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3. Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments.

Author

El-Agnaf OM, Jakes R, Curran MD, Middleton D, Ingenito R, Bianchi E, Pessi A, Neill D, and Wallace A

Subjects
Amyloid chemistry, Amyloid metabolism, Benzothiazoles, Biopolymers metabolism, Biopolymers physiology, Cell Nucleus metabolism, Cell Survival, Circular Dichroism, Humans, Microscopy, Electron, Mutation, Nerve Tissue Proteins chemistry, Nerve Tissue Proteins genetics, Nerve Tissue Proteins metabolism, Neuroblastoma, Neurodegenerative Diseases etiology, Parkinson Disease etiology, Parkinson Disease genetics, Peptides metabolism, Peptides physiology, Protein Structure, Secondary, Synucleins, Thiazoles, Tumor Cells, Cultured, alpha-Synuclein, Amyloid physiology, Apoptosis, Nerve Tissue Proteins physiology, Neurons cytology
Abstract

Alpha-synuclein (alpha-syn) protein and a fragment of it, called NAC, have been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the alpha-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We have shown that human wild-type alpha-syn, mutant alpha-syn(Ala30Pro) and mutant alpha-syn(Ala53Thr) proteins can self-aggregate and form amyloid-like filaments. Here we report that aggregates of NAC and alpha-syn proteins induced apoptotic cell death in human neuroblastoma SH-SY5Y cells. These findings indicate that accumulation of alpha-syn and its degradation products may play a major role in the development of the pathogenesis of these neurodegenerative diseases.

Published
1998
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