So far there is only one chimera Galectin in vertebrates called Galectin-3, it has several alternative names such as Mac-2 antigen, CBP35, and CBP30. Gal-3 predominantly exists as a monomer in solution but can self-associate via its N-terminal or C-terminal domains dependent on the ligand and the concentration of monomeric Gal-3.
Fig.1 Chimera Galectins and mode of self-association. (Ayona, et al., 2020)
The single gene LGALS3 codes the human Galectin-3 on chromosome 14. In its natural state, Galectin-3 is a two-domain protein with a proline-, glycine-, and tyrosine-rich repeat-rich N-terminal oligomerization domain and a carbohydrate-binding domain at the C-terminus. According to research, a bound Gal-3 molecule increases the binding of more Galectin-3 molecules. Gal-3 can interact with other proteins, such as Alix or Bcl-2, in addition to glycans, due to its N-terminal domain.
Intramolecular interactions between the carbohydrate recognition domain (CRD) and the N-terminal render the Galectin-3 molecule relatively inert in the closed conformer state. Two types of intermolecular interactions, N-terminal interactions, and CRD-CRD interactions, they are usually observed during multimerization and this results in an increased biological activity of Galectin-3.
Fig.2 Self-interactions in Galectin-3 bioactivation. (Suthahar, et al., 2018)
Galectin-3 has a variety of actions. Its internal forms often defend cells against apoptosis through processes unrelated to carbohydrates. For binding extracellularly with lactosamine-containing cell surface glycoconjugates via the CRD, the lectin mediates cell-cell and cell-matrix interactions and promotes apoptosis.
Involved in several inflammatory processes, neutrophil adherence and opsonization, monocyte chemoattraction, and mast cell activation, Galectin-3 is released during the differentiation of monocytes into macrophages. Gal-3 is considered to induce pathological remodeling by increasing fibroblast proliferation and collagen deposition when it is expressed more often in activated macrophages.
In recent years, research has found that Galectin-3 binding and cross-linking glycans on cell surface receptors, modulate signal transduction by novel carbohydrate-based recognition systems. In the cornea, Galectin-3 has been detected in the conjunctiva, trabecular meshwork, retina, and the lens where it plays a role in cell differentiation and adhesion of fiber cells through interaction with MP20, a member of the tetraspanin superfamily of integral membrane proteins.
CD BioGlyco has advanced platforms and provides customized services according to our clients’ special needs in the research of Galectin. if you are interested in our services, please contact us for more detailed information.
CD BioGlyco is a world-class biotechnology company with offices in many countries. Our products and services provide a viable option to what is otherwise available.