The many “faces” of copper in medicine and treatment

Biology of Metals - Tập 27 - Trang 611-621 - 2014
Anna Hordyjewska1, Łukasz Popiołek2, Joanna Kocot1
1Chair and Department of Medical Chemistry, Faculty of Medicine, Medical University of Lublin, Lublin, Poland
2Chair and Department of Organic Chemistry, Faculty of Pharmacy, Medical University of Lublin, Lublin, Poland

Tóm tắt

Copper (Cu) is an essential microelement found in all living organisms with the unique ability to adopt two different redox states—in the oxidized (Cu2+) and reduced (Cu+). It is required for survival and serves as an important catalytic cofactor in redox chemistry for proteins that carry out fundamental biological functions, important in growth and development. The deficit of copper can result in impaired energy production, abnormal glucose and cholesterol metabolism, increased oxidative damage, increased tissue iron (Fe) accrual, altered structure and function of circulating blood and immune cells, abnormal neuropeptides synthesis and processing, aberrant cardiac electrophysiology, impaired myocardial contractility, and persistent effects on the neurobehavioral and the immune system. Increased copper level has been found in several disorders like e.g.: Wilson’s disease or Menke’s disease. New findings with the great potential for impact in medicine include the use of copper-lowering therapy for antiangiogenesis, antifibrotic and anti-inflammatory purposes. The role of copper in formation of amyloid plaques in Alzheimer’s disease, and successful treatment of this disorder in rodent model by copper chelating are also of interest. In this work we will try to describe essential aspects of copper in chosen diseases. We will represent the evidence available on adverse effect derived from copper deficiency and copper excess. We will try to review also the copper biomarkers (chosen enzymes) that help reflect the level of copper in the body.

