[Angelova M., Asenova S., Nedkova V., Koleva-Kolarova R. (2011). Copper in the human organism. Trakia J. Sci., 9: 88–98.]Search in Google Scholar
[Aoki T. (2004). Copper deficiency and the clinical practice. Japan Med. Assoc. J., 47: 365–370.10.5124/jkma.2004.47.4.370]Search in Google Scholar
[Balevska P.S., Russanov E.M., Kassabova T.A. (1981). Studies on lipid peroxidation in rat liver by copper deficiency. Int. J. Biochem., 13: 489–493.10.1016/0020-711X(81)90122-1]Search in Google Scholar
[Bhattacharjee A., Chakraborty K., Shukla A. (2017). Cellular copper homeostasis: current concepts on its interplay with glutathione homeostasis and its implication in physiology and human diseases. Metallomics, 10: 1376–1388.10.1039/C7MT00066A]Search in Google Scholar
[Bjorklund G. (2013). The role of zinc and copper in autism spectrum disorders. Acta Neurobiol. Exp. (Wars)., 73: 225–236.]Search in Google Scholar
[Bost M., Houdart S., Oberli M., Kalonji E., Huneau J.F., Margaritis I. (2016). Dietary copper and human health: Current evidence and unresolved issues. J. Trace Elem. Med. Biol., 35: 107–115.10.1016/j.jtemb.2016.02.006]Search in Google Scholar
[Brewer G.J. (2010). Risks of copper and iron toxicity during aging in humans. Chem. Res. Toxicol., 23: 319–326.10.1021/tx900338d]Search in Google Scholar
[Cakatay U., Telci A., Kayalì R., Tekeli F., Akçay T., Sivas A. (2001). Relation of oxidative protein damage and nitrotyrosine levels in the aging rat brain. Exp. Gerontol., 36: 221–229.10.1016/S0531-5565(00)00197-2]Search in Google Scholar
[Carmody R.J., Cotter T.G. (2000). Oxidative stress induces caspase-independent retinal apoptosis in vitro. Cell Death Differ., 7: 282–291.10.1038/sj.cdd.4400646]Search in Google Scholar
[Chauhan A., Sheikh A.M., Chauhan V. (2008). Increased copper-mediated oxidation of membrane phosphatidylethanolamine in autism. Am. J. Biochem. Biotechnol., 4: 95–100.10.3844/ajbbsp.2008.95.100]Search in Google Scholar
[Chen Y., Saari J., Kang Y. (1994). Weak antioxidant defenses make the heart a target for damage in copper-deficient rats. Free Radic. Biol. Med., 17: 529–536.10.1016/0891-5849(94)90092-2]Search in Google Scholar
[Chen Z., Meng H., Xing G., Chen C., Zhao Y., Jia G., Wang T., Yuan H., Ye C., Zhao F., Chai Z., Zhu C., Fang X., Ma B., Wan L. (2006). Acute toxicological effects of copper nanoparticles in vivo. Toxicol. Lett., 163: 109–120.10.1016/j.toxlet.2005.10.003]Search in Google Scholar
[Cholewińska E., Juśkiewicz J., Ognik K. (2018 a). Comparison of the effect of dietary copper nanoparticles and one copper (II) salt on the metabolic and immune status in a rat model. J. Trace Elem. Med. Biol., 48: 111–117.10.1016/j.jtemb.2018.03.01729773169]Search in Google Scholar
[Cholewińska E., Fotschki B., Juśkiewicz J., Rusinek-Prystupa E., Ognik K. (2018 b). The effect of copper level in the diet on the distribution, and biological and immunological responses in a rat model. J. Anim. Feed Sci., 27: 349–360.10.22358/jafs/99893/2018]Search in Google Scholar
