Galectin-3
Galectin-3 is a β-galactoside-binding lectin that regulates cell adhesion, activation, migration, signaling, apoptosis, immune reactions, and neoplastic transformation[1][2]. Mechanistically, its conserved carbohydrate-recognition domain binds β-galactosides, while its intrinsically disordered N-terminal region enables multisite self-association and functional multivalency[1][2]. In inflammation, galectin-3 acts across acute inflammation, chronic inflammation, and tissue fibrogenesis, making it relevant to fibrosis-oriented experimental design[3]. In lung fibrosis models, galectin-3 deficiency or pharmacological inhibition reduced TGF-β1-driven epithelial-mesenchymal transition, myofibroblast activation, and collagen production[4]. More recent human lung fibroblast and IPF lung-slice data show that extracellular galectin-3 promotes integrin-mediated TGF-β1 activation and interacts with αv integrins and TGFβRII in a glycosylation-dependent manner[5]. Compared with related isoforms, galectin-3 is distinguished as the only vertebrate chimera-type galectin, containing one CRD linked to a long proline- and glycine-rich N-terminal domain[1]. For experimental applications, galectin-3 inhibitors that target the carbohydrate-recognition domain blocked integrin colocalization and reduced fibrotic mediators in IPF-derived lung tissue models[5]. In patients with idiopathic pulmonary fibrosis, inhaled TD139 showed target engagement and supported galectin-3 inhibition as a translational research approach[6].- Isoform distinction: galectin-3 differs structurally from prototype and tandem-repeat galectins through its chimera architecture[1]. - Research application: galectin-3 inhibition supports fibrosis studies involving TGF-β1 activation, integrins, and IPF models[4][5][6].
References:
- [1]. Dumic J, et al. Galectin-3: an open-ended story. Biochim Biophys Acta. 2006 Apr;1760(4):616-35. [Content Brief]
- [2]. Lin YH, et al. The intrinsically disordered N-terminal domain of galectin-3 dynamically mediates multisite self-association of the protein through fuzzy interactions. J Biol Chem. 2017 Oct 27;292(43):17845-17856. [Content Brief]
- [3]. Henderson NC, et al. The regulation of inflammation by galectin-3. Immunol Rev. 2009 Jul;230(1):160-71. [Content Brief]
- [4]. Mackinnon AC, et al. Regulation of transforming growth factor-β1-driven lung fibrosis by galectin-3. Am J Respir Crit Care Med. 2012 Mar 1;185(5):537-46. [Content Brief]
- [5]. Calver JF, et al. Defining the mechanism of galectin-3-mediated TGF-β1 activation and its role in lung fibrosis. J Biol Chem. 2024 Jun;300(6):107300. [Content Brief]
- [6]. Hirani N, et al. Target inhibition of galectin-3 by inhaled TD139 in patients with idiopathic pulmonary fibrosis. Eur Respir J. 2021 May 27;57(5):2002559. [Content Brief]
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Galectin-3 Related Products (25)
Related Products (25)
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Antibodies (1)
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Galectin-3-IN-2
0 ImagesCat. No.: HY-144313CAS No.: 2883648-71-1Galectin-3-IN-2 (Compound 9) is a potent multivalent inhibitor of galectin-3 (Gal-3; IC50=8.3 μM). Galectin-3 participates in many cancer-related metabolic processes.
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Galectin-3-IN-6
0 ImagesCat. No.: HY-173235CAS No.: 2604662-64-6Galectin-3-IN-6 is a human and murine galectin-3 (Gal-3) inhibitor, with an IC50 of 12 nM against human galectin-3, an IC50 of 12.6 nM against mutant murine galectin-3 (V160A), and a Kd of 13 nM for human galectin-3, as well as oral bioavailability. Galectin-3-IN-6 reduces the levels of liver fibrosis markers type I collagen and α-smooth muscle actin in mouse models of acute liver injury and fibrosis. Galectin-3-IN-6 can be used for the research of acute liver injury and fibrosis.
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Galectin-3 antagonist 2
0 ImagesCat. No.: HY-146809CAS No.: 2921603-02-1Galectin-3 is a β Galactoside specific carbohydrate recognition protein (lectin) has the ability to promote the migration of B cell precursor acute lymphoblastic leukemia (BCP-ALL) cells and withstand drug research.
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CHI3L1-IN-6
0 ImagesCat. No.: HY-180937CAS No.: 1914772-75-0CHI3L1-IN-6 (Compound 9e) is a CHI3L1 inhibitor with a Kd of 19.11 μM for hCHI3L1. CHI3L1-IN-6 blocks CHI3L1-Galectin-3 interaction. CHI3L1-IN-6 reduces STAT3 signaling. CHI3L1-IN-6 exhibits anti-cancer activity against glioblastoma.
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4A-MPLA ammonium
0 ImagesCat. No.: HY-N16021CAS No.: 2260669-09-64A-MPLA ammonium is an orally active TLR4 agonist. 4A-MPLA ammonium induces TLR4 endocytosis dependent on Cdc42 and galectin-3, triggering TRIF-mediated signaling and sustained IFN-β production. 4A-MPLA ammonium promotes lipid droplet formation, upregulates interferon-stimulated genes and type I IFN signaling genes, downregulates lysosome/phagosome function genes, and modulates tolerogenic dendritic cell function. 4A-MPLA ammonium can be used for the research of colitis.
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