Tài liệu tham khảo

Abuduxikuer K, Wang JS (2014) Zinc mono-therapy in pre-symptomatic chinese children with Wilson disease: a single center, retrospective study. PLoS One 9:1–10 Arnal N, Morel GR, de Alaniz MJT, Castillo O, Marra CA (2013) Role of copper and cholesterol association in the neurodegenerative process. Int J Alzheimer’s Dis 10:1–15 Atwood CS, Scarpa SC, Huang X, Moir RD, Jones WD, Fairlie DP, Tanzi RE, Bush AI (2000) Characterization of copper interaction with Alzheimer amyloid β peptides: identification of an attomolar-affinity copper binding site on amyloid β1-42. J Neurochem 75:1219–1233 Baker A, Gormally S, Saxena R, Baldwin D, Drumm B, Bonham J, Portmann B, Mowat AP (1995) Copper-associated liver disease in childhood. J Hepatol 23:538–543 Bocharova OV, Breydo L, Salnikov VV, Baskakov IV (2005) Copper(II) inhibits in vitro conversion of prion protein into amyloid fibrils. Biochemistry 44:6776–6787 Brewer GJ (2000) Recognition, diagnosis and management of Wilson’s disease. Exp Biol Med 223:39–46 Brewer GJ (2003a) Copper in medicine. Curr Opin Chem Biol 7:207–212 Brewer GJ (2003b) Copper-lowering therapy with tetrathiomolybdate for cancer and diseases of fibrosis and inflammation. J Trace Elem Exp Med 16:191–199 Brewer GJ, Dick RD, Grover DK, LeClaire V, Tseng M, Wicha M, Pienta K, Redman BG, Jahan T, Sondak VK, Strawderman M, LeCarpentier G, Merajver SD (2000) Treatment of metastatic cancer with tetrathiomolybdate, an anticopper, antiangiogenic agent: phase I study. Clin Cancer Res 6:1–10 Brown DR (2003) Prion protein expression modulates neuronal copper content. J Neurochem 87:377–385 Butler P, McIntyre N, Mistry PK (2001) Molecular diagnosis of Wilson disease. Mol Genet Metab 72:223–230 Chen L, Li X, Zheng Z, Lu X, Lin M, Pan C, Liu J (2014) A novel ATP7B gene mutation in a liver failure patient with normal ceruloplasmin and low serum alkaline phosphatase. Gene 538:204–206 Cox C, Teknos TN, Barrios M, Brewer GJ, Dick RD, Merajver SD (2001) The role of copper suppressions as an antiangiogenic strategy in head and neck squamous cell carcinoma. Laryngoscope 111:696–701 Creaven BS, Duff B, Egana DA, Kavanagh K, Rosair G, Thangella VR, Walsh M (2010) Anticancer and antifungal activity of copper(II) complexes of quinolin-2(1H)-one derived from Schiff bases. Inorg Chim Acta 363:4048–4058 de Romana L, Olivares M, Uauy R, Araya M (2011) Risks and benefits of copper in light of new insights of copper homeostasis. J Trace Elem Med Biol 25:3–13 Duce JA, Tsatsanis A, Cater MA, James SA, Robb E, Wikhe K, Leong SL, Perez K, Johanssen T, Greenough MA, Cho HH, Galatis D, Moir RD, Masters CL, McLean C, Tanzi RE, Cappai R, Barnham KJ, Ciccotosto GD, Rogers JT, Bush AI (2010) An iron-export ferroxidase activity of β-amyloid protein precursor is inhibited by zinc in Alzheimer’s Disease. Cell 142:857–867 Easmon J (2002) Copper and iron complexes with antitumor activity. Expert Opin Ther Patents 12:789–818 Eskici G, Axelsen PH (2012) Copper and oxidative stress in the pathogenesis of Alzheimer’s disease. Biochemistry 51:6289–6331 Fernandes AS, Costa J, Gaspar J, Rueff J, Cabral MF, Cipriano M, Castro M, Oliveira NG (2012) Development of pyridine-containing macrocyclic copper(II) complexes: potential role in the redox modulation of oxaliplatin toxicity in human breast cells. Free Rad Res 46:1157–1166 Ferreza M, Hindo S, Chen D, Davenport A, Schmitt S, Tomco D, Dou QP (2010) Novel metals and metal complexes as platforms for cancer therapy. Curr Pharm Des 16:1813–1825 Gonzalez-Dominguez R, Gracia-Barrera Gomez-Ariza JL (2014) Characterization of metal profiles in serum during the progression of Alzheimer’s disease. Metallomics 6:292–300 Gromadzka G, Karpińska A, Przybyłkowski A, Litwin T, Wierzchowska-Ciok A, Dzieżyc K, Chabik G, Członkowska A (2014) Treatment with d-penicillamine or zinc sulphate affects copper metabolism and improves but not normalizes antioxidant capacity parameters in Wilson disease. Biometals 27:207–215 Harris ZL, Klomp LW, Gitlin JD (1998) Aceruloplasminemia: an inherited neurogenerative disease with impairment of iron homeostasis. Am J Clin Nutr 67:972S–977S Hedera P, Peltier A, Fink JK, Wilcock S, London Z, Brewer GJ (2009) Myelopolyneuropathy and pancytopenia due to copper deficiency and high zinc levels of unknown origin II. The denture cream is a primary source of excessive zinc. Neurotoxicology 30:996–999 Hijazi N, Shaked Y, Rosenmann H, Ben-Hur T, Gabizon R (2003) Copper binding to PrPC may inhibit prion disease propagation. Brain Res 993:192–200 Hornshaw MP, McDermott JR, Candy JM (1995a) Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein. Biochem Biophys Res Commun 207:621–629 Hornshaw MP, McDermott JR, Candy JM (1995b) Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein: structural studies using synthetic peptides. Biochem Biophys Res Commun 214:993–999 Hung YH, Bush AI, La Fontaine S (2013) Links between copper and cholesterol in Alzheimer’s. Front Physiol 4:1–11 Iakovidis I, Delimaris I, Piperkadis SM (2011) Copper and its complexes in medicine: a biochemical approach. Mol Biol Intern 20:1–15 Ironside JW (1996) Human prion diseases. J Neural Transm Suppl 47:231–246 Itoh S, Ozumi K, Kim HW, Nakagawa O, McKinney