Parkinson's disease is a type of amyloidosis featuring accumulation of amyloid fibrils of ?-synuclein.

ABSTRACT: Many neurodegenerative diseases are characterized by the accumulation of abnormal protein aggregates in the brain. In Parkinson's disease (PD), ?-synuclein (?-syn) forms such aggregates called Lewy bodies (LBs). Recently, it has been reported that aggregates of ?-syn with a cross-? structure are capable of propagating within the brain in a prionlike manner. However, the presence of cross-? sheet-rich aggregates in LBs has not been experimentally demonstrated so far. Here, we examined LBs in thin sections of autopsy brains of patients with PD using microbeam X-ray diffraction (XRD) and found that some of them gave a diffraction pattern typical of a cross-? structure. This result confirms that LBs in the brain of PD patients contain amyloid fibrils with a cross-? structure and supports the validity of in vitro propagation experiments using artificially formed amyloid fibrils of ?-syn. Notably, our finding supports the concept that PD is a type of amyloidosis, a disease featuring the accumulation of amyloid fibrils of ?-syn.

SUBMITTER: Araki K 

PROVIDER: S-EPMC6731630 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature