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.
Papers published on a yearly basis
Papers
More filters
••
4 citations
•
21 May 2007TL;DR: In this paper, a complex consisting of galectin-3 and chondroitin oligosaccharide and methods for seperating and detecting the chond-roitin in a sample using the immobilized complex are presented.
Abstract: A complex consisting of galectin-3 and chondroitin oligosaccharide and methods for seperating and detecting the chondroitin oligosaccharide in a sample using the immobilized complex.
4 citations
••
TL;DR: This review aims to update current information on lectins from marine organisms, their characterization, extraction, and biofunctionalities.
Abstract: Lectins are a unique group of nonimmune carbohydrate-binding proteins or glycoproteins that exhibit specific and reversible carbohydrate-binding activity in a non-catalytic manner. Lectins have diverse sources and are classified according to their origins, such as plant lectins, animal lectins, and fish lectins. Marine organisms including fish, crustaceans, and mollusks produce a myriad of lectins, including rhamnose binding lectins (RBL), fucose-binding lectins (FTL), mannose-binding lectin, galectins, galactose binding lectins, and C-type lectins. The widely used method of extracting lectins from marine samples is a simple two-step process employing a polar salt solution and purification by column chromatography. Lectins exert several immunomodulatory functions, including pathogen recognition, inflammatory reactions, participating in various hemocyte functions (e.g., agglutination), phagocytic reactions, among others. Lectins can also control cell proliferation, protein folding, RNA splicing, and trafficking of molecules. Due to their reported biological and pharmaceutical activities, lectins have attracted the attention of scientists and industries (i.e., food, biomedical, and pharmaceutical industries). Therefore, this review aims to update current information on lectins from marine organisms, their characterization, extraction, and biofunctionalities.
4 citations
••
4 citations
••
01 Jan 2020TL;DR: This update of the I blood group system continues to show the Ii antigens to be increasingly recognized as important posttranslational modifiers regulating cell adhesion, signaling, differentiation, and cancer.
Abstract: CONCLUSIONS This update of the I blood group system (Cooling L. Polylactosamines, there's more than meets the "Ii": a review of the I system. Immunohematology 2010;26:133-55) continues to show the Ii antigens to be increasingly recognized as important posttranslational modifiers regulating cell adhesion, signaling, differentiation, and cancer. Ii antigens can modulate the immune response through the galectin lattice, as well as influence specific protein-protein interactions. Changes in GCNT2 and I expression accompany stem cell differentiation and are associated with tumor progression in melanoma and breast and colon cancer. Regulation of GCNT2 expression varies between cell types and differentiation. In red blood cell differentiation, GCNT2 is regulated by methylation, microRNAs, and mitogen-activated protein kinase signaling pathways. Methylation and microRNAs also play a prominent role in altering GCNT2 expression in several epithelial cancers. In congenital cataracts, GCNT2 mutations may account for 4-6 percent of all cases. GCNT2 may be particularly susceptible to gene deletion and rearrangements due to the density of Alu-repeat elements.
4 citations