Amyloid-β and tau — a toxic pas de deux in Alzheimer's disease (original) (raw)

• Citron, M. Strategies for disease modification in Alzheimer's disease. Nature Rev. Neurosci. 5, 677–685 (2004).
  Article CAS Google Scholar
• Brunden, K. R., Trojanowski, J. Q. & Lee, V. M. Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies. Nature Rev. Drug Discov. 8, 783–793 (2009).
  Article CAS Google Scholar
• Querfurth, H. W. & LaFerla, F. M. Alzheimer's disease. N. Engl. J. Med. 362, 329–344 (2010).
  Article CAS Google Scholar
• Cairns, N. J. et al. Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration. Acta Neuropathol. 114, 5–22 (2007).
  Article Google Scholar
• Braak, H. & Braak, E. Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol. Aging 16, 271–278; discussion 278–284 (1995).
  Article CAS Google Scholar
• Selkoe, D. J. Alzheimer's disease is a synaptic failure. Science 298, 789–791 (2002).
  Article CAS Google Scholar
• Bertram, L. & Tanzi, R. E. The genetic epidemiology of neurodegenerative disease. J. Clin. Invest. 115, 1449–1457 (2005).
  Article CAS Google Scholar
• Ballatore, C., Lee, V. M. & Trojanowski, J. Q. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nature Rev. Neurosci. 8, 663–672 (2007).
  Article CAS Google Scholar
• Götz, J. & Ittner, L. M. Animal models of Alzheimer's disease and frontotemporal dementia. Nature Rev. Neurosci. 9, 532–544 (2008).
  Article Google Scholar
• Frost, B. & Diamond, M. I. Prion-like mechanisms in neurodegenerative diseases. Nature Rev. Neurosci. 11, 155–159 (2010).
  Article CAS Google Scholar
• Hardy, J. & Selkoe, D. J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353–356 (2002).
  Article CAS Google Scholar
• Sisodia, S. S. & St George-Hyslop, P. H. γ-Secretase, notch, Aβ and Alzheimer's disease: where do the presenilins fit in? Nature Rev. Neurosci. 3, 281–290 (2002).
  Article CAS Google Scholar
• LaFerla, F. M., Green, K. N. & Oddo, S. Intracellular amyloid-β in Alzheimer's disease. Nature Rev. Neurosci. 8, 499–509 (2007).
  Article CAS Google Scholar
• Haass, C. & Selkoe, D. J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nature Rev. Mol. Cell Biol. 8, 101–112 (2007).
  Article CAS Google Scholar
• Shankar, G. M. et al. Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nature Med. 14, 837–842 (2008).
  Article CAS Google Scholar
• Lauren, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W. & Strittmatter, S. M. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers. Nature 457, 1128–1132 (2009).
  Article CAS Google Scholar
• Snyder, E. M. et al. Regulation of NMDA receptor trafficking by amyloid-β. Nature Neurosci. 8, 1051–1058 (2005).
  Article CAS Google Scholar
• Kessels, H. W., Nguyen, L. N., Nabavi, S. & Malinow, R. The prion protein as a receptor for amyloid-β. Nature 466, e3–e4 (2010).
  Article CAS Google Scholar
• Small, D. H. et al. The β-amyloid protein of Alzheimer's disease binds to membrane lipids but does not bind to the α7 nicotinic acetylcholine receptor. J. Neurochem. 101, 1527–1538 (2007).
  Article CAS Google Scholar
• Roberson, E. D. et al. Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer's disease mouse model. Science 316, 750–754 (2007).
  Article CAS Google Scholar
• Goedert, M. & Spillantini, M. G. A century of Alzheimer's disease. Science 314, 777–781 (2006).
  Article CAS Google Scholar
• Hirokawa, N., Funakoshi, T., Sato-Harada, R. & Kanai, Y. Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons. J. Cell Biol. 132, 667–679 (1996).
  Article CAS Google Scholar
• Aronov, S., Aranda, G., Behar, L. & Ginzburg, I. Axonal tau mRNA localization coincides with tau protein in living neuronal cells and depends on axonal targeting signal. J. Neurosci. 21, 6577–6587 (2001).
  Article CAS Google Scholar
• Utton, M. A. et al. The slow axonal transport of the microtubule-associated protein tau and the transport rates of different isoforms and mutants in cultured neurons. J. Neurosci. 22, 6394–6400 (2002).