[Cholewińska E., Ognik K., Fotschki B., Zduńczyk Z., Juśkiewicz J. (2018 c). Comparison of the effect of dietary copper nanoparticles and one copper (II) salt on the copper biodistribution and gastrointestinal and hepatic morphology and function in a rat model. PLoS One, 13: e0197083.10.1371/journal.pone.0197083595154629758074]Search in Google Scholar
[Cichoż-Lach H., Michalak A. (2014). Oxidative stress as a crucial factor in liver diseases. World J. Gastroenterol., 20: 8082–8091.10.3748/wjg.v20.i25.8082]Search in Google Scholar
[Di Nicolantonio J.J., Mangan D., O‘Keefe J.H. (2018). Copper deficiency may be a leading cause of ischaemic heart disease. Open Heart, 5: e000784.10.1136/openhrt-2018-000784]Search in Google Scholar
[Dubick M.A., Barr J.L., Keen C.L., Atkins J.L. (2015). Ceruloplasmin and hypoferremia: studies in burn and non-burn trauma patients. Antioxidants (Basel), 4: 153–169.10.3390/antiox4010153]Search in Google Scholar
[El Meskini R., Crabtree K.L., Cline L.B., Mains R.E., Eipper B.A., Ronnett G.V. (2007). ATP7A (Menkes protein) functions in axonal targeting and synaptogenesis. Mol. Cell. Neurosci., 34: 409–421.10.1016/j.mcn.2006.11.018]Search in Google Scholar
[Fossati P., Prencipe L., Berti G. (1980). Use of 3,5-dichloro-2-hydroxybenzenesulfonic acid/4-aminophenazone chromogenic system in direct enzymic assay of uric acid in serum and urine. Clin Chem., 26: 227–231.10.1093/clinchem/26.2.0227]Search in Google Scholar
[Fotschki B., Jurgoński A., Fotschki J., Majewski M., Ognik K., Juśkiewicz J. (2019). Dietary chicory inulin-rich meal exerts greater healing effects than fructooligosaccharides preparation in rats with trinitrobenzenesulfonic acid-induced necrotic colitis. Pol. J. Food Nutr. Sci., 69: 147–155.10.31883/pjfns-2019-0013]Search in Google Scholar
[Gaetke L.M., Chow C.K. (2003). Copper toxicity, oxidative stress, and antioxidant nutrients. Toxicology, 189: 147–163.10.1016/S0300-483X(03)00159-8]Search in Google Scholar
[Gaetke L.M., Chow-Johnson H.S., Chow C.K. (2014). Copper: toxicological relevance and mechanisms. Arch. Toxicol., 88: 1929–1938.10.1007/s00204-014-1355-y]Search in Google Scholar
[Gamez P., Caballero A.B. (2015). Copper in Alzheimer’s disease: Implications in amyloid aggregation and neurotoxicity. AIP Advances, 5: 092503.10.1063/1.4921314]Search in Google Scholar
[Gürler H.Ş., Bilgici B., Akar A.K., Tomak L., Bedir A. (2014). Increased DNA oxidation (8-OHdG) and protein oxidation (AOPP) by low level electromagnetic field (2.45 GHz) in rat brain and protective effect of garlic. Int. J. Radiat. Biol., 90: 892–896.10.3109/09553002.2014.922717]Search in Google Scholar
[Gybina A.A., Tkac I., Prohaska J.R. (2009). Copper deficiency alters the neurochemical profile of developing rat brain. Nutr. Neurosci., 12: 114–122.10.1179/147683009X423265]Search in Google Scholar
[Hellman N.E., Gitlin J.D. (2002). Ceruloplasmin metabolism and function. Annu. Rev. Nutr., 22: 439–458.10.1146/annurev.nutr.22.012502.114457]Search in Google Scholar
[Höhn T.J., Grune T. (2014). The proteasome and the degradation of oxidized proteins: part III – Redox regulation of the proteasomal system. Redox Biol., 14: 388–394.10.1016/j.redox.2013.12.029]Search in Google Scholar
