Non‐classical exocytosis of α‐synuclein is sensitive to folding states and promoted under stress conditions

摘要: J. Neurochem. (2010) 113, 1263–1274. Abstract Parkinson’s disease is characterized by deposition of misfolded/aggregated α-synuclein proteins in multiple regions the brain. Neurons can release α-synuclein; through this release, pathological forms are propagated between neurons, and also cause neuroinflammation. In study, we demonstrate that consistently increased under various protein misfolding stress conditions both neuroblastoma primary neuron models. This mediated a non-classical, endoplasmic reticulum (ER)/Golgi-independent exocytosis, stress-induced coincides with translocation into vesicles. Both vesicle secretion were blocked attachment highly stable, globular to α-synuclein, whereas forced resulted an increase these activities. Mass spectrometry analysis showed higher degree oxidative modification secreted than cellular protein. Together, results suggest structurally abnormal, damaged translocate preferentially vesicles released from neuronal cells via exocytosis.