상위피인용논문
He-Jin Leea, b, Ji-Eun Suka, Eun-Jin Baea, Seung-Jae Leea,*
a Department of Biomedical Science and Technology, RCTC, IBST, Konkuk University, 1 Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea
b Department of Anatomy, School of Medicine, Konkuk University, Chungju, Chungbuk 380-701, Republic of Korea
*Corresponding author : Seung-Jae Lee
Abstract
Abnormal deposition of α-synuclein in neurons and glia is implicated in many neurological diseases, such as Parkinson’s disease and Dementia with Lewy bodies. Recently, evidence has emerged that this protein and its aggregates are secreted from neuronal cells, and this extracellular protein may contribute to the pathogenic process. Here, we show that all the major brain cell types (neurons, astrocytes, and microglia) are capable of clearing the extracellular α-synuclein aggregates by internalization and degradation. Among these cell types, microglia showed the highest rate of degradation. Upon activation by lipopolysaccharide, the degradation of the internalized α-synuclein aggregates was slowed, causing protein accumulation in the microglial cytoplasm. These results suggest that microglia may be the major scavenger cells for extracellular α-synuclein aggregates in brain parenchyma, and that clearance may be regulated by the activation state of these cells.
Keywords : α-Synuclein; Parkinson’s disease; Microglia; Protein aggregation; Lipopolysaccharide; Astrocyte
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