Publication date: Sep 10, 2019
The research team used cutting-edge imaging techniques to find that Lewy bodies in Parkinson’s disease brains contain α-synuclein protein aggregates, known as amyloid fibrils, that can propagate through the brain.
-Our work follows on from in vitro findings that aggregates of α-synuclein that can propagate through the brain have a cross-β structure,” says lead author of the study Dr Hideki Mochizuki.
The study, using mouse models, has potential therapeutic applications for Parkinson’s disease in humans, according to the researchers.
According to the authors, the -data provide the basis for understanding sex differences in α-synuclein homeostasis and the development of therapeutic approaches to treating men and postmenopausal women,” with Parkinson’s disease.
A study conducted by Oregon Health & Science University, US suggests that Lewy bodies cause problems when they pull α-synuclein out from the nucleus of brain cells.
Using mice models and post-mortem brain tissue from humans, the researchers found that the α-synuclein repair DNA breaks.
The role of α-synuclein in DNA restoration could therefore be crucial in preventing cell death, but this function may be lost in brain diseases such as Parkinson’s, leading to the widespread death of neurons.
The team revealed that the α-synuclein protein is rapidly recruited to the site of DNA damage in the neurons of mice.
According to the researchers, the results suggest that α-synuclein plays a crucial role in binding broken strands of DNA within the cell’s nucleus.
The researchers say that their findings could lead to the development of methods to deliver α-synuclein proteins into the nucleus of cells, or design replacements for its function.
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- MicroRNAs: Game Changers in the Regulation of α-Synuclein in Parkinson’s Disease.
- Parkinson’s disease symptoms “improved” by oestrogen
- Complex of EGCG with Cu(II) Suppresses Amyloid Aggregation and Cu(II)-Induced Cytotoxicity of α-Synuclein.
- Human NPCs can degrade α-syn fibrils and transfer them preferentially in a cell contact-dependent manner possibly through TNT-like structures.