Publish in OALib Journal
ISSN: 2333-9721
APC: Only $99

Paper Submission

Views	Downloads

Relative Articles
Mitochondrial Cytochrome c Oxidase Subunit 1 Sequence Variation in Prostate Cancer
Cytochrome C Oxidase Subunit-1(COX1) Gene in Tilapia (Oreochromis Niloticus): its Cloning and Characterization
Reconstructing Mammalian Phylogenies: A Detailed Comparison of the Cytochrome b and Cytochrome Oxidase Subunit I Mitochondrial Genes
Molecular characterization of Echinococcus granulosusfrom Peru by sequencing of the mitochondrial cytochrome C oxidase subunit 1 gene
The Characteristics of Cytochrome C Oxidase Gene Subunit I in Wild Silkmoth Cricula trifenestrata Helfer and Its Evaluation for Species Marker
Genetic Differentiation of the Mitochondrial Cytochrome Oxidase c Subunit I Gene in Genus Paramecium (Protista, Ciliophora)
Exploring the Utility of Partial Cytochrome c Oxidase Subunit 1 for DNA Barcoding of Gobies
Population structure of the Monocelis lineata (Proseriata, Monocelididae) species complex assessed by phylogenetic analysis of the mitochondrial Cytochrome c Oxidase subunit I (COI) gene
Ecological and Genetic Relationship of Chironomus circumdatus (Diptera, Chironomidae) From Mitochondrial Cytochrome Oxidase Subunit I in Chiang Mai Province, Northern Thailand
The biometric and cytochrome oxidase subunit I (COI) gene sequence analysis of syngnathus abaster (Teleostei: Syngnathidae) in Caspian sea
More...

PLOS ONE 2012

Amyloid-β Peptide Binds to Cytochrome C Oxidase Subunit 1

DOI: 10.1371/journal.pone.0042344

Luis Fernando Hernandez-Zimbron, Jose Luna-Mu？oz, Raul Mena, Ricardo Vazquez-Ramirez, Carlos Kubli-Garfias, David H. Cribbs, Karen Manoutcharian, Goar Gevorkian

Full-Text Cite this paper Add to My Lib

Abstract:

Extracellular and intraneuronal accumulation of amyloid-beta aggregates has been demonstrated to be involved in the pathogenesis of Alzheimer's disease (AD). However, the precise mechanism of amyloid-beta neurotoxicity is not completely understood. Previous studies suggest that binding of amyloid-beta to a number of macromolecules has deleterious effects on cellular functions. Mitochondria were found to be the target for amyloid-beta, and mitochondrial dysfunction is well documented in AD. In the present study we have shown for the first time that Aβ 1–42 bound to a peptide comprising the amino-terminal region of cytochrome c oxidase subunit 1. Phage clone, selected after screening of a human brain cDNA library expressed on M13 phage and bearing a 61 amino acid fragment of cytochrome c oxidase subunit 1, bound to Aβ 1–42 in ELISA as well as to Aβ aggregates present in AD brain. Aβ 1–42 and cytochrome c oxidase subunit 1 co-immunoprecipitated from mitochondrial fraction of differentiated human neuroblastoma cells. Likewise, molecular dynamics simulation of the cytochrome c oxidase subunit 1 and the Aβ 1–42 peptide complex resulted in a reliable helix-helix interaction, supporting the experimental results. The interaction between Aβ 1–42 and cytochrome c oxidase subunit 1 may explain, in part, the diminished enzymatic activity of respiratory chain complex IV and subsequent neuronal metabolic dysfunction observed in AD.

