References
- WHO (World Health Organization). 2020. Food additives. WHO fact sheets. https://www.who.int/news-room/fact-sheets/detail/food-additives.
- FDA (Food and Drug Administration). 2018. Food ingredients and packaging terms. FDA Centre for Food Safety and Applied Nutrition. https://www.fda.gov/food/food-ingredients-packaging/food-ingredient-packaging-terms.
- Zhang Y, An Y, Jiang L, et al. The role of oxidative stress in Sudan IV-induced DNA damage in human liver-derived HepG2 cells. Environ Toxicol. 2011;26(3):292–299. doi:https://doi.org/10.1002/tox.20558.
- Genualdi S, MacMahon S, Robbins K, Farris S, Shyong N, DeJager L. Method development and survey of Sudan I–IV in palm oil and chilli spices in the Washington, DC, area. Food Addit Contam. 2016;33(4):1–591. doi:https://doi.org/10.1080/19440049.2016.1147986.
- Andoh SS, Nuutinen T, Mingle C, Roussey M. Qualitative analysis of Sudan IV in edible palm oil. J Eur Opt Soc. 2019;15(1):1–5.
- Ahmed-Refat NA, Ibrahim ZS, Moustafa GG, Sakamoto KQ, Ishizuka M, Fujita S. The induction of cytochrome P450 1A1 by Sudan dyes. J Biochem Mol Toxicol. 2008;22(2):77–84. doi:https://doi.org/10.1002/jbt.20220.
- Demirkol O, Zhang X, Ercal N. Oxidative effects of tartrazine (CAS No. 1934-21-0) and new coccin (CAS No. 2611-82-7) azo dyes on CHO cells. J Verbr Lebensm. 2012;7(3):229–236. doi:https://doi.org/10.1007/s00003-012-0782-z.
- Ugbaja RN, Akinhanmi TF, James AS, et al. Flavonoid-rich fractions from Clerodendrum volubile and Vernonia amygdalina extenuates arsenic-invoked hepato-renal toxicity via augmentation of the antioxidant system in rats. Clin Nutr Open Sci. 2021;35:12–25. doi:https://doi.org/10.1016/j.nutos.2020.12.003.
- An Y, Jiang L, Cao J, Geng C, Zhong L. Sudan I induces genotoxic effects and oxidative DNA damage in HepG2 cells. Mutat Res Genet Toxicol Environ Mutagen. 2007;627(2):164–170. doi:https://doi.org/10.1016/j.mrgentox.2006.11.004.
- Kim JH, Hahm DH, Yang DC, Kim JH, Lee HJ, Shim I. Effect of crude saponin of Korean red ginseng on high-fat diet-induced obesity in the rat. J Pharmacol Sci. 2005;97(1):124–131. doi:https://doi.org/10.1254/jphs.fp0040184.
- Marklund S, Marklund G. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem. 1974;47(3):469–474. doi:https://doi.org/10.1111/j.1432-1033.1974.tb03714.x.
- Hadwan MH, Abed HN. Data supporting the spectrophotometric method for the estimation of catalase activity. Data Brief. 2016;6:194–199. doi:https://doi.org/10.1016/j.dib.2015.12.012.
- Rotruck JT, Pope AL, Ganther HE, Swanson AB, Hafeman DG, Hoekstra W. Selenium: biochemical role as a component of glutathione peroxidase. Science. 1973;179(4073):588–590. doi:https://doi.org/10.1126/science.179.4073.588.
- Ellman GL. Tissue sulfhydryl groups. Arch Biochem Biophys. 1959;82(1):70–77. doi:https://doi.org/10.1016/0003-9861(59)90090-6.
- Rao MNA. Nitric oxide scavenging by curcuminoids. J Pharm Pharmacol. 1997;49(1):105–107.
- Beuge JA, Aust SD. The thiobarbituric acid assay. Methods Enzymol. 1978;52:305–307.
- Schneider CA, Rasband WS, Eliceiri KW. NIH Image to ImageJ: 25 years of image analysis. Nat Methods. 2012;9(7):671–675. doi:https://doi.org/10.1038/nmeth.2089.
- Nisa A, Zahra N, Butt YN. Sudan dyes and their potential health effects. Pak J Biochem Mol Biol. 2016;49(1):29–35.
- Oguntibeju OO, Esterhuyse AJ, Truter EJ. Red palm oil: nutritional, physiological and therapeutic roles in improving human wellbeing and quality of life. Br J Biomed Sci. 2009;66(4):216–222. doi:https://doi.org/10.1080/09674845.2009.11730279.
