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.

Studies of Arginine–Arene Interactions through Synthesis and Evaluation of a Series of Galectin-Binding Aromatic Lactose Esters

Abstract: Aromatic lactose 2-O-esters were synthesized and used to probe arene-arginine interactions with the galectin family of proteins. They were found to be low mu m inhibitors of galectin-1, -3, and -9N-terminal domain and moderate inhibitors of galectin-7, but not inhibitors of galectin-8N-terminal, which locks an arginine residue close to the critical, esterified lactose 2-O-position. Molecular modeling of galectins in complex with aromatic lactose 2-O-esters, as well as binding studies with a galectin-3 R186S mutant, confirmed that the inhibitory efficiency of the lactose 2-O-esters was due to the formation of strong interactions between the aromatic ester moieties and the arginine guanidinium groups of galectin-1 and -3. An important common feature shared by galectin-1 and -3 was that the arginines formed in-plane ion pairs with two side-chain carboxylates, which resulted in extended planar pi-electron surfaces that did not require solvation by water; these surfaces were ideal for stocking with aromatic moieties of the ligands. The results provide a basis for the design of lectin inhibitors and drugs that exploit interactions with arginine side-chains via aromatic moieties, which are involved in intramolecular protein salt bridges. (Less)

Roles of galectin-3 in immune responses.

Abstract: Galectins are a family of animal lectins with conserved carbohydrate-recognition domains for beta-galactoside. Galectin-3 is the only family member that is composed of a glycine/prolinerich N-terminal repeated sequence and a C-terminal carbohydrate-binding domain.Multiple functions of galectin-3 have been reported, depending on its location. Extracellular galectin-3 can bind to cell surface through glycosylated proteins and thereby trigger or modulate cellular responses such as mediator release or apoptosis. Intracellular galectin-3 has been reported to inhibit apoptosis, regulate the cell cycle, and participate in the nuclear splicing of pre-mRNA. Recent studies have revealed that galectin-3 is expressed in a variety of cell types in the immune system, constitutively or in response to microbial invasion. These studies implicate galectin-3 in both innate and adaptive immune responses, where it participates in the activation or differentiation of immune cells. This review summarizes the roles of galectin-3 in the immune system and discusses the possible underlying mechanisms.

Insect galectins: roles in immunity and development.

Abstract: As evidenced by the reviews in this special issue of Glycoconjugate Journal, much research is focused on determining functions for mammalian galectins. However, the identification of precise functions for mammalian galectins may be complicated by redundancy in tissue expression and in target cell recognition of the many mammalian galectins. Therefore, lower organisms may be useful in deciphering precise functions for galectins. Unfortunately, some genetically manipulable model systems such as Caenorhabditis elegans may have more galectins than mammals. Recently, galectins were identified in two well-studied insect systems, Drosophila melanogaster and Anopheles gambiae. In addition to the powerful genetic manipulation available in these insect models, there is a sophisticated understanding of many biological processes in these organisms that can be directly compared and applied to mammalian systems. Understanding the roles of galectins in insects may provide insight into precise functions of galectins in mammals.