References

[1]	Masters CL, Simms G, Weinmann NA, Multhaup G, McDonald BL, et al. (1985) Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc Natl Acad Sci U S A 82: 4245–4249.
[2]	Walsh DM, Selkoe DJ (2004) Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 44: 181–193.
[3]	Wirths O, Multhaup G, Bayer TA (2004) A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide - the first step of a fatal cascade. J Neurochem 91: 513–520.
[4]	Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8: 101–112.
[5]	LaFerla F, Green KN, Oddo S (2007) Intracellular amyloid-β in Alzheimer's disease. Nat Rev Neurosci 8: 499–509.
[6]	Gouras GK, Tampellini D, Takahashi RH, Capetillo-Zarate E (2010) Intraneuronal beta-amyloid accumulation and synapse pathology in Alzheimer's disease. Acta Neuropathol 119: 523–541.
[7]	Ballard C, Gauthier S, Corbett A, Brayne C, Aarsland D, et al. (2011) Alzheimer's disease. The Lancet 377: 1019–1031.
[8]	Ferreira ST, Klein WL (2011) The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer's disease. Neurobiol Learn Mem 96: 529–543.
[9]	Butterfield DA, Boyd-Kimball D (2004) Amyloid beta-peptide (1–42) contributes to the oxidative stress and neurodegeneration found in Alzheimer disease brain. Brain Pathol 14: 426–432.
[10]	Huang X, Moir RD, Tanzi RE, Bush AI, Rogers JT (2004) Redox-active metals, oxidative stress, and Alzheimer's disease pathology. Ann NY Acad Sci 1012: 153–163.
[11]	Blurton-Jones M, LaFerla FM (2006) Pathways by which Abeta facilitates tau pathology. Curr Alzheimer Res 3: 437–448.
[12]	Demuro A, Parker I, Stutzmann GE (2010) Calcium signaling and amyloid toxicity in Alzheimer disease. J Biol Chem 285: 12463–12468.
[13]	Frautschy SA, Cole GM (2010) Why pleiotropic interventions are needed for Alzheimer's disease. Mol Neurobiol 41: 392–409.
[14]	Bossy-Wetzel E, Schwarzenbacher R, Lipton SA (2004) Molecular pathways to neurodegeneration. Nat Med 10: S2–S9.
[15]	Canevari L, Abramov AY, Duchen MR (2004) Toxicity of amyloid β peptide: tales of calcium, mitochondria, and oxidative stress. Neurochem Res 29: 637–650.
[16]	Tillement L, Lecanu L, Papadopoulos V (2011) Alzheimer's disease: effects of β-amyloid on mitochondria. Mitochondrion 11: 13–21.
[17]	Eckert A, Schmitt K, Gotz J (2011) Mitochondria dysfunction – the beginning of the end in Alzheimer's disease? Separate and synergistic modes of tau and amyloid-b toxicity. Alzheimers Res Ther 3: 15.
[18]	Moreira PI, Santos MS, Moreno A, Rego AC, Oliveira C (2002) Effect of amyloid beta-peptide on permeability transition pore: a comparative study. J Neurosci Res 69: 257–267.
[19]	Casley CS, Canevari L, Land JM, Clark JB, Sharpe MA (2002) β-Amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J Neurochem 80: 91–100.
[20]	Tillement L, Lecanu L, Yao W, Greeson J, Papadopoulos V (2006) The spirostenol (22R, 25R)-20α-spirost-5-en-3β-yl hexanoate blocks mitochondrial uptake of Aβ in neuronal cells and prevents Aβ-induced impairment of mitochondrial function. Steroids 71: 725–735.
[21]	Wang X, Su B, Lee H-g, Li X, Perry G, et al. (2009) Impaired balance of mitochondrial fission and fussion in Alzheimer's disease. J Neurosci 29: 9090–9103.
[22]	Santos RX, Correia SC, Wang X, Perry G, Smith MA, et al. (2010) A synergistic dysfunction of mitochondrial fission/fusion dynamics and miitophagy in Alzheimer's disease. J Alzheimers Dis 20: S401–S412.
[23]	Hauptmann S, Scherping I, Drose S, Brandt U, Schulz KL, et al. (2009) Mitochondrial dysfunction: an early event in Alzheimer pathology accumulates with age in AD transgenic mice. Neurobiol Aging 30: 1574–1586.
