Copper mediated neurological disorder: Visions into amyotrophic lateral sclerosis, Alzheimer and Menkes disease

Journal of Trace Elements in Medicine and Biology

Volumn 29, Issue , 2015, Pages 11-23

  Ahuja, Anami ^a   Dev, Kapil ^b   Tanwar, Ranjeet S ^c   Selwal, Krishan K ^d   Tyagi, Pankaj K ^e  

^a NIMS UNIVERSITY   (India)

^b CHARLES UNIVERSITY   (Czech Republic)

^c NCCollege of Engg   (India)

^d DEENBANDHU CHHOTU RAM UNIVERSITY OF SCIENCE AND TECHNOLOGY   (India)

^e MEERUT INSTITUTE OF ENGINEERING AND TECHNOLOGY   (India)

Author keywords

Alzheimer disease; Amyotrophic lateral sclerosis; Copper; Menkes disease; Neurological disorders

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; GLUTAMIC ACID; GLUTATHIONE; MENKES PROTEIN; MITOCHONDRIAL DNA; WILSON DISEASE PROTEIN;

ALZHEIMER DISEASE; AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; ATP7A GENE; BINDING AFFINITY; BINDING SITE; BLOOD BRAIN BARRIER; COPPER METABOLISM; DISEASE COURSE; DISORDERS OF MITOCHONDRIAL FUNCTIONS; DISULFIDE BOND; DNA DAMAGE; ENZYME MECHANISM; EXCITOTOXICITY; GENE; GENE MUTATION; HOMEOSTASIS; HUMAN; MENKES SYNDROME; MISSENSE MUTATION; MOTONEURON; NERVE CELL NECROSIS; NERVE FIBER TRANSPORT; OXIDATIVE STRESS; PATHOGENESIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; BRAIN; MENKES KINKY HAIR SYNDROME; METABOLISM; PATHOLOGY;

ALZHEIMER DISEASE; AMYOTROPHIC LATERAL SCLEROSIS; BRAIN; COPPER; HUMANS; MENKES KINKY HAIR SYNDROME; OXIDATIVE STRESS;

EID: 84919644280     PISSN: 0946672X     EISSN: 18783252     Source Type: Journal    
DOI: 10.1016/j.jtemb.2014.05.003     Document Type: Review

References (178)

