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.

Galectins in the Pathogenesis of Cerebrovascular Accidents: An Overview.

Abstract: Due to limitations of neuroimaging, such as the isodense appearance of blood to neuronal tissue in subacute hemorrhagic stroke, a body of studies have been performed to evaluate candidate biomarkers which may aid in accurate determination of cerebrovascular accident type. Beyond aiding in the delineation of stroke cause, biomarkers could also confer useful prognostic information to help clinicians plan use of resources. One of the candidate biomarkers studied for detection of cerebrovascular accident (CVA) includes a class of proteins called galectins. Galectins bind β-galactoside through a highly conserved carbohydrate recognition domain, endowing an ability to interact with carbohydrate moieties on glycoproteins, some of which are relevant to CVA response. Furthermore, galectins-1, -2, -3, -9, and -12 are expressed in tissues relevant to CVA, and some exhibit characteristics (eg, extracellular secretion) that could render feasible their detection in serum. Galectins-1 and -3 appear to have the largest amounts of preclinical evidence, consistently demonstrating increased activity and expression levels during CVA. However, a lack of standardization of biochemical assays across cohort studies limits further translation of these basic science studies. This review aims to increase awareness of the biochemical roles of galectins in CVA, while also highlighting challenges and remaining questions preventing the translation of basic science observations into a clinically useful test.

OUP accepted manuscript

Abstract: Scheme for plasma Galectin-3 potentiating agonist-induced platelet activation and hyper-reactivity. Delineation of underlying signalling pathways. Effect of Galectin-3 inhibitor TD139 on platelet hyper-reactivity and thrombosis. Scheme for plasma Galectin-3 potentiating agonist-induced platelet activation and hyper-reactivity. Delineation of underlying signalling pathways. Effect of Galectin-3 inhibitor TD139 on platelet hyper-reactivity and thrombosis.

Galectins: Structures, Binding Properties and Function in Cell Adhesion

Abstract: Galectins are nearly ubiquitous distributed ┚-galactoside binding proteins which share a common amino acid sequence, the carbohydrate recognition domain (CRD) (Barondes et al., 1994a; Cooper, 2002; Elola et al., 2007; Hirabayashi & Kasai, 1993; Hughes, 2001; Klyosov et al., 2008; Leffler et al., 2004). They are evident in vertebrates, invertebrates and also protists, implying fundamental functions of these lectins (Hirabayashi & Kasai, 1993). Some galectins are distributed in a variety of different tissues, others are more specifically expressed (Cooper, 2002). Galectins are known to perform high diversity of functions inside the cells and in the extracellular space. They are regulators of cell cycle, inflammation, immune responses, cancer progression, cell adhesion, cell signalling events and so on. The different functions are performed either by protein-protein or by protein-glycan interactions (Almkvist & Karlsson, 2004; Danguy et al., 2002; Elola et al., 2007; Hernandez & Baum, 2002; Hughes, 2001; Ilarregui et al., 2005; Liu et al., 2002; Liu & Rabinovich, 2005; Rabinovich et al., 2002b; Rabinovich & Toscano, 2009; Vasta, 2009). Different excellent reviews focus on the wide-spread functions of galectins such as tumor progression, cell signalling or inflammation (Garner & Baum, 2008; Hernandez & Baum, 2002; Liu et al., 2002; Liu & Rabinovich, 2005; Nangia-Makker et al., 2008; Rabinovich et al., 2002a; Rabinovich & Toscano, 2009; van den Brule et al., 2004; Vasta, 2009). Review articles discussing functions of galectins in cell adhesion events and their role as matricellular proteins for the crosslinking of extracellular matrix components have also been published (Elola et al., 2007; Hughes, 2001). The function of galectins in the assembly of the extracellular matrix as well as in cell adhesion and cell signalling processes shows their potential as mediators for cell adhesion and proliferation on biomaterial surfaces. Galectins are interesting candidates for the functionalisation of biomaterial surfaces as they can promote the primary binding event of cells to foreign materials and influence specific signalling processes. In this article we want to analyse the potential use of galectins (explained by the examples of galectin-1, -3 and -8) in biomaterial research and application.

Glycan-Binding Profile and Cell Adhesion Activity of American Bullfrog (Rana catesbeiana) Oocyte Galectin-1

Abstract: The glycan-binding profile of a β-galactoside-binding 15 kDa lectin (Galectin-1) purified from the oocytes of the American bullfrog, Rana catesbeiana, was studied using 61 pyridyl-aminated oligosaccharides by frontal affinity chromatography. Human blood type-A-hexasaccharide (GalNAcα1-3(Fucα1-2)Galβ1-4GlcNAcβ1-4Galβ1-4Glc) was found to exhibit the strongest ligand binding to the galectin while Forssman antigen (GalNAcα1-3GalNAcβ1-3Galα1- 4Galβ1-4Glc) and type-A-tetrasaccharide (GalNAcα1-3(Fucα1-2)Galβ1-4GlcNAcβ1-4Glc) were also extensively recognized. The kinetics of affinity of galectin-1 to type-A oligosaccharide was analysed by surface plasmon resonance using neoglycoprotein with type-A oligosaccharides. R. catesbeiana oocyte galectin adhered to human rhabdomyosarcoma cells dose dependently and the activity was specifically cancelled by the neoglycoprotein. It was concluded that galectin-1 from R. catesbeiana oocytes possesses different and rare glycan-binding properties from typical members in galectin family.

Physicochemical properties and amino acid sequence of sheep brain galectin-1.

Abstract: A beta-galactoside-specific soluble 14-kD lectin from sheep brain was isolated, sequenced, and compared with similar galectins from other species. Percent identities of amino acid sequence and the carbohydrate recognition domain (CRD) revealed that the isolated galectin shares all the absolutely preserved and critical residues of the mammalian galectin-1 subfamily. The isolated sheep brain galectin (SBG) showed more than 90% amino acid sequence (92%) and carbohydrate recognition domain identity (96%) with human brain galectin-1. Conformational changes were found induced by interaction of the protein with its specific disaccharide and oxidizing agent (hydrogen peroxide). Upon oxidation a drastic change in the environment of aromatic residues and conformation of the galectin was observed with the loss of hemagglutination activity, while no significant change was observed upon addition of D-lactose (Gal(beta1-4)Glc) in the far-UV and near-UV spectra, suggesting no significant modification in the secondary as well as tertiary structures of sheep brain galectin. But the functional integrity of the CRD is found to be affected in the presence of oxidizing agent, indicating intramolecular disulfide bonds and requirement of complete polypeptide chain for functional integrity of the carbohydrate recognition domain.