  Article CAS Google Scholar
• Konzack, S., Thies, E., Marx, A., Mandelkow, E. M. & Mandelkow, E. Swimming against the tide: mobility of the microtubule-associated protein tau in neurons. J. Neurosci. 27, 9916–9927 (2007).
  Article CAS Google Scholar
• Ittner, L. M. et al. Dendritic function of tau mediates amyloid-β toxicity in Alzheimer's disease mouse models. Cell 142, 387–397 (2010).
  Article CAS Google Scholar
• Götz, J., Ittner, L. M. & Kins, S. Do axonal defects in tau and amyloid precursor protein transgenic animals model axonopathy in Alzheimer's disease? J. Neurochem. 98, 993–1006 (2006).
  Article Google Scholar
• Maas, T., Eidenmuller, J. & Brandt, R. Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments. J. Biol. Chem. 275, 15733–15740 (2000).
  Article CAS Google Scholar
• Brion, J. P., Smith, C., Couck, A. M., Gallo, J. M. & Anderton, B. H. Developmental changes in tau phosphorylation: fetal tau is transiently phosphorylated in a manner similar to paired helical filament-tau characteristic of Alzheimer's disease. J. Neurochem. 61, 2071–2080 (1993).
  Article CAS Google Scholar
• Götz, J. et al. Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J. 14, 1304–1313 (1995).
  Article Google Scholar
• Santacruz, K. et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science 309, 476–481 (2005).
  Article CAS Google Scholar
• Ittner, L. M., Ke, Y. D. & Götz, J. Phosphorylated Tau interacts with c-Jun N-terminal kinase-interacting protein 1 (JIP1) in Alzheimer disease. J. Biol. Chem. 284, 20909–20916 (2009).
  Article CAS Google Scholar
• Lee, G., Newman, S. T., Gard, D. L., Band, H. & Panchamoorthy, G. Tau interacts with src-family non-receptor tyrosine kinases. J. Cell Sci. 111, 3167–3177 (1998).
  CAS PubMed Google Scholar
• Magnani, E. et al. Interaction of tau protein with the dynactin complex. EMBO J. 26, 4546–4554 (2007).
  Article CAS Google Scholar
• Bhaskar, K., Yen, S. H. & Lee, G. Disease-related modifications in tau affect the interaction between Fyn and Tau. J. Biol. Chem. 280, 35119–35125 (2005).
  Article CAS Google Scholar
• Salter, M. W. & Kalia, L. V. Src kinases: a hub for NMDA receptor regulation. Nature Rev. Neurosci. 5, 317–328 (2004).
  Article CAS Google Scholar
• Gu, J. & Zheng, J. Q. Microtubules in dendritic spine development and plasticity. Open Neurosci. J. 3, 128–133 (2009).
  Article CAS Google Scholar
• Small, D. H., Mok, S. S. & Bornstein, J. C. Alzheimer's disease and Aβ toxicity: from top to bottom. Nature Rev. Neurosci. 2, 595–598 (2001).
  Article CAS Google Scholar
• Götz, J. et al. Transgenic animal models of Alzheimer's disease and related disorders: histopathology, behavior and therapy. Mol. Psychiatry 9, 664–683 (2004).
  Article Google Scholar
• Lewis, J. et al. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 293, 1487–1491 (2001).
  Article CAS Google Scholar
• Terwel, D. et al. Amyloid activates GSK-3β to aggravate neuronal tauopathy in bigenic mice. Am. J. Pathol. 172, 786–798 (2008).
  Article CAS Google Scholar
• Götz, J., Chen, F., van Dorpe, J. & Nitsch, R. M. Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Aβ42 fibrils. Science 293, 1491–1495 (2001).
  Article Google Scholar
• Oddo, S., Billings, L., Kesslak, J. P., Cribbs, D. H. & LaFerla, F. M. Aβ immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 43, 321–332 (2004).
  Article CAS Google Scholar
• Coomaraswamy, J. et al. Modeling familial Danish dementia in mice supports the concept of the amyloid hypothesis of Alzheimer's disease. Proc. Natl Acad. Sci. USA 107, 7969–7974 (2010).
