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Molecular events underlying the cell‐to‐cell transmission of α‐synuclein
Author(s) -
Choi Yu Ree,
Park Soo Jin,
Park Sang Myun
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15674
Subject(s) - pathogenesis , endocytosis , microbiology and biotechnology , neurite , intracellular , fibril , alpha synuclein , parkinson's disease , lewy body , chemistry , biology , dementia with lewy bodies , cell , biophysics , disease , biochemistry , in vitro , medicine , immunology , pathology , dementia
The pathogenesis of Parkinson's disease (PD), which is a progressive neurodegenerative disease, is associated with the formation of protein inclusion bodies called Lewy bodies (LB) or Lewy neurites (LN). α‐Synuclein (α‐Syn) is a major component of LB and LN. The formation of LB or LN is mediated by formation of α‐Syn fibrils, which are formed from α‐Syn monomers and oligomers. Additionally, intercellular α‐Syn propagation has been proposed to be important for the progression of PD. Thus, various studies have focused on elucidating the role of α‐Syn propagation in the pathogenesis of PD. Previous studies have reported that α‐Syn species are released from the cells through various pathways, including the unconventional secretion pathways. The released α‐Syn species are internalized by the cells through multiple mechanisms, including receptor‐mediated endocytosis. Some molecular processes involved in intercellular α‐Syn propagation have been recently elucidated. This review discusses the current studies on the molecular mechanisms underlying the release and uptake of α‐Syn and their physiological relevance.