1. Angelova M., Asenova S., Nedkova V., Koleva K.R. Copper in the human organism. Trakia J Sci 2011, 9(1):88-98.
2. Madsen E., Gitlin J.D. Copper and iron disorders of the brain. Annu Rev Neurosci 2007, 30:317-337.
3. Svetlana L., Ashima B., Ann L.H. Copper handling machinery of the brain. Metallomics 2010, 2:596.
4. Lech T., Sadlik J.K. Copper concentration in body tissues and fluids in normal subjects of southern Poland. Biol Trace Elem Res 2007, 118(July (1)):10-15.
5. Gybina A.A., Tkac I., Prohaska J.R. Copper deficiency alters the neurochemical profile of developing rat brain. Nutr Neurosci 2009, 12(June (3)):114-122.
6. Nischwitz V., Achim B., Bernhard M. Speciation analysis of selected metals and determination of their total contents in paired serum and cerebrospinal fluid samples: an approach to investigate the permeability of the human blood-cerebrospinal fluid-barrier. Anal Chim Acta 2008, 627:258-269.
7. Basun H., Forssell L.G., Wetterberg L., Winblad B. Metals and trace elements in plasma and cerebrospinal fluid in normal aging and Alzheimer's disease. J Neural Transm Park Dis Dement Sect 1991, 3:231-258.
8. Hershey C.O., Hershey L.A., Varnes A., Vibhakar S.D., Lavin P., Strain W.H. Cerebrospinal fluid trace element content in dementia: clinical, radiologic, and pathologic correlations. Neurology 1983, 33(October (10)):1350-1353.
9. Hodgson E.K., Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry 1975, 14(December (24)):5294-5299.
10. Blech D.M., Borders C.L. Hydroperoxide anion, HO-2, is an affinity reagent for the inactivation of yeast Cu, Zn superoxide dismutase: modification of one histidine per subunit. Arch Biochem Biophys 1983, 224(July (2)):579-586.
11. 2. Arch Biochem Biophys 1981, 212:411-416.
12. Borders C.L., Fridovich I. A comparison of the effects of cyanide, hydrogen peroxide, and phenylglyoxal on eucaryotic and procaryotic Cu, Zn superoxide dismutases. Arch Biochem Biophys 1985, 241(September (2)):472-476.
13. Yim M.B., Chock P.B., Stadtman E.R. Enzyme function of copper, zinc superoxide dismutase as a free radical generator. J Biol Chem 1993, 268(February (6)):4099-4105.
14. Harris E. Trace elements in health: a review of current issues 1983, Butterworthand Co. Publishers Ltd., Woburn, MA, USA.
15. Strausak D., Mercer J.F.B., Dieter H.H., Stremmel W., Multhaup G. Copper in disorders with neurological symptoms: Alzheimer's, Menkes, and Wilson diseases. Brain Res Bull 2001, 55:175-185.
16. Slivarichová D., Mitrová E., Ursínyová M., Uhnáková I., Koscová S., Wsólová L. Geographic accumulation of Creutzfeldt-Jakob disease in Slovakia - environmental metal imbalance as a possible cofactor. Cent Eur J Publ Health 2011, 19(September (3)):158-164.
17. Mitteregger G., Korte S., Shakarami M., Herms J., Kretzschmar H.A. Role of copper and manganese in prion disease progression. Brain Res 2009, 1292:155-164.
18. Hodak M., Chisnell R., Lu W., Bernholc J. Functional implications of multistage copper binding to the prion protein. Proc Natl Acad Sci USA 2009, 106:11576-11581.
19. Desai V., Kaler S.G. Role of copper in human neurological disorders. Am J Clin Nutr 2008, 88(September (3)):855S-858S.
20. Viles J.H., Klewpatinond M., Nadal R.C. Copper and the structural biology of the prion protein. Biochem Soc Trans 2008, 36(Pt 6):1288-1292.
21. Varela-Nallar L., González A., Inestrosa N.C. Role of copper in prion diseases: deleterious or beneficial?. Curr Pharm Des 2006, 12(20):2587-2595.
22. Quaglio E., Chiesa R., Harris D.A. Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform. J Biol Chem 2001, 276:11432.
23. Roger C.P., Diane E.G. Prions are copper-binding proteins. Trends Biochem Sci 1998, 23(6):197-198.
24. Yamamoto N., Kuwata k. Difference in redox behaviors between copper-binding octarepeat and nonoctarepeat sites in prion protein. J Biol Inorg Chem 2009, 14(November (8)):1209-1218.
25. Linder M.C., Hazegh-Azam M. Copper biochemistry and molecular biology. Am J Clin Nutr 1996, 63(May (5)):797S-811S.
26. Zhou B., Gitschier J. hCTR1: a human gene for copper uptake identified by complementation in yeast. Proc Natl Acad Sci USA 1997, 94:7481-7486.
27. Shim H., Harris Z.L. Genetic defects in copper metabolism. J Nutr 2003, 133(5 (Suppl. 1)):1527S-1531S.
28. Prousek J. Fenton chemistry in biology and medicine. Pure Appl Chem 2007, 79(12):2325-2338.
29. Liochev S.I., Fridovich I. The Haber-Weiss cycle - 70 years later: an alternative view. Redox Rep 2002, 7:55-57.