[24]	Canevari L, Clark JB, Bates TE (1999) Beta-amyloid fragment 25–35 selectively decreases complex IV activity in isolated mitochondria. FEBS Lett 457: 131–134.
[25]	Crouch PJ, Blake R, Duce JA, Ciccotosto GD, Li QX, et al. (2005) Copper-dependent inhibition of human cytochrome c oxidase by a dimeric comformer of amyloid-β 1–42. J Neurosci 25: 672–679.
[26]	Cassano T, Serviddio G, Gaetani S, Romano A, Dipasquale P, et al. (2011) Glutamatergic alterations and mitochondrial impairment in a murine model of Alzheimer disease. Neurobiol Aging doi:10.1016/j.neurobiolaging.2011.09.021？.
[27]	Lustbader JW, Cirilli M, Lin C, Xu HW, Takuma K, et al. (2004) ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease. Science 304: 448–452.
[28]	Yan SD, Fu J, Soto C, Chen X, Zhu H, et al. (1997) An intracellular protein that binds amyloid-β peptide and mediates neurotoxicity in Alzheimer's disease. Nature 389: 689–695.
[29]	Takuma K, Yao J, Huang J, Xu H, Chen X, et al. (2005) ABAD enhances A beta-induced cell stress via mitochondrial dysfunction. FASEB J 19: 597–598.
[30]	Yan SD, Stern DM (2005) Mitochondrial dysfunction and Alzheimer's disease: role of amyloid-beta peptide alcohol dehydrogenase (ABAD). Int J Exp Pathol 86: 161–171.
[31]	Yao J, Du H, Yan S, Fang F, Wang C, et al. (2011) Inhibition of amyloid-beta (Aβ) peptide-binding alcohol dehydrogenase-Aβ interaction reduces Aβ accumulation and improves mitochondrial function in a mouse model of Alzheimer's disease. J Neurosci 31: 2313–2320.
[32]	Munguia ME, Govezensky T, Martinez R, Manoutcharian K, Gevorkian G (2006) Identification of amyloid-beta 1–42 binding protein fragments by screening of a human brain cDNA library. Neurosci Lett 397: 79–82.
[33]	Gevorkian G, Gonzalez-Noriega A, Acero G, Ordo？ez J, Michalak C, et al. (2008) Amyloid-β peptide binds to microtubule-associated protein 1B (MAP1B). Neurochem Int 52: 1030–1036.
[34]	Medecigo M, Manoutcharian K, Vasilevko V, Govezensky T, Munguia ME, et al. (2010) Novel amyloid-beta specific scFv and VH antibody fragments from human and mouse phage display antibody libraries. J Neuroimmunol 223: 104–114.
[35]	McKhann G, Drachman D, Folstein M, Katzman R, Price D, et al. (1984) Clinical diagnosis of Alzheimer's disease: report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human services Task Force on Alzheimer's Disease. Neurology 34: 939–944.
[36]	Luna-Mu？oz J, Peralta-Ramirez J, Chavez-Macias L, Harrington CR, Wischik CM, et al. (2008) Thiazin red as a neuropathological toll for the rapid diagnosis of Alzheimer's disease in tissue imprints. Acta Neuropathol 116: 507–515.
[37]	Perez-Garmendia R, Ibarra-Bracamontes V, Vasilevko V, Luna-Munoz J, Mena R, et al. (2010) Anti-11 [E]-pyroglutamate-modified amyloid β antibodies cross-react with other pathological Aβ species: relevante for immunotherapy. J Neuroimmunol 229: 248–255.
[38]	Coles M, Bicknell W, Watson AA, Fairlie DP, Craik DJ (1998) Solution Structure of Amyloid-β Peptide (1–40) in Water-Micelle Environment. Is the Membrane-Spanning Domain Where We Think It Is? Biochemistry 37: 11064–11077.
[39]	HyperChem Professional release 8.0., 2007. Molecular Modeling System. Hypercube Inc.
[40]	Muramoto K, Ohtab K, Shinzawa-Itoh K, Kandaa K, Taniguchi M (2010) Bovine Cytochrome C Oxidase Structures Enable O2 Reduction with Minimization of Reactive Oxygen and Provide a Proton-Pumping Gate. Proc Natl Acad Sci U.S.A 107: 7740–7745.
[41]	Hess B, Bekker H, Berendsen HJC, Fraajie JGEM (1997) LINCS: A Linear Constraint Solver Molecular Simulations. J Comput Chem 18: 1463–1472.
[42]	Van der Spoel D, Lindahl E, Hess B, Groenhof G, Mark AE, et al. (2005) GROMACS: Fast, Flexible, and Free. J Comp Chem 26: 1701–1718.
