Evidence map›Paper›PMID 35246273›Full record

ArticleActa neuropathologica communications2022

Hornerin deposits in neuronal intranuclear inclusion disease: direct identification of proteins with compositionally biased regions in inclusions.

Hongsun Park, Tomoyuki Yamanaka, Yumiko Toyama, Atsushi Fujita, Hiroshi Doi, Takashi Nirasawa, Shigeo Murayama, Naomichi Matsumoto, Tomomi Shimogori, Masaya Ikegawa and 2 more

Open access · goldAbstract read
In one paragraph

Article in Acta neuropathologica communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed, 1 pooled it
1.0field-weighted citation impact, top 29% 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

7 citing papers in PubMed, 1 synthesis or guideline pooled it, 11 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 2 countries.

Hongsun ParkLaboratory of Structural Neuropathology, Doshisha University Graduate School of Brain Science, 1-3 Miyakodanitatara, Kyotanabe-shi, Kyoto, 610-0394, Japan.
Tomoyuki YamanakaLaboratory of Structural Neuropathology, Doshisha University Graduate School of Brain Science, 1-3 Miyakodanitatara, Kyotanabe-shi, Kyoto, 610-0394, Japan.
Yumiko ToyamaDepartment of Life and Medical Systems, Doshisha University, Kyoto, Japan.
Atsushi FujitaDepartment of Human Genetics, Yokohama City University Graduate School of Medicine, Yokohama, Japan.
Hiroshi DoiDepartment of Neurology and Stroke Medicine, Yokohama City University Graduate School of Medicine, Yokohama, Japan.
Takashi NirasawaBruker Japan K.K., Yokohama, Japan.
Shigeo MurayamaThe Brain Bank for Aging Research, Tokyo Metropolitan Geriatric Hospital and Institute of Gerontology, Tokyo, Japan.
Naomichi MatsumotoDepartment of Human Genetics, Yokohama City University Graduate School of Medicine, Yokohama, Japan.
Tomomi ShimogoriMolecular Mechanisms of Brain Development, RIKEN Center for Brain Science, Saitama, Japan.
Masaya IkegawaDepartment of Life and Medical Systems, Doshisha University, Kyoto, Japan.
Matti J HaltiaDepartment of Pathology, Faculty of Medicine, University of Helsinki, Helsinki, Finland.
Nobuyuki NukinaLaboratory of Structural Neuropathology, Doshisha University Graduate School of Brain Science, 1-3 Miyakodanitatara, Kyotanabe-shi, Kyoto, 610-0394, Japan. nnukina@mail.doshisha.ac.jp.ORCID 0000-0002-4545-5100
Doshisha University · JPYokohama City University · JPRIKEN Center for Brain Science · JPTokyo Metropolitan Geriatric Hospital · JPUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neuronal intranuclear inclusion disease (NIID) is a neurodegenerative disorder, characterized by the presence of eosinophilic inclusions (NIIs) within nuclei of central and peripheral nervous system cells. This study aims to identify the components of NIIs, which have been difficult to analyze directly due to their insolubility. In order to establish a method to directly identify the components of NIIs, we first analyzed the huntingtin inclusion-rich fraction obtained from the brains of Huntington disease model mice. Although the sequence with expanded polyglutamine could not be identified by liquid-chromatography mass spectrometry, amino acid analysis revealed that glutamine of the huntingtin inclusion-rich fraction increased significantly. This is compatible with the calculated amino acid content of the transgene product. Therefore, we applied this method to analyze the NIIs of diseased human brains, which may have proteins with compositionally biased regions, and identified a serine-rich protein called hornerin. Since the analyzed NII-rich fraction was also serine-rich, we suggested hornerin as a major component of the NIIs. A specific distribution of hornerin in NIID was also investigated by Matrix-assisted laser desorption/ionization imaging mass spectrometry and immunofluorescence. Finally, we confirmed a variant of hornerin by whole-exome sequencing and DNA sequencing. This study suggests that hornerin may be related to the pathological process of this NIID, and the direct analysis of NIIs, especially by amino acid analysis using the NII-rich fractions, would contribute to a deeper understanding of the disease pathogenesis.

Indexed as

Intranuclear Inclusion BodiesNeurodegenerative DiseasesAmino AcidsAnimalsMiceProteinsSerineAmino AcidsProteinsSerineAmino acid analysisCompositionally biased regionHornerinLow sequence complexityNeuronal intranuclear inclusionNIID

Identifiers

PMID35246273
PMCPMC8895595
OpenAlexW4214846999

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Registered trials

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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.