30. Speisky H., Gomez M., Burgos-Bravo F., Lopez-Alarcon C., Jullian C., Olea-Azar C., Aliaga M.E. Generation of superoxide radicals by copper-glutathione complexes: redox-consequences associated with their interaction with reduced glutathione. Bioorg Med Chem 2009, 17(5):1803-1810.
31. Aruoma O.I., Halliwell B., Gajewski E., Dizdaroglu M. Copper-ion-dependent damage to the bases in DNA in the presence of hydrogen peroxide. Biochem J 1991, 273(Pt 3):601-604.
32. Barbusinski K. Fenton reaction - controversy concerning the chemistry. Ecol Chem Eng 2009, 16:347-358.
33. Prousek J. Fenton reaction after a century. Chem List 1995, 89(1):11-21.
34. Moriwaki H., Osborne M.R., Phillips D.H. Effects of mixing metal ions on oxidative DNA damage mediated by a Fenton-type reduction. Toxicol In Vitro 2008, 22(February (1)):36-44.
35. Mattie M.D., Freedman J.H. Copper-inducible transcription: regulation by metal- and oxidative stress-responsive pathways. Am J Physiol Cell Physiol 2004, 286(February (2)):C293-C301.
36. Linder M.C. Biochemistry of copper 1991, Plenum Press, New York.
37. Jomova K., Valko M. Advances in metal-induced oxidative stress and human disease. Toxicology 2011, 283(May (2/3)):65-87.
38. Steinebach O.M., Wolterbeek H.T. Role of cytosolic copper, metallothionein and glutathione in copper toxicity in rat hepatoma tissue culture cells. Toxicology 1994, 92(September (1/3)):75-90.
39. El Hachimi K.H., Chaunu M.P., Brown P., Foncin J.F. Modifications of oligodendroglia cells in spongiform encephalopathies. Exp Neurol 1998, 154:23-30.
40. Zatta P., Cervellin D., Favarato M., Gerotto M., Mattiello G. Microelemental concentration in the ontogenesis of rat brain. Trace Elem Med 1994, 11:143-147.
41. Kiaei M., Bush A.I., Morrison B.M., Morrison J.H., Cherny R.A., Volitakis I., et al. Genetically decreased spinal cord copper concentration prolongs life in a transgenic mouse model of amyotrophic lateral sclerosis. J Neurosci 2004, 24(September (36)):7945-7950.
42. Kramer D.R., Llanos R.M., Mercer J.F.B. Molecular basis of copper transport: cellular and physiological functions of Menkes and Wilson disease proteins (ATP7A and ATP7B). Metal ions and neurodegenerative disorders 2003, 207-244. World Scientific, Singapore/London. P. Zatta (Ed.).
43. Paolo Z., Frank A. Copper deficiency and neurological disorders in man and animals. Brain Res Rev 2007, 54(April (1)):19-33.
44. Quian Y., Tiffany-Castiglioni E., Welsh J., Harris E.D. Copper efflux from murine microvascular cells requires expression of the Menkes disease Cu-ATPase. J Nutr 1998, 128:1276-1282.
45. Kodama H. Recent developments in Menkes disease. J Inherit Metab Dis 1993, 16(4):791-799.
46. Kumar N., Low P.A. Myeloneuropathy and anemia due to copper malabsorption. J Neurol 2004, 251(June (6)):747-749.
47. Bukau B., Deuerling E., Pfund C., Craig E.A. Getting newly synthesized proteins into shape. Cell 2000, 101:119-122.
48. Rosenzweig A.C. Copper delivery by metallochaperone protein. Acc Chem Res 2001, 34(February (2)):119-128.
49. Appel S.H., Zhao W., Beers D.R., Henkel J.S. The microglial-motoneuron dialogue in ALS. Acta Myol 2011, 30:4-8.
50. Pasinelli P., Brown R.H. Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat Rev Neurosci 2006, 7:710-723.
51. Czaplinski A., Yen A.A., Simpson E.P., Appel S.H. Slower disease progression and prolonged survival in contemporary patients with amyotrophic lateral sclerosis: is the natural history of amyotrophic lateral sclerosis changing?. Arch Neurol 2006, 63:1139-1143.
52. Maruyama H., Morino H., Ito H., Izumi Y., Kato H., Watanabe Y., et al. Mutations of optineurin in amyotrophic lateral sclerosis. Nature 2010, 465:223-226.
53. Turner M.R., Hardiman O., Benatar M., Brooks B.R., Chio A., de Carvalho M., et al. Controversies and priorities in amyotrophic lateral sclerosis. Lancet Neurol 2013, 12:310-322.
54. Fridovich I. Superoxide dismutases. Annu Rev Biochem 1975, 44(1):147-159.
55. Fitzmaurice P.S., Shaw I.C., Kleiner H.E., Miller R.T., Monks T.J., Lau S.S. Evidence for DNA damage in amyotrophic lateral sclerosis. Muscle Nerve 1996, 19:797-798.
56. Ferrante R.J., Browne S.E., Shinobu L.A., Bowling A.C., Baik M.J., MacGarvey U. Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis. J Neurochem 1997, 69:2064-2074.
