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Molecular structure of
|Lecster ID:307|| Edit Entry |
| Common Nomenclature:||Galectin III|
|Class:||Chimera S-lectin or |
|Characterization Notes:||A soluble beta-galactoside-binding lectin, Galectin-3 has been shown to be involved in cell adhesion and activation of immune cells and plays a significant role in cell to extracellular matrix interactions. galectin-3 is expressed in activated murine T lymphocytes including CD4+ and CD8+ T cells but not in resting T cells. See: J Leukoc Biol 2001 Apr;69(4):555-64 galectin-3 mediates genistein-induced G(2)/M arrest and inhibits apoptosis. See: Carcinogenesis 2000 Nov;21(11):1941-5 Up-regulation of galectin-1 in fibroblasts and galectin-3 in ductular complexes suggests a role of these lectins in tissue remodeling in chronic pancreatitis. See: Lab Invest 2000 Aug;80(8):1233-41 galectin has a binding capacity for various glycoconjugates including IgE. See: J Leukoc Biol 1999 Oct;66(4):644-9|
|Biological Activity:||Galectin-3 is an endogenous beta-galactoside-binding protein with specificity for type I and II ABH blood group epitopes and poly-N-acetyllactosamine glycan-containing cell surface glycoproteins and is the major nonintegrin cellular laminin-binding protein. galectin-3 is expressed at an elevated level in a wide range of neoplasms, and expression was shown to be associated in some tumor cell systems with metastases. The blockage of galectin-3 expression led to a significant suppression of tumor growth in nude mice, evidence that galectin-3 expression is necessary for the maintenance of the transformed and tumorigenic phenotype of MDA-MB-435 breast carcinoma cells. Galectin-3 regulates the adhesive interaction between breast carcinoma cells and elastin. See: J Cell Biochem 1999 Dec 1;75(3):505-14 See: Clin Cancer Res 2001 Mar;7(3):661-8 |
The tumor-associated carbohydrate Thomsen-Friedenreich antigen (T antigen) and beta-galactoside binding lectins (galectins) have been implicated in tumor cell adhesion and tissue invasion. Both galectin-1 and galectin-3 participate in the adhesion of the MDA-MB-435 cells to the endothelium. Clustering of galectin-3 on endothelial cells at the sites of the contact with tumor cells is consistent with its possible interaction with T antigen on cancer cells. See: Cancer Res 2000 May 15;60(10):2584-8 Overexpression of galectin-3 in thyroid papillary carcinoma cells is necessary for the maintenance of transformed phenotype, and suggest galectin-3 as a potential target for therapeutic interventions in the future. See: Int J Oncol 2001 Apr;18(4):787-92 High levels of galectin-3 in metastatic cancer cells suggest an impact on metastasis formation. See: J Histochem Cytochem 2001 Apr;49(4):539-49 galectin-3 was localized and up-regulated in foam cells at human atherosclerotic lesions, which suggests that galectin-3 plays an important role in formation of atherosclerotic lesions in vivo, by modulating endocytic uptake of AGE-proteins and modified LDLs. See: Biochem Biophys Res Commun 2001 Feb 2;280(4):1183-8 Data demonstrate that galectin-3 is downregulated in prostate cancer. The altered downregulation pattern of galectin-3 observed between tumor stages suggests different roles for galectin-3 in the progression of prostate cancer. See: Prostate 2000 Jul 1;44(2):118-23
|Specificity:||Deta-galactoside sugars. The data suggest that fetuin is a natural modulator of galectin-3 secretion/release and that the secreted galectin-3 modulates the activity of cell surface receptors for extracellular matrix proteins. See: Cancer Res 2001 Mar 1;61(5):1869-73|
|References:||J. Biol. Chem., 273, 13047-13052, 1998|
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