[Hordyjewska A., Popiołek Ł., Kocot J. (2014). The many “faces” of copper in medicine and treatment. Biometals., 27: 611–621.10.1007/s10534-014-9736-5]Search in Google Scholar
[Huster D. (2010). Wilson disease. Best Pract. Res. Cl. Ga., 24: 531–539.10.1016/j.bpg.2010.07.014]Search in Google Scholar
[Jaiser S.R., Winston G.P. (2010). Copper deficiency myelopathy. J. Neurol., 257: 869–881.10.1007/s00415-010-5511-x]Search in Google Scholar
[Johnson W.M., Wilson-Delfosse A.L., Mieyal J.J. (2012). Dysregulation of glutathione homeostasis in neurodegenerative diseases. Nutrients, 4: 1399–1440.10.3390/nu4101399]Search in Google Scholar
[Jursa T., Smith D.R. (2008). Ceruloplasmin alters the tissue disposition and neurotoxicity of manganese, but not its loading onto transferrin. Toxicol Sci., 107: 182–193.10.1093/toxsci/kfn231]Search in Google Scholar
[Klevay L.M. (2008). Alzheimer’s disease as copper deficiency. Med. Hypotheses, 70: 802–807.10.1016/j.mehy.2007.04.051]Search in Google Scholar
[Kodama H., Fujisawa C., Bhadhprasit W. (2012). Inherited copper transport disorders: biochemical mechanisms, diagnosis, and treatment. Curr. Drug Metab., 13: 237–250.10.2174/138920012799320455]Search in Google Scholar
[Kumar V., Kalita J., Misra U.K., Bora H.K. (2015). A study of dose response and organ susceptibility of copper toxicity in a rat model. J. Trace Elem. Med. Biol., 29: 269–274.10.1016/j.jtemb.2014.06.004]Search in Google Scholar
[Kumar V., Kalita J., Bora H.K., Misra U.K. (2016). Temporal kinetics of organ damage in copper toxicity: A histopathological correlation in rat model. Regul. Toxicol. Pharmacol., 81: 372–380.10.1016/j.yrtph.2016.09.025]Search in Google Scholar
[Lawrence R.A., Jenkinson S.G. (1987). Effects of copper deficiency on carbon tetrachloride-induced lipid peroxidation. J. Lab. Clin. Med., 109: 134–140.]Search in Google Scholar
[Le A., Shibata N.M., French S.W., Kim K., Kharbanda K.K., Islam M.S., La Sal-le J.M., Halsted C.H., Keen C.L., Medici V. (2014). Characterization of timed changes in hepatic copper concentrations, methionine metabolism, gene expression, and global DNA methylation in the Jackson toxic milk mouse model of Wilson disease. Int. J. Mol. Sci., 15: 8004–8023.10.3390/ijms15058004]Search in Google Scholar
[Li S., Tan H.Y., Wang N., Zhang Z.J., Lao L., Wong C.W., Feng Y. (2015). The role of oxidative stress and antioxidants in liver diseases. Int. J. Mol. Sci., 16: 26087–26124.10.3390/ijms161125942]Search in Google Scholar
[Lisanti S., Omar W.A., Tomaszewski B., De Prins S., Jacobs G., Koppen G., Mathers J.C., Langie S.A.S. (2013). Comparison of methods for quantification of global DNA methylation in human cells and tissues. PLoS One, 8: e79044.10.1371/journal.pone.0079044]Search in Google Scholar
[Lv Y., Liu P., Xiang C., Yang H. (2013). Oxidative stress and hypoxia observed in the kidneys of mice after a 13-week oral administration of melamine and cyanuric acid combination. Res. Vet. Sci., 95: 1100–1106.10.1016/j.rvsc.2013.10.001]Search in Google Scholar
[Maiorino M., Zamburlini A., Roveri A., Ursini F. (1995). Copper-induced lipid peroxidation in liposomes, micelles, and LDL: which is the role of vitamin E? Free Radic. Biol. Med., 18: 67–74.10.1016/0891-5849(94)00103-Q]Search in Google Scholar
