Neurotoxic dopamine quinone facilitates the assembly of tau into fibrillar polymers.

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.

• Authors: Ismael Santa-María, Félix Hernández, Mark A Smith, George Perry, Jesús Avila, Francisco J Moreno
• Journal: Molecular and cellular biochemistry (Mol Cell Biochem) Vol. 278 Issue 1-2 Pg. 203-12 (Oct 2005) ISSN: 0300-8177 [Print] Netherlands
• PMID: 16180106 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Benzoquinones
• Hydroquinones
• Polymers
• tau Proteins
• quinone
• dopamine quinone
• Dopamine
• hydroquinone

Topics

• Animals
• Benzoquinones (metabolism, pharmacology)
• Brain (cytology, metabolism)
• Dopamine (analogs & derivatives, metabolism, pharmacology)
• Dose-Response Relationship, Drug
• Humans
• Hydroquinones (metabolism, pharmacology)
• Immunohistochemistry
• Mice
• Microscopy, Immunoelectron
• Neuroblastoma (metabolism)
• Polymers (metabolism)
• Protein Processing, Post-Translational (physiology)
• Tumor Cells, Cultured
• tau Proteins (drug effects, metabolism)