Evidence map›Paper›PMID 38503797›Full record

ArticleScientific reports2024

Galectin 7 leads to a relative reduction in CD4+ T cells, mediated by PD-1.

Guojin Wu, Wei Deng, Hsin-Yi Chen, Hye-Jeong Cho, Jaehyup Kim

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

10 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. MCell death & disease · 2025
    Article
  8. Proteogenomics Reveals Microproteins in Activated T Cells.Molecular & cellular proteomics : MCP · 2025
    Article
  9. Article
  10. 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

5 authors at 2 institutions in 2 countries.

Guojin WuDepartment of Pathology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX, 75390-9072, USA.
Wei DengDepartment of General Surgery, Beijing Friendship Hospital, Capital Medical University, Beijing, China.
Hsin-Yi ChenDepartment of Pathology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX, 75390-9072, USA.
Hye-Jeong ChoDepartment of Pathology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX, 75390-9072, USA.
Jaehyup KimDepartment of Pathology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX, 75390-9072, USA. jaehyup.kim@UTSouthwestern.edu.
The University of Texas Southwestern Medical Center · USBeijing Friendship Hospital · CN

Funding

The role of LILRB4 in AML progression and immune suppressionK08CA234544 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI KIM, JAEHYUP · 2019 to 2023
$657k
NCI NIH HHS K08 CA234544U.S. Department of Health & Human Services | NIH | National Cancer Institute (NCI) 5K08CA234544
6 · The paper itself

Abstract

The role of glycan-binding proteins as an activator of immune regulatory receptors has gained attention recently. We report that galectin 7 reduced CD4+ T cell percentage in both in vitro culture and mouse tumor models. Immunohistochemical staining of esophageal cancer patient samples showed a lower percentage of CD4+ cells in the galectin 7 high area. The lack of CD4+ T cell depletion by galectin 7 in PD-1 knockout mice supports the role of PD-1 in mediating the effects of galectin 7. The binding assays demonstrate that galectin 7 binds to the N-glycosylation of PD-1 on N74 and N116 sites and leads to the recruitment of SHP-2. NFAT suppressive activity of galectin 7 was abrogated upon overexpression of the dominant negative SHP-2 mutant or inhibition of PD-1 by siRNA. Glycosylation of PD-1 has been reported to play a critical role in surface expression, stability, and interaction with its ligand PD-L1. This report further expands the significance of PD-1 glycosylation and suggests that galectin 7, a glycan-binding protein, interacts with the immune regulatory receptor PD-1 through glycosylation recognition.

Indexed as

CD4-Positive T-LymphocytesProgrammed Cell Death 1 ReceptorAnimalsGalectinsGlycosylationHumansMicePolysaccharidesGalectinsLgals7 protein, mousePdcd1 protein, mousePolysaccharidesProgrammed Cell Death 1 Receptor

Identifiers

PMID38503797
PMCPMC10951237
OpenAlexW4392939092

What OpenQuestion holds

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LicenceCC BY
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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.