Evidence map›Paper›PMID 8692888›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Expression of galectin-3 modulates T-cell growth and apoptosis.

R Y Yang, D K Hsu, F T Liu

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 271 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
271citing papers in PubMed, 1 pooled it
6.7field-weighted citation impact, top 3% 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

271 citing papers in PubMed, 1 synthesis or guideline pooled it, 782 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Review
  6. Generation of CCR4/CD7 Bispecific CAR-T Cells Resistant to Fratricide and Exhaustion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  7. The Role of Galectin-3 in Liver Inflammation and Fibrosis.Journal of inflammation research · 2026
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Biochemistry · 2024
    Article
  20. Review

211 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

R Y YangDepartment of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, CA 92037, USA.
D K Hsu
F T Liu
Scripps Research Institute · US

Funding

IGE BINDING PROTEIN--A MULTIFUNCTIONAL ANIMAL LECTINR01AI020958 · NIAID · UNIVERSITY OF CALIFORNIA DAVIS · PI LIU, FU-TONG · 1985 to 2008
$2.0M
NIAID NIH HHS AI20958
6 · The paper itself

Abstract

Galectin-3 is a member (if a large family of beta-galactoside-binding animal lectins. It has been shown that the expression of galectin-3 is upregulated in proliferating cells, suggesting a possible role for this lectin in regulation of cell growth. Previously, we have shown that T cells infected with human T-cell leukemia virus type I express high levels of galectin-3, in contrast to uninfected cells, which do not express detectable amounts of this protein. In this study, we examined growth properties of human leukemia T cells transfected with galectin-3 cDNA, and thus constitutively overexpressing this lectin. Transfectants expressing galectin-3 displayed higher growth rates than control transfectants, which do not express this lectin. Furthermore, galectin-3 expression in these cells confers resistance to apoptosis induced by anti-Fas antibody and staurosporine. Galectin-3 was found to have significant sequence similarity with Bcl-2, a well-characterized suppressor of apoptosis. In particular, the lectin contains the NWGR motif that is highly conserved among members of the Bcl-2 family and shown to be critical for the apoptosis-suppressing activity. We further demonstrated that galectin-3 interacts with Bc1-2 in a lactose-inhibitable manner. We conclude that galectin-3 is a regulator of cell growth and apoptosis and it may function through a cell death inhibition pathway that involves Bcl-2.

Indexed as

Amino Acid SequenceAntigens, DifferentiationApoptosisBase SequenceBloodCell DivisionCell LineDNA PrimersGalectin 3HumansLectinsMolecular Sequence DataProtein BindingProto-Oncogene ProteinsProto-Oncogene Proteins c-bcl-2Sequence Homology, Amino AcidAntigens, DifferentiationDNA PrimersGalectin 3LectinsProto-Oncogene ProteinsProto-Oncogene Proteins c-bcl-2

Identifiers

PMID8692888
PMCPMC39096
OpenAlexW2060490044

What OpenQuestion holds

Textmetadata
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.