Evidence map›Paper›PMID 29691802›Full record

ArticleInternational journal of hematology2018

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

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

Abstract read
PubMed Publisher
In one paragraph

Article in International journal of hematology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  7. Alpha and Beta Synucleins: From Pathophysiology to Clinical Application as Biomarkers.Movement disorders : official journal of the Movement Disorder Society · 2022
    Review
  8. Article
  9. Article
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  12. Human erythrocytes: cytoskeleton and its origin.Cellular and molecular life sciences : CMLS · 2020
    Review
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  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Katsuya ArakiDepartment of Neurology, Graduate School of Medicine, Osaka University, Suita, 565-0871, Japan. araki@neurol.med.osaka-u.ac.jp.ORCID http://orcid.org/0000-0001-5493-2178
Kotomi SugawaraDepartment of Hematology, Nephrology, and Rheumatology, Master Course of Graduate School of Medicine, Akita University, Akita, Japan.
Eri H HayakawaDivision of Medical Zoology, Department of Infection and Immunity, Jichi Medical University, Shimotsuke, Japan.
Kumi UbukawaDepartment of Hematology, Nephrology, and Rheumatology, Graduate School of Medicine, Akita University, Akita, Japan.
Isuzu KobayashiDepartment of Hematology, Nephrology, and Rheumatology, Graduate School of Medicine, Akita University, Akita, Japan.
Hideki WakuiDepartment of Life Science, Graduate School of Engineering Science, Akita University, Akita, Japan.
Naoto TakahashiDepartment of Hematology, Nephrology, and Rheumatology, Graduate School of Medicine, Akita University, Akita, Japan.
Kenichi SawadaAkita University, Akita, Japan.
Hideki MochizukiDepartment of Neurology, Graduate School of Medicine, Osaka University, Suita, 565-0871, Japan. hmochizuki@neurol.med.osaka-u.ac.jp.
Wataru NunomuraDepartment of Life Science, Graduate School of Engineering Science, Akita University, Akita, Japan.
Akita University · JPThe University of Osaka · JPJichi Medical University · JP

Funding

Japan Society for the Promotion of Science 15K09448Japan Society for the Promotion of Science 15K09516Japan Society for the Promotion of Science 15K19540Japan Society for the Promotion of Science 26293210Japan Society for the Promotion of Science 26461414Japan Society for the Promotion of Science 26461439Japan Society for the Promotion of Science (JP) 15K14339
6 · The paper itself

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.

Indexed as

Acetylationalpha-SynucleinCell DifferentiationCell MembraneCell NucleusCells, CulturedCytoplasmErythroblastsErythrocytesGene ExpressionHumansLiposomesPhosphatidylcholinesPhosphatidylserinesProtein BindingRecombinant Proteinsalpha-SynucleinLiposomesPhosphatidylcholinesPhosphatidylserinesRecombinant ProteinsRNA, MessengerHuman erythroblastsHuman erythrocytesPhosphatidylserineα-Synuclein

Identifiers

PMID29691802
OpenAlexW2802315284

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.