Evidence map›Paper›PMID 36611951›Full record

ArticleCells2022

Calmodulin as a Key Regulator of Exosomal Signal Peptides.

Kenji Ono, Mikio Niwa, Hiromi Suzuki, Nahoko Bailey Kobayashi, Tetsuhiko Yoshida, Makoto Sawada

Open access · goldAbstract read
In one paragraph

Article in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.5field-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

9 citing papers in PubMed, 7 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Kenji OnoDepartment of Brain Function, Division of Stress Adaptation and Protection, Research Institute of Environmental Medicine, Nagoya University, Nagoya 464-8601, Aichi, Japan.ORCID 0000-0002-5402-6535
Mikio NiwaInstitute for Advanced Sciences, Toagosei Co., Ltd., Tsukuba 300-2611, Ibaraki, Japan.
Hiromi SuzukiDepartment of Brain Function, Division of Stress Adaptation and Protection, Research Institute of Environmental Medicine, Nagoya University, Nagoya 464-8601, Aichi, Japan.
Nahoko Bailey KobayashiInstitute for Advanced Sciences, Toagosei Co., Ltd., Tsukuba 300-2611, Ibaraki, Japan.
Tetsuhiko YoshidaInstitute for Advanced Sciences, Toagosei Co., Ltd., Tsukuba 300-2611, Ibaraki, Japan.
Makoto SawadaDepartment of Brain Function, Division of Stress Adaptation and Protection, Research Institute of Environmental Medicine, Nagoya University, Nagoya 464-8601, Aichi, Japan.
Nagoya University · JPToagosei (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signal peptides (SPs) and their fragments play important roles as biomarkers and substances with physiological functions in extracellular fluid. We previously reported that SP fragments were released into extracellular fluid via exosomes and bound to calmodulin (CaM), an exosomal component, in a cell-free system. However, it currently remains unclear whether CaM intracellularly interacts with SP fragments or is involved in the trafficking of these fragments to exosomes. Therefore, the present study examined the binding of CaM to SP fragments in T-REx AspALP cells, transformed HEK293 cells expressing amyloid precursor protein (APP) SP flanking a reporter protein, and their exosomes. APP SP fragments were detected in exosomes from T-REx AspALP cells in the absence of W13, a CaM inhibitor, but were present in lower amounts in exosomes from W13-treated cells. Cargo proteins, such as Alix, CD63, and CD81, were increased in W13-treated T-REx AspALP cells but were decreased in their exosomes. Furthermore, CaM interacted with heat shock protein 70 and CD81 in T-REx AspALP cells and this increased in the presence of W13. APP SP fragments were detected in intracellular CaM complexes in the absence of W13, but not in its presence. These results indicate that CaM functions as a key regulator of the transport of SP fragments into exosomes and plays novel roles in the sorting of contents during exosomal biogenesis.

Indexed as

CalmodulinProtein Sorting SignalsAmyloid beta-Protein PrecursorHEK293 CellsHumansSulfonamidesAmyloid beta-Protein PrecursorCalmodulinN-(4-aminobutyl)-5-chloro-2-naphthalenesulfonamideProtein Sorting SignalsSulfonamidescalmodulinexosomesintercellular communicationsignal peptide

Identifiers

PMID36611951
PMCPMC9818429
OpenAlexW4313472308

What OpenQuestion holds

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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.