ArticleGlycobiology2017
Novel polysaccharide binding to the N-terminal tail of galectin-3 is likely modulated by proline isomerization.
Article in Glycobiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Developing Galectin-3-Targeted Therapeutics in Diseases: Three Distinct Galectin-3 Segments for Targeting.Expert reviews in molecular medicine · 2026Review
- Heterologous Interactions with Galectins and Chemokines and Their Functional Consequences.International journal of molecular sciences · 2023Review
- Article
- Galectin-3 inhibition as a potential therapeutic target in non-alcoholic steatohepatitis liver fibrosis.World journal of hepatology · 2023Review
- The Use of Endo-Cellulase and Endo-Xylanase for the Extraction of Apple Pectins as Factors Modifying Their Anticancer Properties and Affecting Their Synergy with the Active Form of Irinotecan.Pharmaceuticals (Basel, Switzerland) · 2022Article
- The Complex Biological Effects of Pectin: Galectin-3 Targeting as Potential Human Health Improvement?Biomolecules · 2022Review
- Degraded Arabinogalactans and Their Binding Properties to Cancer-Associated Human Galectins.International journal of molecular sciences · 2021Article
- Galectins as Checkpoints of the Immune System in Cancers, Their Clinical Relevance, and Implication in Clinical Trials.Biomolecules · 2020Review
- Novel Dextran-Supported Biological Probes Decorated with Disaccharide Entities for Investigating the Carbohydrate-Protein Interactions of Gal-3.Chembiochem : a European journal of chemical biology · 2019Article
- Galectins as Molecular Targets for Therapeutic Intervention.International journal of molecular sciences · 2018Review
- Messenger RNA Life-Cycle in Cancer Cells: Emerging Role of Conventional and Non-Conventional RNA-Binding Proteins?International journal of molecular sciences · 2018Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interactions between galectins and polysaccharides are crucial to many biological processes, and yet these are some of the least understood, usually being limited to studies with small saccharides and short oligosaccharides. The present study is focused on human galectin-3 (Gal-3) interactions with a 60 kDa rhamnogalacturonan RG-I-4 that we use as a model to garner information as to how galectins interact with large polysaccharides, as well as to develop this agent as a therapeutic against human disease. Gal-3 is unique among galectins, because as the only chimera-type, it has a long N-terminal tail (NT) that has long puzzled investigators due to its dynamic, disordered nature and presence of numerous prolines. Here, we use 15N-1H heteronuclear single quantum coherence NMR spectroscopy to demonstrate that multiple sites on RG-I-4 provide epitopes for binding to three sites on 15N-labeled Gal-3, two within its carbohydrate recognition domain (CRD) and one at a novel site within the NT encompassing the first 40 residues that are highly conserved among all species of Gal-3. Moreover, strong binding of RG-I-4 to the Gal-3 NT occurs on a very slow time scale, suggesting that it may be mediated by cis-trans proline isomerization, a well-recognized modulator of many biological activities. The NT binding epitope within RG-I-4 appears to reside primarily in the side chains of the polysaccharide, some of which are galactans. Our results provide new insight into the role of the NT in Gal-3 function.
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