High pressure promotes alpha-synuclein aggregation in cultured neuronal cells.
α-Synuclein is found in plaques associated with Parkinson's and other neurodegenerative diseases. Changes in α-synuclein oligomerization are thought to give rise to nucleation of neurodegenerative plaques. Here, we investigated the effect of hydrostatic pressure on the aggregation of α-synuclein in cultured neuronal cells. We found that hydrostatic pressure is associated with a transition from monomeric to higher order α-synuclein aggregates. We then tested whether this aggregation is associated with the loss of binding partners, such as phospholipase Cβ. We found that increased pressure reduces the level of PLCβ1 and the amount of α-synuclein/PLCβ1 complexes. These studies suggest that pressure promotes release of α-synuclein from protein partners promoting its oligomerization.
['Golebiewska|Urszula|U|', 'Scarlata|Suzanne|S|']
D000818:Animals D002460:Cell Line D006801:Humans D006874:Hydrostatic Pressure D008958:Models, Molecular D009474:Neurons D054799:Phospholipase C beta D066329:Protein Aggregates D011485:Protein Binding D011487:Protein Conformation D055503:Protein Multimerization D051381:Rats D051844:alpha-Synuclein
Aggregation Hydrostatic pressure Alpha synuclein Parkinson’s disease Phospholipase beta 1