clinical Anesthesia, 67, 110005. https://doi.org/10.1016/j.jclinane.2020.110005
Alamdari, D. H., Moghaddam, A. B., Amini, S., Keramati, M. R., Zarmehri, A. M., Alamdari, A. H., Damsaz, M., Banpour, H., Yarahmadi, A., & Koliakos, G. (2020). Application of methylene blue -vitamin C -N-acetyl cysteine for treatment of critically ill COVID-19 patients, report of a phase-I clinical trial. European Journal of Pharmacology, 885, 173494. https://doi.org/10.1016/j.ejphar.2020.173494
Hemilä, H., & de Man, A. M. E. (2021). Vitamin C and COVID-19. Frontiers in Medicine, 7, 559811. https://doi.org/10.3389/fmed.2020.559811
Sokary, S., Ouagueni, A., & Ganji, V. (2022). Intravenous ascorbic acid and lung function in severely Ill COVID-19 patients. Metabolites, 12(9), 865. https://doi.org/10.3390/metabo12090865
Pedrosa, L. F. C., Barros, A. N. A. B., & Leite-Lais, L. (2022). Nutritional risk of vitamin D, vitamin C, zinc, and selenium deficiency on risk and clinical outcomes of COVID-19: A narrative review. Clinical Nutrition ESPEN, 47, 9-27. https://doi.org/10.1016/j.clnesp.2021.11.003
Izzo, R., Trimarco, V., Mone, P., Aloè, T., Capra Marzani, M., Diana, A., Fazio, G., Mallardo, M., Maniscalco, M., Marazzi, G., Messina, N., Mininni, S., Mussi, C., Pelaia, G., Pennisi, A., Santus, P., Scarpelli, F., Tursi, F., Zanforlin, A., …, Trimarco, B. (2022). Combining L-Arginine with vitamin C improves long-COVID symptoms: The LINCOLN Survey. Pharmacological Research, 183, 106360. https://doi.org/10.1016/j.phrs.2022.106360
Carr, A. C., & Gombart, A. F. (2022). Multi-level immune support by vitamins C and D during the SARS-CoV-2 pandemic. Nutrients, 14(3), 689. https://doi.org/10.3390/nu14030689
Olczak-Pruc, M., Swieczkowski, D., Ladny, J. R., Pruc, M., Juarez-Vela, R., Rafique, Z., Peacock, F. W., & Szarpak, L. (2022). Vitamin C supplementation for the treatment of COVID-19: A systematic review and meta-analysis. Nutrients, 14(19), 4217. https://doi.org/10.3390/nu14194217
RS, N., Reddy, M. V. N. J., Batra, S., Srivastava, S. K., & Syal, K. (2022). Vitamin C and its therapeutic potential in the management of COVID19. Clinical Nutrition ESPEN, 50, 8-14. https://doi.org/10.1016/j.clnesp.2022.05.026
Coppock, D., Violet, P.-C., Vasquez, G., Belden, K., Foster, M., Mullin, B., Magee, D., Mikell, I., Shah, L., Powers, V., Curcio, B., Monti, D., & Levine, M. (2022). Correction: Coppock et al. pharmacologic ascorbic acid as early therapy for hospitalized patients with COVID-19: A randomized clinical trial. Life, 12, 453. https://doi.org/10.3390/life12091354
Komal, Kumar, J., & Sen, A. (2022). The role of vitamin C: From prevention of pneumonia to treatment of Covid-19. Materials Today: Proceedings, https://doi.org/10.1016/j.matpr.2022.11.213
Hu, L., Lu, J., Cheng, J., Rao, Q., Li, Z., Hou, H., Lou, Z., Zhang, L., Li, W., Gong, W., Liu, M., Sun, C., Yin, X., Li, J., Tan, X., Wang, P., Wang, Y., Fang, D., Cui, Q., …, Xu, Y. (2015). Structural insight into substrate preference for TET-mediated oxidation. Nature, 527(7576), 118-122. https://doi.org/10.1038/nature15713
Cheng, Z., Cheung, P., Kuo, A. J., Yukl, E. T., Wilmot, C. M., Gozani, O., & Patel, D. J. (2014). A molecular threading mechanism underlies Jumonji lysine demethylase KDM2A regulation of methylated H3K36. Genes & Development, 28(16), 1758-1771. https://doi.org/10.1101/gad.246561.114
Zhang, J., Le Gras, S., Pouxvielh, K., Faure, F., Fallone, L., Kern, N., Moreews, M., Mathieu, A.-L., Schneider, R., Marliac, Q., Jung, M., Berton, A., Hayek, S., Vidalain, P.-O., Marçais, A., Dodard, G., Dejean, A., Brossay, L., Ghavi-Helm, Y., & Walzer, T. (2021). Sequential actions of EOMES and T-BET promote stepwise maturation of natural killer cells. Nature Communications, 12(1), 5446. https://doi.org/10.1038/s41467-021-25758-2