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Int J Hematol. 2018 Aug;108(2):130-138. doi: 10.1007/s12185-018-2457-8. Epub 2018 Apr 24.

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

Author information

1
Department of Neurology, Graduate School of Medicine, Osaka University, Suita, 565-0871, Japan. araki@neurol.med.osaka-u.ac.jp.
2
Department of Hematology, Nephrology, and Rheumatology, Master Course of Graduate School of Medicine, Akita University, Akita, Japan.
3
Division of Medical Zoology, Department of Infection and Immunity, Jichi Medical University, Shimotsuke, Japan.
4
Department of Hematology, Nephrology, and Rheumatology, Graduate School of Medicine, Akita University, Akita, Japan.
5
Department of Life Science, Graduate School of Engineering Science, Akita University, Akita, Japan.
6
Akita University, Akita, Japan.
7
Department of Neurology, Graduate School of Medicine, Osaka University, Suita, 565-0871, Japan. hmochizuki@neurol.med.osaka-u.ac.jp.
8
Research Center for Engineering Science, Graduate School of Engineering Science, Akita University, Akita, Japan.

Abstract

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.

KEYWORDS:

Human erythroblasts; Human erythrocytes; Phosphatidylserine; α-Synuclein

PMID:
29691802
DOI:
10.1007/s12185-018-2457-8
[Indexed for MEDLINE]

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