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Galectin

About: Galectin is a research topic. Over the lifetime, 2076 publications have been published within this topic receiving 103409 citations. The topic is also known as: IPR001079 & Galectin.


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Journal ArticleDOI
TL;DR: The present results suggest that mimicking glycan complexity and microdomain occurrence on the glycodendrimersome surface can provide key insights into mechanisms to accomplish natural selectivity and specificity of lectins in structural and topological terms.
Abstract: Surface-presented glycans (complex carbohydrates) are docking sites for adhesion/growth-regulatory galectins within cell–cell/matrix interactions. Alteration of the linker length in human galectin-8 and single-site mutation (F19Y) are used herein to illustrate the potential of glycodendrimersomes with programmable glycan displays as a model system to reveal the functional impact of natural sequence variations in trans recognition. Extension of the linker length slightly reduces lectin capacity as agglutinin and slows down aggregate formation at low ligand surface density. The mutant protein is considerably less active as agglutinin and less sensitive to low-level ligand presentation. The present results suggest that mimicking glycan complexity and microdomain occurrence on the glycodendrimersome surface can provide key insights into mechanisms to accomplish natural selectivity and specificity of lectins in structural and topological terms.

66 citations

Journal ArticleDOI
H Idikio1
TL;DR: The galectin-3 expression pattern suggests that increasing histologic grade of breast cancer leads to reduced expression of galectIn-3 and possibly reduced matrix binding and increased cancer cell motility.
Abstract: Galectins (S-type lectins) are a family of low-molecular weight, calcium-independent, mannose-binding lectins with functions in cell growth, cell activation, cell-cell and cell-matrix adhesion including binding to carcinoembryonic antigens and laminin and metalloproteinase. Anti-galectin antisera can inhibit metastases of rat prostate cancers and human melanomas. To define the role of galectins in human breast cancer, the expression of galectin-3 were determined in 27 invasive breast cancers by immunohistochemical methods. The histologic grades of excised breast cancers were determined and immunohistochemical staining for galectin-3 (1: 1000 dilution of anti-galectin rat polyclonal antibody) was defined by scoring the intensity and distribution of staining (0-3+). The mean age of breast cancer patients was 63 years for 20 grade II breast cancers and 56 years for 7 grade III breast cancers. The mean immunohistochemical staining score for grade II breast cancers was 3. 7 (20% less than 2, 80% 3-6) and 2.5 for grade III (71.4% less than 2 and 28.6% 3-6). The galectin-3 expression pattern suggests that increasing histologic grade of breast cancer leads to reduced expression of galectin-3 and possibly reduced matrix binding and increased cancer cell motility.

66 citations

Journal ArticleDOI
TL;DR: The library approach is defined as a facile route for the discovery of selective (glyco)peptide-based galectin inhibitors and inhibitory activity on carbohydrate-dependent galECTin binding was tested by solid-phase and cell assays.

66 citations

Journal ArticleDOI
TL;DR: Crystal structure of the human galectin-9 N-terminal carbohydrate recognition domain in complex with N-acetyllactosamine dimers and trimers revealed that the galectins can recognize internal N-ACetyllACTosamine units within poly-N-actyllactOSamine chains.
Abstract: Galectins are a family of β-galactoside-specific lectins bearing a conserved carbohydrate recognition domain. Interactions between galectins and poly-N-acetyllactosamine sequences are critical in a variety of biological processes. Galectin-9, a member of the galectin family, has two carbohydrate recognition domains at both the N- and C-terminal regions. Here we report the crystal structure of the human galectin-9 N-terminal carbohydrate recognition domain in complex with N-acetyllactosamine dimers and trimers. These complex structures revealed that the galectin-9 N-terminal carbohydrate recognition domain can recognize internal N-acetyllactosamine units within poly-N-acetyllactosamine chains. Based on these complex structures, we propose two putative recognition modes for poly-N-acetyllactosamine binding by galectins.

66 citations

Journal ArticleDOI
TL;DR: Pilot data is provided showing that HCV‐infected human hepatocytes express higher levels of Gal‐9 and TGF‐β, and upregulate Tim‐3 expression and regulatory cytokines T GF‐β/IL‐10 in co‐cultured human CD4+ T cells, suggesting that Tim‐ 3/Gal‐9 interactions may regulate human Foxp3+ Treg‐cell development and function during HCV infection.
Abstract: HCV is remarkable at disrupting human immunity to establish chronic infection. The accumulation of Treg cells at the site of infection and upregulation of inhibitory signaling pathways (such as T-cell Ig and mucin domain protein-3 (Tim-3) and galectin-9 (Gal-9)) play pivotal roles in suppressing antiviral effector T (Teff) cells that are essential for viral clearance. While Tim-3/Gal-9 interactions have been shown to negatively regulate Teff cells, their role in regulating Treg cells is poorly understood. To explore how Tim-3/Gal-9 interactions regulate HCV-mediated Treg-cell development, here we provide pilot data showing that HCV-infected human hepatocytes express higher levels of Gal-9 and TGF-β, and upregulate Tim-3 expression and regulatory cytokines TGF-β/IL-10 in co-cultured human CD4+ T cells, driving conventional CD4+ T cells into CD25+Foxp3+ Treg cells. Additionally, recombinant Gal-9 protein can transform TCR-activated CD4+ T cells into Foxp3+ Treg cells in a dose-dependent manner. Importantly, blocking Tim-3/Gal-9 ligations abrogates HCV-mediated Treg-cell induction by HCV-infected hepatocytes, suggesting that Tim-3/Gal-9 interactions may regulate human Foxp3+ Treg-cell development and function during HCV infection.

65 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023182
2022176
2021107
2020120
201995
2018119