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.

Essentials of Glycobiology

Abstract: General principles - historical background and overview saccharide structure and nomenclature evolution of glycan diversity protein-glycan Interactions exploring the biological roles of glycans biosynthesis, metabolism, and function - monosaccharide metabolism N-glycans O-glycans glycosphingolipids glycophospholipid anchors proteoglycans and glycosaminoglycans other classes of golgi-derived glycans nuclear and cytoplasmic glycosylation the O-GlcNAc modification sialic acids structures common to different types of glycans glycosyltransferases degradation and turnover of glycans glycosylation in "model" organisms glycobiology of plant cells bacterial polysaccharides proteins that recognize glycans - discovery and classification of animal lectins P-type lectins I-type lectins C-type lectins selectins S-type lectins (galectins) microbial glycan-binding proteins glycosaminoglycan-binding proteins plant lectins glycans in genetic disorders and disease - genetic disorders of glycosylation in cultured cells naturally occurring genetic disorders of glycosylation in animals determining glycan function using genetically modified mice glycosylation changes in ontogeny and cell activation glycosylation changes in cancer glycobiology of protozoal and helminthic parasites acquired glycosylation changes in human disease methods and applications - structural analysis and sequencing of glycans chemical and enzymatic synthesis of glycans natural and synthetic inhibitors of glycosylation glycobiology in biotechnology and medicine.

The Tim-3 ligand galectin-9 negatively regulates T helper type 1 immunity

Abstract: Tim-3 is a T helper type 1 (T(H)1)-specific cell surface molecule that seems to regulate T(H)1 responses and the induction of peripheral tolerance. However, the identity of the Tim-3 ligand and the mechanism by which this ligand inhibits the function of effector T(H)1 cells remain unknown. Here we show that galectin-9 is the Tim-3 ligand. Galectin-9-induced intracellular calcium flux, aggregation and death of T(H)1 cells were Tim-3-dependent in vitro, and administration of galectin-9 in vivo resulted in selective loss of interferon-gamma-producing cells and suppression of T(H)1 autoimmunity. These data suggest that the Tim-3-galectin-9 pathway may have evolved to ensure effective termination of effector T(H)1 cells.

Galectins as modulators of tumour progression

Abstract: Galectins are a family of animal lectins with diverse biological activities. They function both extracellularly, by interacting with cell-surface and extracellular matrix glycoproteins and glycolipids, and intracellularly, by interacting with cytoplasmic and nuclear proteins to modulate signalling pathways. Current research indicates that galectins have important roles in cancer; they contribute to neoplastic transformation, tumour cell survival, angiogenesis and tumour metastasis. They can modulate the immune and inflammatory responses and might have a key role helping tumours to escape immune surveillance. How do the different members of the Galectin family contribute to these diverse aspects of tumour biology?

Feature-based prediction of non-classical and leaderless protein secretion.

Abstract: We present a sequence-based method, SecretomeP, for the prediction of mammalian secretory proteins targeted to the non-classical secretory pathway, i.e. proteins without an N-terminal signal peptide. So far only a limited number of proteins have been shown experimentally to enter the non-classical secretory pathway. These are mainly fibroblast growth factors, interleukins and galectins found in the extracellular matrix. We have discovered that certain pathway-independent features are shared among secreted proteins. The method presented here is also capable of predicting (signal peptide-containing) secretory proteins where only the mature part of the protein has been annotated or cases where the signal peptide remains uncleaved. By scanning the entire human proteome we identified new proteins potentially undergoing non-classical secretion. Predictions can be made at http://www.cbs.dtu.dk/services/SecretomeP.