RD, Folz RJ, Zelko IN, Ushio-Fukai M, Fukai T (2009) Novel mechanism for regulation of extracellular SOD transcription and activity by copper; role of antioxidant-1. Free Rad Biol Med 46:95–104 Jacobs P, Wood L (2003) Hematology of malnutrition. Part one. Dis Mon 49:589–600 Joseph J, Nagashri K (2012) Novel copper-based therapeutic agent for anti-inflammatory: synthesis, characterization and biochemical activities of copper(II) complexes of hydroxyflavone schiff bases. Appl Biochem Biotechnol 167:1446–1458 Kalita J, Kumar V, Chandra S, Kumar B, Kant Misra U (2014) Worsening of Wilson disease following penicillamine therapy. Eur Neurol 71:126–131 Katwal R, Kaur H, Kapur BK (2013) Applications of copper—Schiff’s base complexes: a review. Sci Rev Chem Commun 3:1–15 Kramer ML, Kratzin HD, Schmidt B, Römer A, Liemann OW, Hornemann S, Kretzschmar H (2001) Prion protein binds copper within the physiological concentration range. J Biol Chem 276:16711–16719 Litwin T, Gromadzka G, Szpak GM, Jabłonka-Salach K, Bulska E, Członkowska A (2013) Brain metal accumulation in Wilson’s disease. J Neurol Sci 329:55–58 Lopes da Silva S, Vellas B, Elemans S, Luchsinger J, Kamphuis P, Yaffe K, Sijben J, Groenendijk M, Stijnen T (2013) Plasma nutrient status of patients with Alzheimer’s disease: systematic review and meta-analysis. Alzheimer’s Dement 10:1–18 Lynch SM, Colón W (2005) Dominant role of copper in the kinetic stability of Cu/Zn superoxide dismutase. Biochem Biophys Res Commun 340:457–461 Mittergger G, Korte S, Shakarami M, Herms J, Kretzschmar HA (2009) Role of copper and manganese in prion disease progression. Brain Res 1292:155–164 Nasulewicz A, Mazur A, Opolski A (2004) Role of copper in tumour angiogenesis—clinical implications. J Trace Elem Med Biol 18:1–8 Nations SP, Boyer PJ, Love LA, Burritt MF, Butz JA, Wolfe GI, Hynan LS, Reisch J, Trivedi JR (2008) Denture cream: an unusual source of excess zinc, leading to hypocupremia and neurologic disease. Neurology 71:639–643 Noda Y, Asada M, Kubota M, Maesako M, Watanabe K, Uemura M, Kihara T, Shimohama S, Takahashi R, Kinoshita A, Uemura K (2013) Copper enhances APP dimerization and promotes Aβ production. Neurosci Lett 547:10–15 Ogra Y, Aoyama M, Suzuki KT (2006) Protective role of metallothionein against copper depletion. Arch Biochem Biophys 451:112–118 Pan Q, Kleer CG, van Golen KN, Irani J, Bottema KM, Bias C, De Carvalho M, Mesri EA, Robins DM, Dick RD, Brewer GJ, Merajver SD (2002) Copper deficiency induced by tetrathiomolybdate suppresses tumor growth and angiogenesis. Cancer Res 62:4854–4859 Pauly PC, Harris DA (1998) Copper stimulates endocytosis of the prion protein. J Biol Chem 273:33107–33110 Peña MMO, Lee J, Thiele DJ (2000) A delicate balance: homeostatic control of copper uptake and distribution. J Nutr 130:1251–1260 Percival SS (1998) Copper and immunity. Am J Clin Nutr 67:1064S–1068S Prasad AS (2013) Discovery of human zinc deficiency: its impact on human health and disease. Adv Nutr 4:176–190 Puig S, Thiele D (2002) Molecular mechanism of copper uptake and distribution. Curr Opin Chem Biol 6:171–180 Roney N, Colman J (2004) Interaction profile for lead, manganese, zinc and copper. Environ Toxicol Pharmacol 18:231–234 Rowland LP, Schneider NA (2001) Amyotrophic lateral sclerosis. N Engl J Med 344:1688–1700 Shim H, Harris ZL (2003) Genetic defects in copper metabolism. J Nutr 133:1527S–1531S Takahashi Y, Miyajima H, Shirabe S, Nagataki S, Suenaga A, Gitlin JD (1996) Characterization of a nonsense mutation in the ceruloplasmin gene resulting in diabetes and neurodegenerative disease. Hum Mol Genet 5:81–84 Tapiero H, Townsend DM, Tew KD (2003) Trace elements in human physiology and pathology. Copper Biomed Pharmacother 57:386–398 Thiele DJ (2003) Intergrating trace element metabolism from the cell to the whole organism. J Nutr 133:1579S–1580S Turecky L, Kalina P, Uhlikova E, Namerova S, Krizko J (1984) Serum ceruloplasmin and copper levels in patients with primary brain tumors. Klin Wochenschr 62:187–189 Ugarte M, Osborne NN, Brown LA, Bishop PN et al (2013) Iron, zinc, and copper in retinal physiology and disease. Surv Ophthalmol 58:585–609 Uriu-Adams JY, Keen CL (2005) Copper, oxidative stress, and human health. Mol Aspects Med 26:268–298 Wang N, Qin-Yun D, Yue Z, Zhi-Ying W (2013) Zinc monotherapy and a mow-copper diet are beneficial in patients with Wilson Disease after liver transplantation. CNS Neurosci Ther 19:905–907 White A, Multhaup G, Maher F, Bellingham S, Camakaris J, Zheng H, Bush AI, Beyreuther K, Masters CL, Cappai R (1999) The Alzheimer’s disease amyloid precursor protein modulates copper-induced toxicity and oxidative stress in primary neuronal cultures. J Neurosci 19:9170–9179 Wiernicka A, Jańczyk W, Dądalski M, Avsar Y, Schmidt H, Socha P (2013) Gastrointestinal side effects in children with Wilson’s disease treated with zinc sulfate. World J Gastroenterol 19:4356–4362 Yoshii J, Yoshiji H, Kuriyama S, Ikenaka Y, Noguchi R, Okuda H, Tsujinoue H, Nakatani T, Kishida H, Nakae D, Gomez DE, De Lorenzo MS, Tejera AM, Fukui H (2001) The copper-chelating agent, trientine, suppresses tumor development and angiogenesis in the murine hepatocellular carcinoma cells. Int J Cancer 94:768–773