[Menkes J.H., Alter M., Steigleder G.K., Weakley D.R., Sung J.H. (1962). A sex-linked recessive disorder with retardation of growth, peculiar hair, and focal cerebral and cerebellar degeneration. Pediatrics, 29: 764–779.]Search in Google Scholar
[Moore L.D., Le T., Fan G. (2013). DNA methylation and its basic function. Neuropsychopharmacology, 38: 23–38.10.1038/npp.2012.112]Search in Google Scholar
[Muriel P., Gordillo K.R. (2016). Role of oxidative stress in liver health and disease. Oxid. Med Cell. Longev., 2016: 9037051.10.1155/2016/9037051]Search in Google Scholar
[Nishihara E., Furuyama T., Yamashita S., Mori N. (1998). Expression of copper trafficking genes in the mouse brain. Neuroreport, 9: 3259–3263.10.1097/00001756-199810050-00023]Search in Google Scholar
[NRC (National Research Council) (1989). Recommended Dietary Allowances, 10th ed. Washington, D.C., National Academy Press.]Search in Google Scholar
[Ognik K., Wertelecki T. (2012). Effect of different vitamin E sources and levels on selected oxidative status indices in blood and tissues as well as on rearing performance of slaughter turkey hens. J. Appl. Poult. Res., 21: 259–271.10.3382/japr.2011-00366]Search in Google Scholar
[Ognik K., Sembratowicz I., Cholewińska E., Jankowski J., Kozłowski K., Juś-kiewicz J., Zduńczyk Z. (2018). The effect of administration of copper nanoparticles to chickens in their drinking water on the immune and antioxidant status of the blood. Anim. Sci. J., 89: 579–588.10.1111/asj.12956]Search in Google Scholar
[Ognik K., Cholewińska E., Juśkiewicz J., Zduńczyk Z., Tutaj K., Szlązak R. (2019). The effect of copper nanoparticles and copper (II) salt on redox reactions and epigenetic changes in a rat model. J. Anim. Physiol. Anim. Nutr. (Berl.), 103: 675–686.10.1111/jpn.13025]Search in Google Scholar
[Opazo C.M., Greenough M.A., Bush A.I. (2014). Copper: from neurotransmission to neuroproteostasis. Front. Aging Neurosci., 6: 143.10.3389/fnagi.2014.00143]Search in Google Scholar
[Paglia D.E., Valentine W.N. (1967). Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J. Lab. Clin. Med., 70: 158–169.]Search in Google Scholar
[Palumaa P. (2013). Copper chaperones. The concept of conformational control in the metabolism of copper. FEBS Lett., 587: 1902–1910.10.1016/j.febslet.2013.05.019]Search in Google Scholar
[Prohaska J.R., Lukasewycz O.A. (1981). Copper deficiency suppresses the immune response of mice. Science, 213: 559–561.10.1126/science.7244654]Search in Google Scholar
[Reeves P.G. (1997). Components of the AIN-93 diets as improvements in the AIN-76A diet. J. Nutr., 127: 838S–8341S.10.1093/jn/127.5.838S]Search in Google Scholar
[Scheiber I.F., Mercer J.F., Dringen R. (2014). Metabolism and functions of copper in brain. Prog. Neurobiol., 116: 33–57.10.1016/j.pneurobio.2014.01.002]Search in Google Scholar
[Seol J.K., Jeong J.H., Nam S.Y., Yun J.W., Kim J.S., Lee B.J. (2015). Comparison of the bioavailability of nano- and micro-sized copper oxide particles in copper-deficient mice. J. Prev. Vet. Med., 39: 3–14.10.13041/jpvm.2015.39.1.3]Search in Google Scholar
