高压促进培养的神经元细胞中α-突触核蛋白的聚集。
High pressure promotes alpha-synuclein aggregation in cultured neuronal cells.
作者信息
Golebiewska Urszula, Scarlata Suzanne
机构信息
Dept. of Biological Sciences and Geology, Queensborough Community College, Bayside, NY 11364, USA.
Dept. of Chemistry and Biochemistry, Worcester Polytechnic Institute, Worcester, MA 01609 USA.
出版信息
FEBS Lett. 2015 Oct 24;589(21):3309-12. doi: 10.1016/j.febslet.2015.09.019. Epub 2015 Oct 3.
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.
α-突触核蛋白存在于与帕金森病和其他神经退行性疾病相关的斑块中。α-突触核蛋白寡聚化的变化被认为会引发神经退行性斑块的成核。在此，我们研究了流体静压对培养的神经元细胞中α-突触核蛋白聚集的影响。我们发现流体静压与α-突触核蛋白从单体向高阶聚集体的转变有关。然后，我们测试了这种聚集是否与结合伴侣（如磷脂酶Cβ）的丧失有关。我们发现压力增加会降低PLCβ1的水平以及α-突触核蛋白/PLCβ1复合物的数量。这些研究表明，压力促进α-突触核蛋白从促进其寡聚化的蛋白质伴侣中释放出来。
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