- Amin KA, Hameid HA, II, Abd Elsttar AH. Effect of food azo dyes tartrazine and carmoisine on biochemical parameters related to renal, hepatic function and oxidative stress biomarkers in young male rats. Food Chem Toxicol. 2010;48(10):2994–2999. doi:https://doi.org/10.1016/j.fct.2010.07.039.
- Ighodaro OM, Akinloye OA. First line defence antioxidants-superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX): Their fundamental role in the entire antioxidant defence grid. Alexandria J Med. 2018;54(4):287–293. doi:https://doi.org/10.1016/j.ajme.2017.09.001.
- Collin F. Chemical basis of reactive oxygen species reactivity and involvement in neurodegenerative diseases. Int J Mol Sci. 2019;20(10):2407. doi:https://doi.org/10.3390/ijms20102407.
- Lushchak VI. Glutathione homeostasis and functions: potential targets for medical interventions. J Amino Acids. 2012;2012:736837. doi:https://doi.org/10.1155/2012/736837.
- Nelson DL, Cox MM. Lehninger Principles of Biochemistry. New York (NY): W.H. Freeman and Company; 2008:434.
- Perez KM, Laughon M. Sildenafil in term and premature infants: a systematic review. Clin Ther. 2015;37(11):2598–2607. doi:https://doi.org/10.1016/j.clinthera.2015.07.019.
- Szabó C, Ischiropoulos H, Radi R. Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nat Rev Drug Discov. 2007;6(8):662–680. doi:https://doi.org/10.1038/nrd2222.
- Mates JM. Effects of antioxidant enzymes in the molecular control of reactive oxygen species toxicology. Toxicology. 2000;153(1-3):83–104.
- Yu BP, Suescun EA, Yang SY. Effect of age-related lipid peroxidation on membrane fluidity and phospholipase A2: modulation by dietary restriction. Mech Ageing Dev. 1992;65(1):17–33. doi:https://doi.org/10.1016/0047-6374(92)90123-U.
- Cheeseman KH. Mechanisms and effects of lipid peroxidation. Mol Asp Med. 1993;14(3):191–197. doi:https://doi.org/10.1016/0098-2997(93)90005-X.
- Niedernhofer LJ, Daniels JS, Rouzer CA, Greene RE, Marnett LJ. Malondialdehyde, a product of lipid peroxidation, is mutagenic in human cells. J Biol Chem. 2003;278(33):31426–31433. doi:https://doi.org/10.1074/jbc.M212549200.
- Vistoli G, De Maddis D, Cipak A, Zarkovic N, Carini M, Aldini G. Advanced glycoxidation and lipoxidation end products (AGEs and ALEs): an overview of their mechanisms of formation. Free Radic Res. 2013;47 Suppl 1:3–27. doi:https://doi.org/10.3109/10715762.2013.815348.
- Gentile F, Arcaro A, Pizzimenti S, et al. DNA damage by lipid peroxidation products: implications in cancer, inflammation and autoimmunity. AIMS Genet. 2017;4(2):103–137. doi:https://doi.org/10.3934/genet.2017.2.103.
- Gureev AP, Popov VN, Starkov AA. Crosstalk between the mTOR and Nrf2/ARE signaling pathways as a target in the improvement of long-term potentiation. Exp Neurol. 2020;328:113285. doi:https://doi.org/10.1016/j.expneurol.2020.113285.
- Chan K, Han XD, Kan YW. An important function of Nrf2 in combating oxidative stress: detoxification of acetaminophen. Proc Natl Acad Sci USA. 2001;98(8):4611–4616. doi:https://doi.org/10.1073/pnas.081082098.
- Hoshino T, Tabuchi K, Nishimura B, et al. Protective role of Nrf2 in age-related hearing loss and gentamicin ototoxicity. Biochem Biophys Res Commun. 2011;415(1):94–98. doi:https://doi.org/10.1016/j.bbrc.2011.10.019.
- Zweig JA, Brandes MS, Brumbach BH, et al. Loss of NRF2 accelerates cognitive decline, exacerbates mitochondrial dysfunction, and is required for the cognitive enhancing effects of Centella asiatica during aging. Neurobiol Aging. 2021;100:48–58. doi:https://doi.org/10.1016/j.neurobiolaging.2020.11.019.
- Ma Q. Role of nrf2 in oxidative stress and toxicity. Annu Rev Pharmacol Toxicol. 2013;53:401–426. doi:https://doi.org/10.1146/annurev-pharmtox-011112-140320.