Journal Article

The localization of α-synuclein in the process of differentiation of human erythroid cells

Kobayashi, Isuzu, Nunomura, Wataru, Takahashi, Naoto, Sawada, Kenichi, Mochizuki, Hideki, Hayakawa, Eri H, Wakui, Hideki, Ubukawa, Kumi, Araki, Katsuya, Sugawara, Kotomi

2018

Overview

Although the neuronal protein α-synuclein (α-syn) is thought to play a central role in the pathogenesis of Parkinson’s disease (PD), its physiological function remains unknown. It is known that α-syn is also abundantly expressed in erythrocytes. However, its role in erythrocytes is also unknown. In the present study, we investigated the localization of α-syn in human erythroblasts and erythrocytes. Protein expression of α-syn increased during terminal differentiation of erythroblasts (from day 7 to day 13), whereas its mRNA level peaked at day 11. α-syn was detected in the nucleus, and was also seen in the cytoplasm and at the plasma membrane after day 11. In erythroblasts undergoing nucleus extrusion (day 13), α-syn was detected at the periphery of the nucleus. Interestingly, we found that recombinant α-syn binds to trypsinized inside-out vesicles of erythrocytes and phosphatidylserine (PS) liposomes. The dissociation constants for binding to PS/phosphatidylcholine (PC) liposomes of N-terminally acetylated (NAc) α-syn was lower than that of non NAc α-syn. This suggests that N-terminal acetylation plays a significant functional role. The results of the present study collectively suggest that α-syn is involved in the enucleation of erythroblasts and the stabilization of erythroid membranes.

• Publisher: Springer Nature B.V
• Subject: Acetylation / Cytoplasm / Differentiation / Enucleation / Erythroblasts / Erythrocytes / Erythroid cells / Extrusion / Lecithin / Liposomes / Localization / Membranes / Movement disorders / mRNA / Neurodegenerative diseases / Nuclei / Parkinson's disease / Pathogenesis / Phosphatidylcholine / Phosphatidylserine / Synuclein