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.

Surface-bound galectin-4 regulates gene transcription and secretion of chemokines in human colorectal cancer cell lines.

Abstract: One long-term complication of chronic intestinal inflammation is the development of colorectal cancer. However, the mechanisms linking inflammation to the colorectal tumorigenesis are poorly defined. Previously, we have demonstrated that galectin-4 is predominantly expressed in the luminal epithelia of the gastrointestinal tract, and its loss of expression plays a key role in the colorectal tumorigenesis. However, the mechanism by which galectin-4 regulates inflammation-induced tumorigenesis is unclear. Here, we show that galectin-4 secreted by the colorectal cancer cell lines was bound to the cell surface. Neutralization of surface-bound galectin-4 with anti-galectin-4 antibody resulted in increased cell proliferation with concomitant secretion of several chemokines into the extracellular medium. Neutralization of the surface-bound galectin-4 also resulted in the up-regulation of transcription of 29 genes, several of which are components of multiple inflammation signaling pathways. In an alternate experiment, binding of recombinant galectin-4 protein to cell surface of the galectin-4-negative colorectal cancer cells resulted in increased p27, and decreased cyclin D1 and c-Myc levels, leading to cell cycle arrest and apoptosis. Together, these data demonstrated that surface-bound galectin-4 is a dual function protein-down-regulating cell proliferation and chemokine secretion in galectin-4-expressing colorectal cancer cells on one hand and inducing apoptosis in galectin-4-negative colorectal cancer cells on the other hand.

Burn control, an adipocyte-specific function for galectin-12

Abstract: Families of molecules often have similar functions—think of kinases, transcription factors, chemokines, or Toll-like receptors. The galectins, an evolutionarily ancient family of carbohydrate binding proteins found in organisms from multicellular fungi to humans, are different (1, 2). Galectins are a family of lectins; the family designation is based on highly conserved structural features, particularly the conserved carbohydrate recognition domains (CRDs) that define the proteins as lectins. In contrast, the pleiotropic functions of galectins do not seem to be conserved. Based on the cell type investigated, galectins have been reported to regulate cell proliferation, migration, adhesion, differentiation, survival, and death, and they also positively and negatively regulate host defense against microbial pathogens. Extracellular functions of galectins typically depend on the carbohydrate binding properties of the lectins, but many different glycoprotein receptors can be recognized by various galectins if the glycoprotein receptors bear the appropriate glycan ligands, resulting in the vast array of cellular functions triggered by galectin binding. In addition, galectins are also found intracellularly, where for example, protein–protein interactions at the cytoplasmic face of the plasma membrane, nucleus, and mitochondria promote association of galectin-3 with K-Ras, β-catenin, and Bcl-2 family members to regulate oncogenesis and cell death (3–5). In PNAS, the work by Yang et al. (6) reports an unexpected function for a galectin, galectin-12, at an unexpected subcellular location.

Inhibitors against galectins

Abstract: The present invention relates to novel compounds, the use of said compounds as a medicament as well as for the manufacture of a medicament for treatment of disorders relating to the binding of galectin to receptors in a mammal. Said galectin is preferably a galectin 3.