[Sirajwala H.B., Dabhi A.S., Malukar N.R., Bhalgami R.B., Pandya T.P. (2007). Serum ceruloplasmin level as an extracellular antioxidant in acute myocardial infarction. JIACM, 8: 135–138.]Search in Google Scholar
[Sunderman F.W., Nomoto S. (1970). Measurement of human serum ceruloplasmin by its p-phenylenediamine oxidase activity. Clin. Chem., 16: 903–910.10.1093/clinchem/16.11.903]Search in Google Scholar
[Surai P.F., Kochish I.I., Fisinin V.I. (2018). Glutathione peroxidases in poultry biology: Part 1. Classification and mechanisms of action. Worlds Poult. Sci. J., 74: 185–198.10.1017/S0043933918000284]Search in Google Scholar
[Telianidis J., Hung Y.H., Materia S., Fontaine S.L. (2013). Role of the P-Type ATPases, ATP7A and ATP7B in brain copper homeostasis. Front. Aging Neurosci., 23: 44.10.3389/fnagi.2013.00044]Search in Google Scholar
[Tishchenko K.I., Beloglazkina E.K., Mazhuga A.G., Zyk N.V. (2016). Copper containing enzymes: site types and low molecular weight model compounds. Rev. J. Chem., 6: 49–82.10.1134/S2079978016010027]Search in Google Scholar
[Tümer Z., Møller L.B. (2010). Menkes disease. Eur. J. Hum. Genet., 18: 511–518.10.1038/ejhg.2009.187]Search in Google Scholar
[Udomsinprasert W., Kitkumthorn N., Mutirangura A., Chongsrisawat V., Poovorawan Y., Honsawek S. (2016). Global methylation, oxidative stress, and relative telomere length in biliary atresia patients. Sci. Rep., 6: 26969.10.1038/srep26969]Search in Google Scholar
[Uttara B., Singh A.V., Zamboni P., Mahajan R.T. (2009). Oxidative stress and neurode-generative diseases: a review of upstream and downstream antioxidant therapeutic options. Curr. Neuropharmacol., 7: 65–74.10.2174/157015909787602823]Search in Google Scholar
[Venza M., Visalli M., Beninati C., De Gaetano G.V., Teti D., Venza I. (2015). Cellular mechanisms of oxidative stress and action in melanoma. Oxid Med. Cell. Longev., 2015: 481782.10.1155/2015/481782]Search in Google Scholar
[Walsh W.J. (2012). Nutrient Power: Heal your biochemistry and heal your brain. New York, NY, Skyhorse.]Search in Google Scholar
[Weschawalit S., Thongthip S., Phutrakool P., Asawanonda P. (2017). Glutathione and its antiaging and antimelanogenic effects. Clin. Cosmet. Investig. Dermatol., 10: 147–153.10.2147/CCID.S128339]Search in Google Scholar
[Yamada H., Ono S., Wada S., Aoi W., Park E.Y., Nakamura Y., Sato K. (2018). Statuses of food-derived glutathione in intestine, blood, and liver of rat. NPJ Sci. Food, 2: 3.10.1038/s41538-018-0011-y]Search in Google Scholar
[Yanar K., Aydın S., Cakatay U., Mengi M., Buyukpınarbaşılı N., Atukeren P., Sitar M.E., Sönmez A., Uslu E. (2011). Protein and DNA oxidation in different anatomic regions of rat brain in a mimetic ageing model. Basic Clin. Pharmacol. Toxicol., 109: 423–433.10.1111/j.1742-7843.2011.00756.x]Search in Google Scholar
[Yang J., Yu L., Gaiteri C., Srivastava G.P., Chibnik L.B., Leurgans S.E., Schnei-der J.A., Meissner A., De Jager P.L., Bennett D.A. (2015). Association of DNA methylation in the brain with age in older persons is confounded by common neuropathologies. Int. J. Biochem. Cell Biol., 67: 58–64.10.1016/j.biocel.2015.05.009]Search in Google Scholar