Evidence map›Paper›PMID 28548942›Full record

ArticleOncotarget2017

The N-terminal tail coordinates with carbohydrate recognition domain to mediate galectin-3 induced apoptosis in T cells.

Huiting Xue, Lu Liu, Zihan Zhao, Zhongyu Zhang, Yuan Guan, Hairong Cheng, Yifa Zhou, Guihua Tai

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 1 synthesis or guideline pooled it, 43 citations in OpenAlex.

  1. Pooled it
  2. Chimerolectins: Classification, structural architecture, and functional perspectives.Protein science : a publication of the Protein Society · 2025
    Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Apoptosis: aJournal for immunotherapy of cancer · 2023
    Review
  8. Review
  9. Review
  10. Review
  11. Physical tuning of galectin-3 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Targeting ERK-Hippo Interplay in Cancer Therapy.International journal of molecular sciences · 2020
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
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

8 authors at 1 institution in 1 country.

Huiting XueSchool of Life Sciences, Northeast Normal University, Changchun, China.
Lu LiuSchool of Life Sciences, Northeast Normal University, Changchun, China.
Zihan ZhaoSchool of Life Sciences, Northeast Normal University, Changchun, China.
Zhongyu ZhangSchool of Life Sciences, Northeast Normal University, Changchun, China.
Yuan GuanSchool of Life Sciences, Northeast Normal University, Changchun, China.
Hairong ChengSchool of Life Sciences, Northeast Normal University, Changchun, China.
Yifa ZhouSchool of Life Sciences, Northeast Normal University, Changchun, China.
Guihua TaiSchool of Life Sciences, Northeast Normal University, Changchun, China.
Northeast Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Galectin-3 is a galectin with a unique flexible N-terminal tail (NT) connected to the conserved carbohydrate recognition domain (CRD). Galectin-3 is associated with tumor immune tolerance and exhibits an ability to induce T cell apoptosis. We used Jurkat, Jurkat E6-1 and CEM T-cell lines and human peripheral blood mononuclear cells (PBMCs) to investigate the specific roles of the CRD and NT in inducing T cell apoptosis. Galectin-3 triggered sustained extracellular signal-regulated kinase (ERK) phosphorylation that induced apoptosis. ERK was situated upstream of caspase-9 and was independently activated by reactive oxygen species (ROS) and protein kinase C (PKC). The first twelve NT residues had no role in the apoptosis. Residues 13-68 were essential for activating ROS, but did not activate PKC. However, residues 69-110 were required for activation of PKC. An NT fragment and a NT-specific antibody antagonized the apoptosis triggered by full-length galectin-3 further supporting our findings. These findings indicate the CRD and NT play important roles during induction of T cell apoptosis, which suggests their potential as therapeutic targets for reversing cancer immune tolerance.

Indexed as

ApoptosisCarbohydratesProtein Interaction Domains and MotifsCaspase 9Cell Line, TumorGalectin 3HumansLeukocyte Common AntigensLeukocytes, MononuclearMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3PhosphorylationProtein Kinase CReactive Oxygen SpeciesT-LymphocytesCarbohydratesCaspase 9Galectin 3Leukocyte Common AntigensMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Protein Kinase CReactive Oxygen SpeciesapoptosisERKgalectin-3ROStruncated protein

Identifiers

PMID28548942
PMCPMC5564810
OpenAlexW2612876234

What OpenQuestion 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 OpenQuestion graph.