57. Shibata N., Nagai R., Uchida K., Horiuchi S., Yamada S., Hirano A. Morphological evidence for lipid peroxidation and protein glycoxidation in spinal cords from sporadic amyotrophic lateral sclerosis patients. Brain Res 2001, 917:97-104.
58. Barber S.C., Shaw P.J. Oxidative stress in ALS: key role in motor neuron injury and therapeutic target. Free Radical Biol Med 2010, 48(5):629-641.
59. Barnham K.J., Masters C.L., Bush A.I. Neurodegenerative diseases and oxidative stress. Nat Rev Drug Discovery 2004, 3(3):205-214.
60. Yim M.B., Chock P.B., Stadtman E.R. Copper, zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide. Proc Natl Acad Sci 1990, 87(13):5006-5010.
61. Genova M.L., Pich M.M., Bernacchia A. The mitochondrial production of reactive oxygen species in relation to aging and pathology. Ann N Y Acad Sci 2004, 1011(1):86-100.
62. Saxena S., Cabuy E., Caroni P.A. Role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nat Neurosci 2009, 12(5):627-636.
63. Schulz J.B., Lindenau J., Seyfried J. Glutathione, oxidative stress and neurodegeneration. Eur J Biochem 2000, 267:4904-4911.
64. Beal M.F. Mitochondria and the pathogenesis of ALS. Brain 2000, 123:1291-1292.
65. Vielhaber S., Kunz D., Winkler K., Wiedemann F.R., Kirches E., Feistner H., et al. Mitochondrial DNA abnormalities in skeletal muscle of patients with sporadic amyotrophic lateral sclerosis. Brain 2000, 123:1339-1348.
66. Klivenyi P., Ferrante R.J., Matthews R.T., Bogdanov M.B., Klein A.M., Andreassen O.A., et al. Neuroprotective effects of creatine in a transgenic animal model of amyotrophic lateral sclerosis. Nat Med 1999, 5:347-350.
67. Shaw P.J., Eggett C.J. Molecular factors underlying selective vulnerability of motor neurons to neurodegeneration in amyotrophic lateral sclerosis. J Neurol 2000, 247(Suppl. 1):17-27.
68. Cleveland D.W., Rothstein J.D. From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat Rev Neurosci 2001, 2:806-819.
69. Rothstein J.D., Tsai G., Kuncl R.W. Abnormal excitatory amino acid metabolism in amyotrophic lateral sclerosis. Ann Neurol 1990, 28:18-25.
70. Spreux-Varoquaux O., Bensimon G., Lacomblez L., Salachas F., Pradat P.F., Le Forestier N., et al. Glutamate levels in cerebrospinal fluid in amyotrophic lateral sclerosis: a reappraisal using a new HPLC method with coulometric detection in a large cohort of patients. J Neurol Sci 2002, 193:73-78.
71. Rothstein J.D., Dykes-Hoberg M., Pardo C.A., Bristol L.A., Jin L., Kuncl R.W., et al. Knockout of glutamate transporters reveals a major role for astroglial transport in excitotoxicity and clearance of glutamate. Neuron 1996, 16:675-686.
72. Valentine J.S., Hart P.J. Misfolded Cu Zn SOD and amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 2003, 100(7):3617-3622.
73. Hart P.J. Pathogenic superoxide dismutase structure, folding, aggregation and turnover. Curr Opin Chem Biol 2006, 10(April (2)):131-138.
74. Rivera-Mancía S., Pérez-Neri I., Ríos C., Tristán-López L., Rivera-Espinosa L., Montes S. The transition metals copper and iron in neurodegenerative diseases. Chem Biol Interact 2010, 186(July (2)):184-199.
75. Estévez A.G., Crow J.P., Sampson J.B., Reiter C., Zhuang Y., Richardson G.J., et al. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science 1999, 286:2498-2500.
76. Levenson C.W. Trace metal regulation of neuronal apoptosis: from genes to behavior. Physiol Behav 2005, 86(October (3)):399-406.
77. Burstein E., Ganesh L., Dick R.D., van De Sluis B., Wilkinson J.C., Klomp L.W., et al. A novel role for XIAP in copper homeostasis through regulation of MURR1. EMBO J 2004, 23(January (1)):244-254.
78. Mufti A.R., Burstein E., Csomos R.A., Graf P.C., Wilkinson J.C., Dick R.D., et al. XIAP Is a copper binding protein deregulated in Wilson's disease and other copper toxicosis disorders. Mol Cell 2006, 21(March (6)):775-785.
79. Pasinelli P., Belford M.E., Lennon N., Bacskai B.J., Hyman B.T., Trotti D., et al. Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria. Neuron 2004, 43(July (1)):19-30.
80. Higgins C.M., Jung C., Ding H., Xu Z. Mutant Cu-Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS. J Neurosci 2002, 22(March (6)):RC215.
81. Okado-Matsumoto A., Fridovich I. Amyotrophic lateral sclerosis: a proposed mechanism. Proc Natl Acad Sci USA 2002, 99(June (13)):9010-9014.
82. Glenner G.G., Wong C.W. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovasculaar amyloid protein. Biochem Biophys Res Commun 1984, 120(May (3)):885-890.
