Parkinson disease (PD) is characterized by widespread distribution of aggregated α-synuclein (α-Syn) protein in inclusions known as Lewy bodies. α-Syn is secreted from neurons and transferred to neighboring cells including pericytes, one of the blood-brain barrier (BBB) constituent cells. This cell-to-cell transmission is thought to underlie the progress of PD. In addition, blood-borne α-Syn can penetrate into the brain across the BBB. Here, we investigated how α-Syn is taken up by pericytes. Uptake of α-Syn by pericytes was increased with time during a 120-min period. The α-Syn uptake by pericytes was decreased by an excess amount of α-Syn and showed a temperature-dependent manner, suggesting that α-Syn uptake by pericytes is mediated by a saturable transport system. This uptake was inhibited by cyclosporine, but not sertraline, a clathrin-mediated endocytosis inhibitor. Intracellular accumulation of α-Syn in pericytes during a 24-hr period was lower than that in brain endothelial cells and astrocytes. In the presence of a lysosome inhibitor bafilomycin A1, the intracellular accumulation of α-Syn in pericytes was increased. These results suggest that pericytes possess a specific transport and degradation system of α-Syn.