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.

The Galectin Family as Molecular Targets: Hopes for Defeating Pancreatic Cancer.

Abstract: Galectins are a family of proteins that bind β-galactose residues through a highly conserved carbohydrate recognition domain. They regulate several important biological functions, including cell proliferation, adhesion, migration, and invasion, and play critical roles during embryonic development and cell differentiation. In adults, different galectin members are expressed depending on the tissue type and can be altered during pathological processes. Numerous reports have shown the involvement of galectins in diseases, mostly inflammation and cancer. Here, we review the state-of-the-art of the role that different galectin family members play in pancreatic cancer. This tumor is predicted to become the second leading cause of cancer-related deaths in the next decade as there is still no effective treatment nor accurate diagnosis for it. We also discuss the possible translation of recent results about galectin expression and functions in pancreatic cancer into clinical interventions (i.e., diagnosis, prediction of prognosis and/or therapy) for this fatal disease.

Possible regulatory role of galectin-9 on Ascaris suum-induced eosinophilic lung inflammation in mice.

Abstract: Background: Galectin-9 (Gal-9) is a member of the galectin family of lectins that exhibit binding affinity for β-galactosides. We found a T cell line-derived Gal-

Characterization of a neutralizing anti-human galectin-1 monoclonal antibody with angioregulatory and immunomodulatory activities

Abstract: Galectins, a family of highly conserved β-galactoside-binding proteins, control tumor progression by modulating different hallmarks of cancer. Galectin-1 (Gal-1), a proto-type member of this family, plays essential roles in tumor angiogenesis and immunosuppression by cross-linking glycosylated receptors on the surface of endothelial and immune cells. Targeted disruption of Gal-1 suppresses tumor growth by counteracting aberrant angiogenesis and reinforcing antitumor immunity in several experimental settings. Given the multiple therapeutic benefits associated with Gal-1 blockade, several Gal-1 inhibitors, including glycan-based competitors, antagonistic peptides, aptamers and neutralizing monoclonal antibodies, have been designed and evaluated in pre-clinical tumor models. Here we report the biochemical and functional characterization of a newly developed neutralizing anti-human Gal-1 monoclonal antibody (Gal-1-mAb3), which specifically recognizes a unique epitope in Gal-1 protein and exerts both angioregulatory and immunomodulatory activities. Blockade of Gal-1 function using Gal-1-mAb3, might be relevant not only in cancer but also in other pathologic conditions characterized by aberrant angiogenesis and uncontrolled immunosuppression.

Carbohydrate specificity of chicken and human tandem-repeat-type galectins-8 in composition of cells.

Abstract: The network of adhesion/growth-regulatory galectins in chicken (chicken galectin, CG) has only one tandemrepeat-type protein, CG8. Using a cell-based assay and probing galectin reactivity with a panel of fluorescent neoglycoconjugates (glycoprobes), its glycan-binding profile was determined. For internal validation, human galectin-8 (HG8) was tested. In comparison to HG8, CG8 showed a rather similar specificity: both galectins displayed high affinity to blood group ABH antigens as well as to 3′-sialylated and 3′-sulfated lactosamine chains. The most remarkable difference was found to be an ability of HG8 (but not CG8) to bind the disaccharide Galβ1-3GlcNAc (Lec) as well as branched and linear oligolactosamines. The glycan-binding profile was shown to be influenced by glycocalix of the cell, where the galectin is anchored. Particularly, glycosidase treatment of galectin-loaded cells led to the change of the profile. Thus, we suppose the involvement of cis-glycans in the interaction of cell-anchored galectins with external glycoconjugates.

Galectins in Regulation of Apoptosis

Abstract: The term “galectins” was given in 1994 to a family of animal lectins that bind to β-galactosides and contain comparable sequences of amino acids in their genes and proteins [1]. At that time, there were just four identified members, but now 15 members have been described in mammals, with similar proteins found in various animal species, as well as in insects and plants.