83. Haass C., Schlossmacher M.G., Hung A.Y., Vigo-Pelfrey C., Mellon A., Ostaszewski B.L., et al. Amyloid beta-peptide is produced by cultured cells during normal metabolism. Nature 1992, 359(September (6393)):322-325.
84. Masters C.L., Multhaup G., Simms G., Pottgiesser J., Martins R.N., Beyreuther K. Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels. EMBO J 1985, 4(November (11)):2757-2760.
85. Masters C.L., Simms G., Weinman N.A., Multhaup G., McDonald B.L., Beyreuther K. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc Natl Acad Sci USA 1985, 82:4245-4249.
86. Roher A.E., Chaney M.O., Kuo Y.M., Webster S.D., Stine W.B., Haverkamp L.J., et al. Morphology and toxicity of Abeta-(1-42) dimer derived from neuritic and vascularamyloid deposits of Alzheimer's disease. J Biol Chem 1996, 271(August (34)):20631-20635.
87. Roher A.E., Palmer K.C., Yurewicz E.C., Ball M.J., Greenberg B.D. Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue. J Neurochem 1993, 61:1916-1926.
88. Seubert P., Vigo-Pelfrey C., Esch F., Lee M., Dovey H., Davis D., et al. Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids. Nature 1992, 359:325-327.
89. Shoji M., Golde T.E., Ghiso J., Cheung T.T., Estus S., Shaffer L.M., et al. Production of the Alzheimer amyloid beta protein by normal proteolytic processing. Science 1992, 258(October (5079)):126-129.
90. Vigo-Pelfrey C., Lee D., Keim P., Lieberburg I., Schenk D.B. Characterization of beta-amyloid peptide from human cerebrospinal fluid. J Neurochem 1993, 61:1965-1968.
91. Atwood C.S., Perry G., Zeng H., Kato Y., Jones W.D., Ling K.Q., et al. Copper mediates dityrosine cross-linking of Alzheimer's amyloid beta. Biochemistry 2004, 43(January (2)):560-568.
92. 2. J Biol Chem 2002, 277(October (43)):40302-40308.
93. Atwood C.S., Scarpa R.C., Huang X., Jones W.D., Fairlie D.P., Tanzi R.E., et al. Characterization of copper interactions with Alzheimer Aβ peptides identification of an attomole affinity copper binding site on Aβ1-42. J Neurochem 2000, 75:1219-1233.
94. White A.R., Reyes R., Mercer J.F., Camakaris J., Zheng H., Bush A.I., et al. Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice. Brain Res 1999, 842(September (2)):439-444.
95. Lovell M.A., Robertson J.D., Teesdale W.J., Campbell J.L., Markesbery W.R. Copper, iron and zinc in Alzheimer's disease senile plaques. J Neurol Sci 1998, 158(July (1)):47-52.
96. Vassiliev V., Harris Z.L., Zatta P. Ceruloplasmin in neurodegenerative diseases. Brain Res Brain Res Rev 2005, 49(November (3)):633-640.
97. Deibel M.A., Ehmann W.D., Markesbery W.R. Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: possible relation to oxidative stress. J Neurol Sci 1996, 143(November (1/2)):137-142.
98. Schlief M.L., Craig A.M., Gitlin J.D. NMDA receptor activation mediates copper homeostasis in hippocampal neurons. J Neurosci 2005, 25(January (1)):239-246.
99. Mawuenyega K.G., Sigurdson W., Ovod V., Munsell L., Kasten T., Morris J.C., et al. Decreased clearance of CNS beta-amyloid in Alzheimer's disease. Science 2010, 330(December (6012)):1774.
100. Fonteh A.N., Harrington R.J., Tsai A., Liao P., Harrington M.G. Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids 2007, 32(February (2)):213-224.
101. Chung R.S., Howells C., Eaton E.D., Shabala L., Zovo K., Palumaa P., et al. The native copper- and zinc-binding protein metallothionein blocks copper-mediated A beta aggregation and toxicity in rat cortical neurons. PLoS ONE 2010, 5(August (8)):e12030.
102. Snyder E.M., Nong Y., Almeida C.G., Paul S., Moran T., Choi E.Y., et al. Regulation of NMDA receptor trafficking by amyloid-beta. Nat Neurosci 2005, 8(August (8)):1051-1058.
103. Menkes J.H., Alter M., Steigleder G.K., Weakley D.R., Sung J.H. A sex-linked recessive disorder with growth retardation, peculiar hair, and focal cerebral and cerebellar degeneration. Pediatrics 1962, 29(May):764-779.
104. Kaler S.G. Menkes disease. Adv Pediatr 1994, 41:263-304.
105. Danks D.M., Campbell P.E., Walker-Smith J., Stevens B.J., Gillespie J.M., Blomfield J., et al. Menkes' kinky hair syndrome. Lancet 1972, 1(May (7760)):1100-1102.
106. Danks D.M., Cartwright E., Stevens B.J., Townley R.R. Menkes' kinky hair disease: further definition of the defect in copper transport. Science 1973, 179(March (4078)):1140-1142.
107. Berg B.O. The neurologic examination. Child neurology: a clinical manual 1994, 1-26. JB Lippencott, Philadelphia. B.O. Berg (Ed.).