  Article CAS Google Scholar
• Rhein, V. et al. Amyloid-β and tau synergistically impair the oxidative phosphorylation system in triple transgenic Alzheimer's disease mice. Proc. Natl Acad. Sci. USA 106, 20057–20062 (2009).
  Article CAS Google Scholar
• Rapoport, M., Dawson, H. N., Binder, L. I., Vitek, M. P. & Ferreira, A. Tau is essential to β-amyloid-induced neurotoxicity. Proc. Natl Acad. Sci. USA 99, 6364–6369 (2002).
  Article CAS Google Scholar
• Vossel, K. A. et al. Tau reduction prevents Aβ-induced defects in axonal transport. Science 330, 198 (2010).
  Article CAS Google Scholar
• Harada, A. et al. Altered microtubule organization in small-calibre axons of mice lacking tau protein. Nature 369, 488–491 (1994).
  Article CAS Google Scholar
• Dawson, H. N. et al. Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J. Cell Sci. 114, 1179–1187 2001).
  CAS PubMed Google Scholar
• Tucker, K. L., Meyer, M. & Barde, Y. A. Neurotrophins are required for nerve growth during development. Nature Neurosci. 4, 29–37 (2001).
  Article CAS Google Scholar
• Takashima, A. The mechanism for tau aggregation and its relation to neuronal dysfunction. Alzheimer's & Dementia 6, S144 (2010)
  Article Google Scholar
• Dawson, H. N. et al. Loss of tau elicits axonal degeneration in a mouse model of Alzheimer's disease. Neuroscience 169, 516–531 (2010).
  Article CAS Google Scholar
• Saper, C. B., Wainer, B. H. & German, D. C. Axonal and transneuronal transport in the transmission of neurological disease: potential role in system degenerations, including Alzheimer's disease. Neuroscience 23, 389–398 (1987).
  Article CAS Google Scholar
• Stamer, K., Vogel, R., Thies, E., Mandelkow, E. & Mandelkow, E. M. Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J. Cell Biol. 156, 1051–1063 (2002).
  Article CAS Google Scholar
• Pappolla, M. A., Omar, R. A., Kim, K. S. & Robakis, N. K. Immunohistochemical evidence of oxidative [corrected] stress in Alzheimer's disease. Am. J. Pathol. 140, 621–628 (1992).
  CAS PubMed PubMed Central Google Scholar
• Williamson, R., Usardi, A., Hanger, D. P. & Anderton, B. H. Membrane-bound β-amyloid oligomers are recruited into lipid rafts by a fyn-dependent mechanism. FASEB J. 22, 1552–1559 (2008).
  Article CAS Google Scholar
• Ittner, L. M. et al. Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia. Proc. Natl Acad. Sci. USA 105, 15597–16002 (2008).
  Article Google Scholar
• Gong, C. X. & Iqbal, K. Hyperphosphorylation of microtubule-associated protein tau: a promising therapeutic target for Alzheimer disease. Curr. Med. Chem. 15, 2321–2328 (2008).
  Article CAS Google Scholar
• Noble, W. et al. Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo. Proc. Natl Acad. Sci. USA 102, 6990–6995 (2005).
  Article CAS Google Scholar
• van Eersel, J. et al. Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer's disease models. Proc. Natl Acad. Sci. USA 107, 13888–13893 (2010).
  Article CAS Google Scholar
• Klein, C. et al. Process. outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau. J. Neurosci. 22, 698–707 (2002).
  Article CAS Google Scholar
• Oddo, S. et al. Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Aβ and synaptic dysfunction. Neuron 39, 409–421 (2003).
  Article CAS Google Scholar
• Bolmont, T. et al. Induction of tau pathology by intracerebral infusion of amyloid-β-containing brain extract and by amyloid-β deposition in APP x Tau transgenic mice. Am. J. Pathol. 171, 2012–2020 (2007).
  Article CAS Google Scholar
• Palop, J. J. et al. Aberrant excitatory neuronal activity and compensatory remodeling of inhibitory hippocampal circuits in mouse models of Alzheimer's disease. Neuron 55, 697–711 (2007).
  Article CAS Google Scholar
• Grueninger, F. et al. Phosphorylation of Tau at S422 is enhanced by Aβ in TauPS2APP triple transgenic mice. Neurobiol. Dis. 37, 294–306 (2010).
  Article CAS Google Scholar