galectin-16 Activators

galectin-16 can influence its activity through various molecular interactions, primarily involving the binding to its carbohydrate recognition domain (CRD). β-Lactose, a disaccharide consisting of glucose and galactose, can engage galectin-16 through its CRD, leading to the activation of the protein's lectin functions. Similarly, Thiodigalactoside, a synthetic disaccharide, is known to interact with the CRD of galectin-16, triggering its activation. This activation mechanism is also seen with N-Acetyllactosamine, a compound that can facilitate the lectin activity of galectin-16 by directly binding to it. Methyl β-D-galactopyranoside is another activator that specifically interacts with galectin-16, reinforcing its lectin activity. The CRD of galectin-16 is further activated by Lactulose, a synthetic sugar, which has an affinity for the protein, and Phenyl β-D-galactopyranoside, which targets galectin-16 to instigate activation.

In addition to these activators, specific antigenic determinants such as Fucosylated Thomsen-Friedenreich antigen can engage galectin-16 through its CRD, leading to activation. Even galectin inhibitors like TD139 can, under certain conditions, bind to galectin-16 and activate it. PNP-GalNAc, a synthetic substrate for glycosyltransferases, is recognized by galectin-16 and mediates its activation, emphasizing the protein's role in glycan recognition and binding. The glycan structure of Lacto-N-fucopentaose III also provides a binding interface for galectin-16, thereby activating it in cell adhesion processes. Moreover, natural glycan structures from ABH Blood Group Substances, which contain fucose and GalNAc residues, can activate galectin-16 through their interaction with the protein's CRD. Lastly, the disaccharide 3'-sulfo-Lewis A, a sulfated carbohydrate, has a high affinity for galectin-16 and results in the protein's activation, which underscores the significance of post-translational modifications like sulfation in modulating galectin-16 activity.