Topic
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.
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TL;DR: Gal-3 inhibition appears to improve renal disease in several pathological conditions, thus justifying the development of multiple drug inhibitors, from its role as a biomarker to its potential as a therapeutic agent.
Abstract: Galectin-3 (Gal-3) is a 30KDa lectin implicated in multiple pathophysiology pathways including renal damage and fibrosis. Gal-3 binds β-galactoside through its carbohydrate-recognition domain. From intra-cellular to extra-cellular localization, Gal-3 has multiple roles including transduction signal pathway, cell-to-cell adhesion, cell to extracellular matrix adhesion, and immunological chemoattractant protein. Moreover, Gal-3 has also been linked to kidney disease in both preclinical models and clinical studies. Gal-3 inhibition appears to improve renal disease in several pathological conditions, thus justifying the development of multiple drug inhibitors. This review aims to summarize the latest literature regarding Gal-3 in renal pathophysiology, from its role as a biomarker to its potential as a therapeutic agent.
6 citations
TL;DR: A combination of site-directed mutagenesis of the N-terminal lectin domain of galectin LEC-1 and an analysis of the sugar-binding profile by frontal affinity chromatography to identify the amino acid residues important for this recognition of A-hexasaccharide are identified.
Abstract: The basic disaccharide structure recognized by galectin family members is the lactosamine-like structure Galβ1-4(3)Glc(NAc). In galectins, eight highly conserved amino acid residues participate in the recognition of this basic structure. Each galectin seems to mediate diverse biological functions due to recognition of different modifications of the basic disaccharide Galβ1-4(3)Glc(NAc), but there is very little information about which amino acid residue in galectin is responsible for recognizing these modifications. The 32-kDa galectin LEC-1 of the nematode Caenorhabditis elegans is composed of two domains, each of which is homologous to vertebrate 14-kDa-type galectins. Although both lectin domains have an affinity for N-acetyllactosamine (Galβ1-4GlcNAc)-containing, N-linked, complex-type sugar chains, the N-terminal lectin domain of LEC-1 recognizes blood group A saccharide (GalNAcα1-3(Fucα1-2)Galβ1-3GlcNAc), whereas this saccharide is only poorly recognized by the C-terminal domain. Here, we used a combination of site-directed mutagenesis of the N-terminal lectin domain of galectin LEC-1 and an analysis of the sugar-binding profile by frontal affinity chromatography to identify the amino acid residues important for this recognition. Our results indicate that Thr41 in the N-terminal lectin domain of LEC-1 is important for its affinity for A-hexasaccharide.
6 citations
TL;DR: Study of the galectin of lymphatic filarial parasite Wb-Gal shows that it is a member of the lectin family of proteins binding to different carbohydrates and may have an important role in the pathophysiology of filarial infection which needs to be investigated in greater detail.
6 citations
TL;DR: Immunocytochemical examination of galectin 4 confirmed more highly elevated levels of the protein in endocrine, parietal, and chief cells in weaned rats than in suckling rats, suggesting that galectIn 4 is implicated in nuclear events and perhaps in secretory processes.
6 citations
18 Dec 2012
6 citations