108. Cox D.W., Moore S.D. Copper transporting P-type ATPases and human disease. J Bioenerg Biomembr 2002, 34(October (5)):333-338.
109. Rinaldi A.C. Meeting report: copper research at the top. Biometals 2000, 13:9-13.
110. Kaler S.G. Metabolic and molecular bases of Menkes disease and occipital horn syndrome. Pediatr Dev Pathol 1998, 1:85-98.
111. Liu P.C., McAndrew P.E., Kaler S.G. Rapid and robust screening of the Menkes disease/occipital horn syndrome gene. Genet Test 2002, 6(Winter (4)):255-260.
112. Kaler S.G., Buist N.R.M., Holmes C.S., Goldstein D.S., Miller R.C., Gahl W.A. Early copper therapy in classic Menkes disease patients with a novel splicing mutation. Ann Neurol 1995, 38:921-928.
113. Kaler S.G., Das S., Levinson B., Goldstein D.S., Holmes C.S., Patronas N.J., et al. Successful early copper therapy in Menkes disease associated with a mutant transcript containing a small in-frame deletion. Biochem Mol Med 1996, 57:37-46.
114. Kaler S.G. Menkes disease mutations and response to early copper histidine treatment. Nat Genet 1996, 13:21-22.
115. Liu P.C., Chen Y.W., Centano J., Quesado M., Lem K.E., Kaler S.G. Down regulation of myelination, energy, and translational genes in Menkes disease brain. Mol Genet Metab 2005, 85:291-300.
116. Kaler S.G., Holmes C.S., Goldstein D.S., Tang J., Godwin S.C., Donsante A., et al. Neonatal diagnosis and treatment of Menkes disease. N Engl J Med 2008, 358:605-614.
117. Kaler S.G., Gallo L.K., Proud V.K., Percy A.K., Mark Y., Segal N.A., et al. Occipital horn syndrome and a mild Menkes phenotype associated with splice site mutations at the MNK locus. Nat Genet 1994, 8:195-202.
118. Chelly J., Tumer Z., Tonnesen T., Petterson A., Ishikawa-Brush Y., Tommerup N., et al. Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein. Nat Genet 1993, 3:14-19.
119. Mercer J.F., Livingston J., Hall B., Paynter J.A., Begy C., Chandrasekharappa S., et al. Isolation of a partial candidate gene for Menkes disease by positional cloning. Nat Genet 1993, 3:20-25.
120. Vulpe C., Levinson B., Whitney S., Packman S., Gitschier J. Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper transporting ATPase. Nat Genet 1993, 3:7-13.
121. Arnesano F., Banci L., Bertini I., Ciofi-Baffoni S., Molteni E., Huffman D.L., et al. Metallochaperones and metal-transporting ATPases: a comparative analysis of sequences and structures. Genome Res 2002, 12(February (2)):255-271.
122. Tumer Z., Moller L.B., Horn N. Mutation spectrum of ATP7A, the gene defective in Menkes disease. Adv Exp Med Biol 1999, 448:83-95.
123. Hsi G., Cox D.W. A comparison of the mutation spectra of Menkes disease and Wilson disease. Human Genet 2004, 114:165-172.
124. Govindaraju M., Shekar H.S. Role of copper in the clinics of neurological disorders. IJRPC 2011, 1(3).
125. Culotta V.C., Gitlin J.D. The metabolic molecular basis of inherited disease 2001, 3115-3118. McGraw-Hill Companies, New York, NY. 8th ed.
126. Suzuki N., Cheung T.T., Cai X.D., Odaka A., Otvos L., Eckman C., et al. An increased percentage of long amyloid betaprotein secreted by familial amyloid beta protein precursor (beta APP717) mutants. Science 1994, 264(May (5163)):1336-1340.
127. Claire J.S. The copper-amyloid-beta-peptide complex of Alzheimer's disease: affinity, structure, fibril formation and toxicity 2010, (Ph.D. thesis), University of London.
128. Lesne S., Ali C., Gabriel C., Croci N., MacKenzie E.T., Glabe C.G., et al. NMDAreceptor activation inhibits alpha-secretase and promotes neuronal amyloid beta production. J Neurosci 2005, 25:9367-9377.
129. Meloni G., Sonois V., Delaine T., Guilloreau L., Gillet A., Teissié J., et al. Metal swap between Zn7-metallothionein-3 andamyloid-beta-Cu protects against amyloid-beta toxicity. Nat Chem Biol 2008, 4(June (6)):366-372.
130. Kohen R., Yamamoto Y., Cundy K.C., Ames B.N. Antioxidant activity of carnosine, homocarnosine, and anserine present in muscle and brain. Proc Natl Acad Sci USA 1988, 85(May (9)):3175-3179.
131. Horning M.S., Blakemore L.J., Trombley P.Q. Endogenous mechanisms of neuroprotection: role of zinc, copper, and carnosine. Brain Res 2000, 852(January (1)):56-61.
132. Lanza V., Bellia F., D'Agata R., Grasso G., Rizzarelli E., Vecchio G. New glycoside derivatives of carnosine and analogs resistant to carnosinase hydrolysis: synthesis and characterization of their copper(II) complexes. J Inorg Biochem 2011, 105(February (2)):181-188.