[43]	MacKerell AD Jr, Bashford D, Bellott M, Dunbrack RL Jr, Evanseck JD, et al. (1998) All-atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins. J Phys Chem B 102: 3586–3616.
[44]	Van der Spoel D, Lindahl E, Hess B, Groenhof G, Mark AE, Berendsen HJC (2005) GROMACS: Fast, flexible, and free. J Comp Chem 26: 1701–1718.
[45]	Humphrey W, Dalke A, Schulten K (1996) VMD - Visual Molecular Dynamics. J Mol Graph 14: 33–38.
[46]	Asami-Odaka A, Ishibashi Y, Kikuchi T, Kitada C, Suzuki N (1995) Long amyloid b-protein secreted from wild-type human neuroblastoma IMR-32 cells. Biochemistry 34: 10272–10278.
[47]	Aleardi AM, Benard G, Augereau O, Malgat M, Talbot JC, et al. (2005) Gradual alteration of mitochondrial structure and function by β-amyloids: importance of membrane viscosity changes, energy deprivation, reactive oxygen species production, and cytochrome c release. J Bioenerg Biomembr 37: 207–225.
[48]	Caspersen C, Wang N, Yao J, Sosunov A, Chen X, et al. (2005) Mitochondrial Abeta: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease. FASEB J 19: 2040–2041.
[49]	Manczak M, Anekonda TS, Henson E, Park BS, Quinn J, et al. (2006) Mitochondria are a direct site of Ab accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum Mol Genet 15: 1437–1449.
[50]	Hansson Petersen CA, Alikhani N, Behbahani H, Wiehager B, Pavlov PF, et al. (2008) The amyloid beta-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae. Proc Natl Acad Sci U S A 105: 13145–13150.
[51]	Singh P, Suman S, Chandna S, Das TK (2009) Possible role of amyloid-beta, adenine nucleotide translocase and cyclophilin-D interaction in mitochondrial dysfunction of Alzheimer's disease. Bioinformation 3: 440–445.
[52]	Du H, Guo L, Zhang W, Rydzewska M, Yan S (2011) Cyclophilin D deficiency improves mitochondrial function and learning and memory in aging Alzheimer disease mouse model. Neurobiol Aging 32: 398–406.
[53]	Pavlov PF, Wiehager B, Sakai J, Frykman S, Behbahani H, et al. (2011) Mitochondrial g-secretase participates in the metabolism of mitochondria-associated amyloid precursor protein. FASEB J 25: 78–88.
[54]	Blass JP, Sheu RK, Gibson GE (2000) Inherent abnormalities in energy metabolism in Alzheimer disease. Interaction with cerebrovascular compromise. Ann N Y Acad Sci 903: 204–221.
[55]	Yao J, Irwin R, Zhao L, Nilsen J, Hamilton RT, et al. (2009) Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease. Proc Natl Acad Sci U S A 106: 14670–14675.
[56]	Du H, Guo L, Yan S, Sosunov AA, McKhann GM, et al. (2010) Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model. Proc Natl Acad Sci U S A 107: 18670–18675.
[57]	Dragicevic N, Mamcarz M, Zhu Y, Buzzeo R, Tan J, et al. (2010) Mitochondrial amyloid-beta levels are associated Ruth the extent of mitochondrial dysfunction in different brain regions and the degree of cognitive impairment in Alzheimer's transgenic mice. J Alzheimers Dis 20: S535–S550.
[58]	Cardoso SM, Santos S, Swerdlow RH, Oliveira CR (2001) Functional mitochondia are required for amyloid b-mediated neurotoxicity. FASEB J 15: 1439–1441.
[59]	Fukui H, Diaz F, Garcia S, Moraes CT (2007) Cytochrome c oxidase deficiency in neurons decreases both oxidative stress and amyloid formation in a Mouse model of Alzheimer's disease. Proc Natl Acad Sci U S A 104: 14163–14168.
[60]	Yoshikawa S, Shinzawa-Itoh K, Nakashima R, Yaono R, Yamashita E, et al. (1998) Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Science 280: 1723–1729.

Full-Text

comments powered by Disqus

Contact Us

service@oalib.com

QQ:3279437679

微信:OALib Journal