Kinetic Stabilization of the α-Synuclein Protofibril by a Dopamine-α-Synuclein Adduct

The substantia nigra in Parkinson's disease (PD) is depleted of dopaminergic neurons and contains fibrillar Lewy bodies comprising primarily α-synuclein. We screened a library to identify drug-like molecules to probe the relation between neurodegeneration and α-synuclein fibrilization. All but one of 15 fibril inhibitors were catecholamines related to dopamine. The inhibitory activity of dopamine depended on its oxidative ligation to α-synuclein and was selective for the protofibril-to-fibril conversion, causing accumulation of the α-synuclein protofibril. Adduct formation provides an explanation for the dopaminergic selectivity of α-synuclein–associated neurotoxicity in PD and has implications for current and future PD therapeutic and diagnostic strategies.

[1]  S Fahn,et al.  Parkinson disease, the effect of levodopa, and the ELLDOPA trial. Earlier vs Later L-DOPA. , 1999, Archives of neurology.

[2]  W. Bender,et al.  A Drosophila model of Parkinson's disease , 2000, Nature.

[3]  Y. Agid Levodopa: Is toxicity a myth? , 1998, Neurology.

[4]  M. Zigmond,et al.  Role of oxidation in the neurotoxic effects of intrastriatal dopamine injections. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[5]  T. Dawson New Animal Models for Parkinson's Disease , 2000, Cell.

[6]  P. Lansbury,et al.  Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson’s disease? , 2000, Nature Cell Biology.

[7]  T. Osawa,et al.  Immunochemical detection of protein dityrosine in atherosclerotic lesion of apo-E-deficient mice using a novel monoclonal antibody. , 2000, Biochemical and biophysical research communications.

[8]  D. Kuhn,et al.  Dopamine Inactivates Tryptophan Hydroxylase and Forms a Redox-Cycling Quinoprotein: Possible Endogenous Toxin to Serotonin Neurons , 1998, The Journal of Neuroscience.

[9]  P. Lansbury,et al.  Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein. , 2000, Biochemistry.

[10]  P. Lansbury,et al.  Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? , 1993, Cell.

[11]  J. Waite,et al.  Cross-linking in adhesive quinoproteins: studies with model decapeptides. , 2000, Biochemistry.