133. Urbanc B., Cruz L., Le R., Sanders J., Ashe K.H., Duff K., et al. Neurotoxic effects of thioflavin positive amyloid deposits in transgenic mice and Alzheimer's disease. Proc Natl Acad Sci USA 2002, 99(October (22)):13990-13995.
134. Meyer-Luehmann M., Spires-Jones T.L., Prada C., Garcia-Alloza M., de Calignon A., Rozkalne A., et al. Rapid appearance and local toxicity of amyloid-beta plaques in a mouse model of Alzheimer's disease. Nature 2008, 451(February (7179)):720-724.
135. Horn N., Tonnesen T., Tulmer Z. Menkes disease: an X-linked neurological disorder of the copper metabolism. Brain Pathol 1992, 2:351-362.
136. Danks D.M. Disorders of copper transport. The metabolic basis of inherited disease 1995, 2211-2235. McGraw-Hill, New York. J.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.).
137. Keydorn K., Damsgaard E., Horn N., Mikkelsen M., Tygstrup I., Vestemark S., et al. Extra-hepatic storage of copper: a male foetus suspected of Menkes' disease. Humangenetik 1975, 29(2):171-175.
138. Horn N., Heydorn K., Damsgaard E., Tygstrup I., Vestermark S. Is Menkes syndrome a copper storage disorder?. Clin Genet 1978, 14(September (3)):186-187.
139. Lutsenko S., LeShane E.S., Shinde U. Biochemical basis of regulation of human copper-transporting ATPases. Arch Biochem Biophys 2007, 463(July (2)):134-148.
140. Palmgren M.G., Axelsen K.B. Evolution of P-type ATPases. Biochim Biophys Acta 1998, 1365(June (1/2)):37-45.
141. Tumer Z., Møller L.B. Menkes disease. Eur J Human Genet 2010, 18:511-518.
142. Yamaguchi Y., Heiny M.E., Suzuki M., Gitlin J.D. Biochemical characterization and intracellular localization of the Menkes disease protein. Proc Natl Acad Sci USA 1996, 93:14030-14035.
143. Hung I.H., Suzuki M., Yamaguchi Y., Yuan D.S., Klausner R.D., Gitlin J.D. Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae. J Biol Chem 1997, 272:21461-21466.
144. Petris M.J., Mercer J.F., Culvenor J.G., Lockhart P., Gleeson P.A., Camakaris J. Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking. EMBO J 1996, 156084-156095.
145. Harada M., Sakisaka S., Terada K., Kimura R., Kawaguchi T., Koga H., et al. Role of ATP7B in biliary copper excretion in a human hepatoma cell line and normal rat hepatocytes. Gastroenterology 2000, 118:921-928.
146. Harada M., Kawaguchi T., Kumemura H., Terada K., Ninomiya H., Taniguchi E., et al. The Wilson disease protein ATP7B resides in the late endosomes with Rab7 and the Niemann-Pick C1 protein. Am J Pathol 2005, 166:499-510.
147. Huster D., Hoppert M., Lutsenko S., Zinke J., Lehmann C., Mossner J., et al. Defective cellular localization of mutant ATP7B in Wilson's disease patients and hepatoma cell lines. Gastroenterology 2003, 124:335-345.
148. Forbes J.R., Cox D.W. Copper-dependent trafficking of Wilson disease mutant ATP7B proteins. Hum Mol Genet 2000, 9:1927-1935.
149. Roelofsen H., Wolters H., Van Luyn M.J., Miura N., Kuipers F., Vonk R.J. Copper induced apical trafficking of ATP7B in polarized hepatoma cells provides a mechanism for biliary copper excretion. Gastroenterology 2000, 119:782-793.
150. Schaefer M., Roelofsen H., Wolters H., Hofmann W.J., Muller M., Kuipers F., et al. Localization of the Wilson's disease protein in human liver. Gastroenterology 1999, 117:1380-1385.
151. Schaefer M., Hopkins R.G., Failla M.L., Gitlin J.D. Hepatocyte-specific localization and copper-dependent trafficking of the Wilson's disease protein in the liver. Am J Physiol 1999, 276:G639-G646.
152. Mercer J.F., Barnes N., Stevenson J., Strausak D., Llanos R.M. Copper-induced trafficking of the Cu-ATPases: a key mechanism for copper homeostasis. Biometals 2003, 16:175-184.
153. La Fontaine S., Theophilos M.B., Firth S.D., Gould R., Parton R.G., Mercer J.F. Effect of the toxic milk mutation (tx) on the function and intracellular localization of Wnd, the murine homologue of the Wilson copper ATPase. Hum Mol Genet 2001, 10:361-370.
154. Guo Y., Nyasae L., Braiterman L.T., Hubbard A.L. NH2-terminal signals in ATP7B Cu-ATPase mediate its Cu-dependent anterograde traffic in polarized hepatic cells. Am J Physiol Gastrointest Liver Physiol 2005, 289:G904-G916.
155. Lutsenko S., Cooper M.J. Localization of the Wilson's disease protein product to mitochondria. Proc Natl Acad Sci USA 1998, 95:6004-6009.
156. Petris M.J., Mercer J.F. The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal. Hum Mol Genet 1999, 8:2107-2115.
