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Amyloid-β and tau--a toxic pas de deux in Alzheimer’s disease

Ittner, Lars M., Götz, Jürgen·2011·Nature Reviews Neuroscience
DOI 10.1038/nrn2967
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Abstract

Amyloid-β and tau are the two hallmark proteins in Alzheimer's disease. Although both amyloid-β and tau have been extensively studied individually with regard to their separate modes of toxicity, more recently new light has been shed on their possible interactions and synergistic effects in Alzheimer's disease. Here, we review novel findings that have shifted our understanding of the role of tau in the pathogenesis of Alzheimer's disease towards being a crucial partner of amyloid-β. As we gain a deeper understanding of the different cellular functions of tau, the focus shifts from the axon, where tau has a principal role as a microtubule-associated protein, to the dendrite, where it mediates amyloid-β toxicity.

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  • During progression of AD and other tauopathies, abnormally phosphorylated forms of Tau aggregate and accumulate in the somatodendritic compartment in neurons and can localize to synapses.

    “During progression of AD and other tauopathies, abnormally phosphorylated forms of Tau aggregate and accumulate in the somatodendritic compartment in neurons and can localize to synapses (Ittner and Götz, 2011; Tai et al., 2012”

    From Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies (2018) · cites this paper as Ittner and Götz, 2011

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Research works printed but not linked: 47

  1. Citron, M. Strategies for disease modification in Alzheimer's disease. Nature Rev. Neurosci. 5, 677–685 (2004). · DOI
  2. 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). · DOI · Paper page
  3. Braak, H. & Braak, E. Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol. Aging 16, 271–278; discussion 278–284 (1995). · DOI · Paper page
  4. Götz, J. & Ittner, L. M. Animal models of Alzheimer's disease and frontotemporal dementia. Nature Rev. Neurosci. 9, 532–544 (2008). · DOI · Paper page
  5. Frost, B. & Diamond, M. I. Prion-like mechanisms in neurodegenerative diseases. Nature Rev. Neurosci. 11, 155–159 (2010). · DOI · Paper page
  6. 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). · DOI · Paper page
  7. 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). · DOI · Paper page
  8. Goedert, M. & Spillantini, M. G. A century of Alzheimer's disease. Science 314, 777–781 (2006). · DOI
  9. 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). · DOI
  10. 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). · DOI
  11. 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). · DOI
  12. Ittner, L. M. et al. Dendritic function of tau mediates amyloid-β toxicity in Alzheimer's disease mouse models. Cell 142, 387–397 (2010). · DOI · Paper page
  13. 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). · DOI
  14. 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). · DOI
  15. 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). · DOI
  16. Santacruz, K. et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science 309, 476–481 (2005). · DOI · Paper page
  17. 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). · DOI
  18. 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). · DOI
  19. Magnani, E. et al. Interaction of tau protein with the dynactin complex. EMBO J. 26, 4546–4554 (2007). · DOI
  20. 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). · DOI
  21. Salter, M. W. & Kalia, L. V. Src kinases: a hub for NMDA receptor regulation. Nature Rev. Neurosci. 5, 317–328 (2004). · DOI
  22. Gu, J. & Zheng, J. Q. Microtubules in dendritic spine development and plasticity. Open Neurosci. J. 3, 128–133 (2009). · DOI
  23. 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). · DOI
  24. Götz, J. et al. Transgenic animal models of Alzheimer's disease and related disorders: histopathology, behavior and therapy. Mol. Psychiatry 9, 664–683 (2004). · DOI
  25. Lewis, J. et al. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 293, 1487–1491 (2001). · DOI · Paper page
  26. Terwel, D. et al. Amyloid activates GSK-3β to aggravate neuronal tauopathy in bigenic mice. Am. J. Pathol. 172, 786–798 (2008). · DOI · Paper page
  27. 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). · DOI · Paper page
  28. 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). · DOI
  29. 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). · DOI · Paper page
  30. 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). · DOI · Paper page
  31. Vossel, K. A. et al. Tau reduction prevents Aβ-induced defects in axonal transport. Science 330, 198 (2010). · DOI · Paper page
  32. Harada, A. et al. Altered microtubule organization in small-calibre axons of mice lacking tau protein. Nature 369, 488–491 (1994). · DOI
  33. Dawson, H. N. et al. Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J. Cell Sci. 114, 1179–1187 2001). · DOI · Paper page
  34. Tucker, K. L., Meyer, M. & Barde, Y. A. Neurotrophins are required for nerve growth during development. Nature Neurosci. 4, 29–37 (2001). · DOI · Paper page
  35. Takashima, A. The mechanism for tau aggregation and its relation to neuronal dysfunction. Alzheimer's & Dementia 6, S144 (2010) · DOI
  36. Dawson, H. N. et al. Loss of tau elicits axonal degeneration in a mouse model of Alzheimer's disease. Neuroscience 169, 516–531 (2010). · DOI
  37. 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). · DOI
  38. 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). · DOI · Paper page
  39. 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).
  40. 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). · DOI
  41. 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). · DOI
  42. 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). · DOI
  43. 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). · DOI · Paper page
  44. 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). · DOI · Paper page
  45. 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). · DOI · Paper page
  46. 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). · DOI · Paper page
  47. 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). · DOI · Paper page

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Metadata

Authors
Ittner, L. M., & Götz, J.
Venue
Nature Reviews Neuroscience
Publisher
Springer Science and Business Media LLC
Published
2010-12-31
Volume
12
Issue
2
Pages
67-72
ISSN
  • 1471-003X
  • 1471-0048
DOI
10.1038/nrn2967
Cited by
1,269
References
18
Language
en
Licence
www.springer.com/tdm (tdm)

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