Molecular and Cellular Biochemistry

, Volume 278, Issue 1, pp 203–212

Neurotoxic dopamine quinone facilitates the assembly of tau into fibrillar polymers

Authors

  • Ismael Santa-María
    • Centro de Biología Molecular “Severo Ochoa”Universidad Autónoma de Madrid
  • Félix Hernández
    • Centro de Biología Molecular “Severo Ochoa”Universidad Autónoma de Madrid
  • Mark A. Smith
    • Institute of PathologyCase Western Reserve University
  • George Perry
    • Institute of PathologyCase Western Reserve University
    • Centro de Biología Molecular “Severo Ochoa”Universidad Autónoma de Madrid
    • Centro de Biología Molecular “Severo Ochoa”, Facultad de Ciencias, Campus de CantoblancoUniversidad Autónoma de Madrid
  • Francisco J. Moreno
    • Centro de Biología Molecular “Severo Ochoa”Universidad Autónoma de Madrid
Article

DOI: 10.1007/s11010-005-7499-6

Cite this article as:
Santa-María, I., Hernández, F., Smith, M.A. et al. Mol Cell Biochem (2005) 278: 203. doi:10.1007/s11010-005-7499-6

Abstract

Aberrant aggregation of microtubule associated protein tau is the main characteristic of different disorders known as tauopathies. Different compounds have been described to facilitate tau aberrant aggregation. In this work, we demonstrate that oxidized products of dopamine (neurotoxic dopamine quinone), a neurotransmitter involved in Parkinson's disease, promote tau polymerization. Curiously, neurons expressing dopamine (substantia nigra) show a low content of tau protein and seldom have tau aggregation in tauopathies. In non-dopaminergic neurons, quinone oxidation products may be involved in tau polymerization. These results support a link between oxidative damage and the onset of tauopathies. (Mol Cell Biochem 278: 203–212, 2005)

Key Word

Alzheimer's diseasedopaminepaired helical filamentsquinonestau protein
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Copyright information

© Springer Science + Business Media, Inc. 2005