Evidence map›Paper›PMID 35402512›Full record

ArticleFrontiers in molecular biosciences2022

Extracellular Vesicles Contribute to the Metabolism of Transthyretin Amyloid in Hereditary Transthyretin Amyloidosis.

Hiroki Yamaguchi, Hironori Kawahara, Noriyuki Kodera, Ayanori Kumaki, Yasutake Tada, Zixin Tang, Kenji Sakai, Kenjiro Ono, Masahito Yamada, Rikinari Hanayama

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Pathogenesis and kidney prognosis of renal amyloidosis.Cellular and molecular life sciences : CMLS · 2026
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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

10 authors at 3 institutions in 1 country.

Hiroki YamaguchiDepartment of Immunology, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan.
Hironori KawaharaDepartment of Immunology, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan.
Noriyuki KoderaWPI Nano Life Science Institute (NanoLSI), Kanazawa University, Kanazawa, Japan.
Ayanori KumakiDepartment of Immunology, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan.
Yasutake TadaDepartment of Immunology, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan.
Zixin TangDepartment of Immunology, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan.
Kenji SakaiDepartment of Neurology and Neurobiology of Aging, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan.
Kenjiro OnoDepartment of Neurology and Neurobiology of Aging, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan.
Masahito YamadaDepartment of Neurology and Neurobiology of Aging, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan.
Rikinari HanayamaDepartment of Immunology, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan.
Kanazawa University · JPLife Science Institute · JPKudanzaka Hospital · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hereditary (variant) transthyretin amyloidosis (ATTRv amyloidosis), which is caused by variants in the transthyretin (TTR) gene, leads to TTR amyloid deposits in multiple organs and various symptoms such as limb ataxia, muscle weakness, and cardiac failure. Interaction between amyloid proteins and extracellular vesicles (EVs), which are secreted by various cells, is known to promote the clearance of the proteins, but it is unclear whether EVs are involved in the formation and deposition of TTR amyloid in ATTRv amyloidosis. To clarify the relationship between ATTRv amyloidosis and EVs, serum-derived EVs were analyzed. In this study, we showed that cell-derived EVs are involved in the formation of TTR amyloid deposits on the membrane of small EVs, as well as the deposition of TTR amyloid in cells. Human serum-derived small EVs also altered the degree of aggregation and deposition of TTR. Furthermore, the amount of TTR aggregates in serum-derived small EVs in patients with ATTRv amyloidosis was lower than that in healthy controls. These results indicate that EVs contribute to the metabolism of TTR amyloid, and suggest that TTR in serum-derived small EVs is a potential target for future ATTRv amyloidosis diagnosis and therapy.

Indexed as

amyloidosisatomic force microscopeATTRv amyloidosisextracellular vesicletransthyretin

Identifiers

PMID35402512
PMCPMC8983912
OpenAlexW4221065483

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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.