Evidence map›Paper›PMID 40763927›Full record

ArticleGenes to cells : devoted to molecular & cellular mechanisms2025

Functional Differences Between SIRPα Splice Isoforms.

Mihoko Kajita, Yojiro Matsui, Kotaro Sugimoto, Shuto Takeuchi, Shota Matsumoto, Takahiro Okumura, Hiroyuki Kajiura, Kazuki Motomura, Atsushi Takeda, Tomomi Koshiyama and 1 more

Abstract read
In one paragraph

Article in Genes to cells : devoted to molecular & cellular mechanisms, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Functional Differences Between SIRPα Splice Isoforms.Genes to cells : devoted to molecular & cellular mechanisms · 2025
    Article
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

11 authors.

Mihoko KajitaDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kyoto, Japan.ORCID https://orcid.org/0009-0001-6429-0321
Yojiro MatsuiDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kyoto, Japan.
Kotaro SugimotoDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kyoto, Japan.
Shuto TakeuchiDepartment of Applied Chemistry, College of Life Sciences, Ritsumeikan University, Kyoto, Japan.
Shota MatsumotoDepartment of Applied Chemistry, College of Life Sciences, Ritsumeikan University, Kyoto, Japan.
Takahiro OkumuraDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kyoto, Japan.
Hiroyuki KajiuraInternational Center for Biotechnology, Osaka University, Osaka, Japan.
Kazuki MotomuraResearch Organization of Science and Technology, Ritsumeikan University, Kyoto, Japan.
Atsushi TakedaDepartment of Biotechnology, College of Life Sciences, Ritsumeikan University, Kyoto, Japan.
Tomomi KoshiyamaDepartment of Applied Chemistry, College of Life Sciences, Ritsumeikan University, Kyoto, Japan.
Kyoko ShirakabeDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kyoto, Japan.

Funding

Astellas Foundation for Research on Metabolic DisordersJapan Society for the Promotion of ScienceJapan Society for the Promotion of Science 18K06911Japan Society for the Promotion of Science 21K07236Japan Society for the Promotion of Science 24K23395Naito FoundationTakeda Science Foundation
6 · The paper itself

Abstract

Signal regulatory protein (SIRP) α, an inhibitory receptor belonging to the immunoglobulin (Ig) superfamily is abundantly expressed in phagocytes such as macrophages. CD47, the ligand for SIRPα, is expressed in most healthy cells, and called "don't eat me" signal because it binds to SIRPα on the surface of macrophages and inhibits phagocytosis. SIRPα has multiple splice isoforms, but most functional analyses have been carried out using long SIRPα, the SIRPα isoform with three extracellular Ig domains. In this study, we analyzed the expression and function of short SIRPα, an SIRPα isoform with only one extracellular Ig domain. In resting mouse macrophage Raw 264.7 cells, the short and long SIRPα mRNA expression levels were similar, and the proportion of short SIRPα mRNA decreased substantially after endotoxin stimulation. Short SIRPα bound to CD47 as same as long SIRPα, however, did not suppress the phagocytosis of recombinant CD47-coated beads, unlike long SIRPα. These results suggest that short SIRPα may be a "don't eat me" signal regulator with different expression and function from long SIRPα.

Indexed as

Antigens, DifferentiationReceptors, ImmunologicAlternative SplicingAnimalsCD47 AntigenMacrophagesMicePhagocytosisProtein IsoformsRAW 264.7 CellsAntigens, DifferentiationCD47 AntigenProtein IsoformsReceptors, ImmunologicSirpa protein, mouseCD47“don't eat me” signalmacrophagephagocytosisSIRPαsplice isoform

Identifiers

PMID40763927
PMCPMC12324903

What OpenQuestion holds

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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.