157. Nyasae L., Bustos R., Braiterman L., Eipper B., Hubbard A. Dynamics of endogenous ATP7A (Menkes protein) in intestinal epithelial cells: copperdependent redistribution between two intracellular sites. Am J Physiol Gastrointest Liver Physiol 2007, 292:G1181-G1194.
158. Greenough M., Pase L., Voskoboinik I., Petris M.J., O'Brien A.W., Camakaris J. Signals regulating trafficking of Menkes (MNK; ATP7A) copper-translocating Ptype ATPase in polarized MDCK cells. Am J Physiol Cell Physiol 2004, 287:C1463-C1471.
159. Monty J.F., Llanos R.M., Mercer J.F., Kramer D.R. Copper exposure induces trafficking of the Menkes protein in intestinal epithelium of ATP7A transgenic mice. J Nutr 2005, 135:2762-2766.
160. Ravia J.J., Stephen R.M., Ghishan F.K., Collins J.F. Menkes copper ATPase (Atp7a) is a novel metal-responsive gene in rat duodenum, and immunoreactive protein is present on brush-border and basolateral membrane domains. J Biol Chem 2005, 280:36221-36227.
161. Ke B.X., Llanos R.M., Wright M., Deal Y., Mercer J.F. Alteration of copper physiology in mice overexpressing the human Menkes protein ATP7A. Am J Physiol Regul Integr Comp Physiol 2006, 290:R1460-R1467.
162. Cater M.A., La Fontaine S., Shield K., Deal Y., Mercer J.F. ATP7B mediates vesicular sequestration of copper: insight into biliary copper excretion. Gastroenterology 2006, 130:493-506.
163. Ambrosini L., Mercer J.F. Defective copper-induced trafficking and localization of the Menkes protein in patients with mild and copper-treated classical Menkes disease. Hum Mol Genet 1999, 8:1547-1555.
164. Kim B.E., Smith K., Petris M.J. A copper treatable Menkes disease mutation associated with defective trafficking of a functional Menkes copper ATPase. J Med Genet 2003, 40:290-295.
165. Forbes J.R., Cox D.W. Functional characterization of missense mutations in ATP7B: Wilson disease mutation or normal variant?. Am J Hum Genet 1998, 63:1663-1674.
166. de Bie P., Muller P., Wijmenga C.L., Klomp W.J. Molecular pathogenesis of Wilson and Menkes disease: correlation of mutations with molecular defects and disease phenotypes. J Med Genet 2007, 44:673-688.
167. Bruijn L.I., Becher M.W., Lee M.K., Anderson K.L., Jenkins N.A., Copeland N.G., et al. ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 1997, 18:327-338.
168. Howland D.S., Liu J., She Y., Goad B., Maragakis N.J., Kim B., et al. Focal loss of the glutamate transporter EAAT2 in a transgenic rat model of SOD1 mutant mediated amyotrophic lateral sclerosis (ALS). Proc Natl Acad Sci USA 2002, 99:1604-1609.
169. Trotti D., Rolfs A., Danbolt N.C., Brown R.H., Hediger M.A. SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter. Nat Neurosci 1999, 2:427-433.
170. Guo H., Lai L., Butchbach M.E., Stockinger M.P., Shan X., Bishop G.A., et al. Increased expression of the glial glutamate transporter EAAT2 modulates excitotoxicity and delays the onset but not the outcome of ALS in mice. Hum Mol Genet 2003, 12:2519-2532.
171. Rothstein J.D., Patel S., Regan M.R., Haenggeli C., Huang Y.H., Bergles D.E., et al. Beta-lactam antibiotics offer neuroprotection by increasing glutamate transporter expression. Nature 2005, 433:73-77.
172. Rothstein J.D., Van Kammen M., Levey A.I., Martin L.J., Kuncl R.W. Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis. Ann Neurol 1995, 38:73-84.
173. Xu Z., Cork L.C., Griffin J.W., Cleveland D.W. Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease. Cell 1993, 73:23-33.
174. Lee M.K., Marszalek J.R., Cleveland D.W. A mutant neurofilament subunit causes massive, selective motor neuron death: implications for the pathogenesis of human motor neuron disease. Neuron 1994, 13:975-988.
175. Couillard-Després S., Zhu Q., Wong P.C., Price D.L., Cleveland D.W., Julien J.P. Protective effect of neurofilament heavy gene overexpression in motor neuron disease induced by mutant superoxide dismutase. Proc Natl Acad Sci USA 1998, 95:9626-9630.
176. Nguyen M.D., Lariviere R.C., Julien J.P. Deregulation of Cdk5 in a mouse model of ALS: toxicity alleviated by perikaryal neurofilament inclusions. Neuron 2001, 30:135-147.
177. Williamson T.L., Cleveland D.W. Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons. Nat Neurosci 1999, 2:50-56.
178. Puls I., Jonnakuty C., LaMonte B.H., Holzbaur E.L., Tokito M., Mann E., et al. Mutant dynactin in motor neuron disease. Nat Genet 2003, 33:455-456.