ArticleThe Journal of biological chemistry2008
Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed.
- Trial
- Article
- Aging and Thymosin Alpha-1.International journal of molecular sciences · 2025Review
- Galectin-9-An Emerging Glyco-Immune Checkpoint Target for Cancer Therapy.International journal of molecular sciences · 2025Review
- Galectin-3 disrupts tight junctions of airway epithelial cell monolayers by inducing expression and release of matrix metalloproteinases upon influenza A infection.Glycobiology · 2025Article
- It's about TIME - Gal-9 as a potential immunotherapeutic target in pancreatic ductal adenocarcinoma.Frontiers in immunology · 2025Review
- Galectin-9 as a new biomarker of acute-on-chronic liver failure.Scientific reports · 2024Article
- Knockdown of the Shwachman-Diamond syndrome gene, SBDS, induces galectin-1 expression and impairs cell growth.International journal of hematology · 2024Article
- Galectin-9 - ligand axis: an emerging therapeutic target for multiple myeloma.Frontiers in immunology · 2024Review
- A new emerging target in cancer immunotherapy: Galectin-9 (LGALS9).Genes & diseases · 2023Review
- KLF12 overcomes anti-PD-1 resistance by reducing galectin-1 in cancer cells.Journal for immunotherapy of cancer · 2023Article
- Galectin-9 in Gastroenterological Cancer.International journal of molecular sciences · 2023Review
- Decoding Strategies to Evade Immunoregulators Galectin-1, -3, and -9 and Their Ligands as Novel Therapeutics in Cancer Immunotherapy.International journal of molecular sciences · 2022Review
- The interplay of galectins-1, -3, and -9 in the immune-inflammatory response underlying cardiovascular and metabolic disease.Cardiovascular diabetology · 2022Review
- Chemokines modulate glycan binding and the immunoregulatory activity of galectins.Communications biology · 2021Article
- Review
- Imitating evolution's tinkering by protein engineering reveals extension of human galectin-7 activity.Histochemistry and cell biology · 2021Article
- Immune Checkpoint Inhibitors in Colorectal Cancer: Challenges and Future Prospects.Biomedicines · 2021Review
- Effect of the use of Galectin-9 and blockade of TIM-3 receptor in the latent cellular reservoir of HIV-1.Journal of virology · 2021Article
- Molecular Identification and mRNA Expression Profiles of Galectin-9 Gene in Red Sea Bream (Animals : an open access journal from MDPI · 2021Article
15 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The galectin family of lectins regulates multiple biologic functions, such as development, inflammation, immunity, and cancer. One common function of several galectins is the ability to trigger T cell death. However, differences among the death pathways triggered by various galectins with regard to glycoprotein receptors, intracellular death pathways, and target cell specificity are not well understood. Specifically, galectin-9 and galectin-1 both kill thymocytes, peripheral T cells, and T cell lines; however, we have found that galectin-9 and galectin-1 require different glycan ligands and glycoprotein receptors to trigger T cell death. The two galectins also utilize different intracellular death pathways, as galectin-9, but not galectin-1, T cell death was blocked by intracellular Bcl-2, whereas galectin-1, but not galectin-9, T cell death was blocked by intracellular galectin-3. Target cell susceptibility also differed between the two galectins, as galectin-9 and galectin-1 killed different subsets of murine thymocytes. To define structural features responsible for distinct activities of the tandem repeat galectin-9 and dimeric galectin-1, we created a series of bivalent constructs with galectin-9 and galectin-1 carbohydrate recognition domains connected by different peptide linkers. We found that the N-terminal carbohydrate recognition domain and linker peptide contributed to the potency of these constructs. However, we found that the C-terminal carbohydrate recognition domain was the primary determinant of receptor recognition, death pathway signaling, and target cell susceptibility. Thus, carbohydrate recognition domain specificity, presentation, and valency make distinct contributions to the specific effects of different galectins in initiating T cell death.
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Registered trials
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