Evidence map›Paper›PMID 40746997›Full record

ArticleiScience2025

Protein arginine methylation regulates anti-inflammatory programming in response to aging stress.

Yao Yuan, Kaori Motomura, Jun-Dal Kim, Kowit Hengphasatporn, Koichiro Kako, Syunsuke Maruhashi, Fumiya Kasai, Hayase Mizukami, Sachiko Toma-Fukai, Masafumi Muratani and 3 more

Abstract read
In one paragraph

Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Yao YuanLife Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, Ibaraki 305-8575, Japan.
Kaori MotomuraLife Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, Ibaraki 305-8575, Japan.
Jun-Dal KimLife Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, Ibaraki 305-8575, Japan.
Kowit HengphasatpornCenter for Computational Sciences, University of Tsukuba, Ibaraki 305-8577, Japan.
Koichiro KakoLife Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, Ibaraki 305-8575, Japan.
Syunsuke MaruhashiLife Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, Ibaraki 305-8575, Japan.
Fumiya KasaiLife Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, Ibaraki 305-8575, Japan.
Hayase MizukamiLife Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, Ibaraki 305-8575, Japan.
Sachiko Toma-FukaiAMED-CREST, Japan Agency for Medical Research and Development, Chiyoda-ku, Tokyo, Japan.
Masafumi MurataniDepartment of Genome Biology, Institute of Medicine, University of Tsukuba, Ibaraki 305-8575, Japan.
Yasuteru ShigetaCenter for Computational Sciences, University of Tsukuba, Ibaraki 305-8577, Japan.
Hiroaki DaitokuLife Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, Ibaraki 305-8575, Japan.
Akiyoshi FukamizuLife Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, Ibaraki 305-8575, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PRMT1 is a key enzyme responsible for protein arginine methylation, which regulates various cellular processes. However, its physiological significance at whole-body level remains unknown due to embryonic lethality of Prmt1-null mice. Despite only one amino acid difference at position 179, molecular dynamics simulations and biochemical assays showed that human PRMT1 exhibits enhanced methyltransferase activity compared to its mouse counterpart. Capitalizing on this finding, we generated humanized PRMT1 knock-in mice (huMice) carrying the H179Y substitution. Notably, huMice displayed distinct transcriptomic signatures associated with attenuated inflammatory responses compared to wild-type mice in an age-dependent manner. In particular, huMice exhibited reduced pro-inflammatory cytokines production following lipopolysaccharide (LPS) challenge at 12 months, revealing that heightened PRMT1 activity confers a physiological advantage in alleviating age-related inflammatory stress. Our findings underscore PRMT1's key role in the modulation of anti-inflammatory programming at the organismal level and open avenues for leveraging this knowledge in developing mitigation strategies against inflammaging.

Indexed as

Epigeneticsmmunologyranscriptomics

Identifiers

PMID40746997
PMCPMC12312054

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.