Evidence map›Paper›PMID 25990096›Full record

ArticleActa neuropathologica communications2015

Filamentous aggregations of phosphorylated α-synuclein in Schwann cells (Schwann cell cytoplasmic inclusions) in multiple system atrophy.

Keiko Nakamura, Fumiaki Mori, Tomoya Kon, Kunikazu Tanji, Yasuo Miki, Masahiko Tomiyama, Hidekachi Kurotaki, Yasuko Toyoshima, Akiyoshi Kakita, Hitoshi Takahashi and 2 more

Open access · goldAbstract read
In one paragraph

Article in Acta neuropathologica communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Review
  3. Astrocyte alterations in α-synucleinopathies.Frontiers in cellular neuroscience · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
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  11. Review
  12. Article
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  14. A Mouse Model of Multiple System Atrophy: Bench to Bedside.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2023
    Review
  15. Review
  16. Article
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  18. Article
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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

12 authors at 4 institutions in 1 country.

Keiko NakamuraDepartment of Neuropathology, Institute of Brain Science, Hirosaki University Graduate School of Medicine, 5 Zaifu-cho, Hirosaki, 036-8562, Japan. k-nkmr@med.kanazawa-u.ac.jp.
Fumiaki MoriDepartment of Neuropathology, Institute of Brain Science, Hirosaki University Graduate School of Medicine, 5 Zaifu-cho, Hirosaki, 036-8562, Japan. neuropal@hirosaki-u.ac.jp.
Tomoya KonDepartment of Neurology, Aomori Prefectural Central Hospital, Aomori, Japan. t-kon@umin.ac.jp.
Kunikazu TanjiDepartment of Neuropathology, Institute of Brain Science, Hirosaki University Graduate School of Medicine, 5 Zaifu-cho, Hirosaki, 036-8562, Japan. kunikazutanji@hotmail.com.
Yasuo MikiDepartment of Neuropathology, Institute of Brain Science, Hirosaki University Graduate School of Medicine, 5 Zaifu-cho, Hirosaki, 036-8562, Japan. yasuomiki@hotmail.com.
Masahiko TomiyamaDepartment of Neurology, Aomori Prefectural Central Hospital, Aomori, Japan. masahiko_tomiyama@med.pref.aomori.jp.
Hidekachi KurotakiDepartment of Pathology, Aomori Prefectural Central Hospital, Aomori, Japan. hidekachi_kurotaki@med.pref.aomori.jp.
Yasuko ToyoshimaDepartment of Pathology, Brain Research Institute, University of Niigata, Niigata, Japan. yasuko@bri.niigata-u.ac.jp.
Akiyoshi KakitaDepartment of Pathological Neuroscience, Center for Bioresource-based Researches, Brain Research Institute, University of Niigata, Niigata, Japan. kakita@bri.niigata-u.ac.jp.
Hitoshi TakahashiDepartment of Pathology, Brain Research Institute, University of Niigata, Niigata, Japan. hitoshi@bri.niigata-u.ac.jp.
Masahito YamadaDepartment of Neurology and Neurobiology of Ageing, Kanazawa University Graduate School of Medical Science, Kanazawa, Japan. m-yamada@med.kanazawa-u.ac.jp.
Koichi WakabayashiDepartment of Neuropathology, Institute of Brain Science, Hirosaki University Graduate School of Medicine, 5 Zaifu-cho, Hirosaki, 036-8562, Japan. koichi@hirosaki-u.ac.jp.
Hirosaki University · JPAomori Prefectural Central Hospital · JPNiigata University · JPKanazawa University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe histological hallmark of multiple system atrophy (MSA) is the presence of filamentous aggregations of phosphorylated α-synuclein in oligodendrocytes, referred to as glial cytoplasmic inclusions (GCIs). Although GCIs can occur widely in the central nervous system, accumulation of phosphorylated α-synuclein in Schwann cells has not been reported in MSA. We immunohistochemically examined the cranial and spinal nerves, peripheral ganglia and visceral autonomic nervous system of patients with MSA (n = 14) and control subjects (n = 20).

resultsIn MSA, accumulation of phosphorylated α-synuclein was found in the cytoplasm of Schwann cells. These Schwann cell cytoplasmic inclusions (SCCIs) were also immunopositive for ubiquitin and p62. SCCIs were found in 12 of 14 patients with MSA (85.7 %). They were most frequent in the anterior nerve of the sacral cord and, to a lesser extent, in the cranial nerves (oculomotor, glossopharyngeal-vagus and hypoglossal nerves), and spinal and sympathetic ganglia. SCCIs were rarely found in the visceral organs. Immunoelectron microscopy demonstrated that the SCCIs consisted of abnormal filaments, 15-20 nm in diameter. No such inclusions were found in controls.

conclusionThe present findings indicate that Schwann cells are also involved in the disease process of MSA.

Indexed as

Adaptor Proteins, Signal TransducingAgedalpha-SynucleinAutonomic Nervous SystemCranial NervesCytoskeletonFemaleGangliaHumansImmunohistochemistryInclusion BodiesMaleMicroscopy, ImmunoelectronMiddle AgedMultiple System AtrophyPhosphorylationAdaptor Proteins, Signal Transducingalpha-SynucleinSequestosome-1 ProteinSQSTM1 protein, humanUbiquitin

Identifiers

PMID25990096
PMCPMC4438578
OpenAlexW2166363953

What OpenQuestion holds

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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.