-
Product Directory
Custom Product
-
Services Offered
Custom Capabilities
-
|
|
||||||||||||||||||||||||
|
Galectins are a family of animal carbohydrate binding proteins; the name is from their description as β–galactoside-specific lectins. They have been strongly implicated in inflammation and cancer and may be useful as targets for the development of new anti-inflammatory and anti-cancer therapies. Galectins occur at high concentration in a limited range of cell types, different for each galectin. Galectins bind to sugar molecules on the surface of cells. All galectins bind lactose and other β-galactosides, but they differ in their affinity for more complex saccharides.1 The galectins are defined by their structural similarities in their carbohydrate recognition domains (CRD) and by their affinity for β-galactosides; fourteen human members have been reported so far.2 The galectins have been classified into three classes, prototype, chimera, and tandem-repeat galectins. The prototype galectins (-1, -2, -5, -7, -10, -11, -13, -14), all containing one CRD and are either monomers or noncovalent homodimers. The only chimera galectin currently identified (galectin-3) contains one CRD connected to a non-lectin domain. The tandem-repeat galectins (-4, -6, -8, -9, -12) consist of two CRDs joined by a linker peptide. Extracellular galectins crosslink cell-surface and extracellular glycoproteins and may thereby modulate cell adhesion and induce intracellular signals. Galectins may also bind intracellular non-carbohydrate ligands and have intracellular regulatory roles in processes such as RNA splicing, apoptosis, and, suggested most recently, the cell cycle.1 Galectin-3, G5170 Galectin-3, also called Mac-2, L29, CBP35 and εBP, is a chimera galectin that is expressed in tumor cells, macrophages, activated T cells, epithelial cells, and fibroblasts. It binds a variety of matrix glycoproteins including laminin and fibronectin. Intracellularly, galectin-3 acts to prevent apoptosis. Depending on the cell type, galectin-3 can be localized in the extracellular matrix, the cell surface, in the cytoplasm, or in the nucleus. Galectin-3 has been shown to exhibit proinflammatory activities in vitro and in vivo; it induces pro-inflammatory and inhibits Th2 type cytokine production.3 High levels of circulating galectin-3 have been shown to correlate with the malignancy potential of several types of cancer. Galectin-3 is known to play a role in tumor growth, metastasis, and cell-to-cell adhesion. It also serves as a preferred substrate for matrix metalloproteinase-9 (MMP-9), M4809 and M1552.4 Human and mouse Galectin-3 share approximately 80% homology in their amino acid sequence.5
Galectin-3C, G5295 Galectin-3C is a truncated form of galectin-3 that contains the carboxy-terminus carbohydrate-binding domain. Recombinant galectin-3C competes with endogenous galactin-3 for carbohydrate binding sites and acts as a negative inhibitor of galectin-36 in promoting cell adhesion7 and cell signaling. Galectin-3C has been found to be effective in reducing metastases and tumor volumes and weights in primary tumors in an orthotropic nude mouse model of human breast cancer.8
Galectin-8, G3670 Galectin-8, also known as prostate carcinoma tumor antigen 1 (PCTA1) in human, is a tandem repeat-type galectin. High levels of circulating galectin-8 have been shown to correlate with lung carcinomas, certain forms of prostate carcinomas, as well as other tumor cells.9 It binds to a subset of cell surface integrins to modulate ECM-integrin interactions. It acts as a physiological modulator of cell adhesion and cellular growth, and may be involved in neoplastic transformation.10,11,12 Human and mouse galectin-8 share approximately 80% homology in their amino acid sequence.5
|
|||||||||||||||||||||||
|
|
||||||||||||||||||||||||
