Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions.

Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions.

J Neurochem. 2010 Mar 24;

Authors: Jang A, Lee HJ, Suk JE, Jung JW, Kim KP, Lee SJ

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

PMID: 20345754 [PubMed - as supplied by publisher]

Read the complete post at http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?tmpl=NoSidebarfile&db=PubMed&cmd=Retrieve&list_uids=20345754&dopt=Abstract

Posted 30 Mar 2010 3:48 AM by pubmed: neuroblastoma
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