Galectins are important therapeutic targets because they are the mediators of fundamental biologic mechanisms in pathological processes. There are 15 galectin protein subtypes with the common characteristic of a carbohydrate recognition domain that binds to β-galactose-containing carbohydrates and glycoproteins. A key factor that differentiates galectin protein subtypes is their oligomerization domains that allow the galectin protein to bind with another protein of the same family, creating a dimer, (See Figure 1). Secreted galectins have been shown to bind with high affinity to galactose-containing glycoproteins on the cell surface and in the extracellular matrix. Their ability to dimerize creates the opportunity for galectins to link glycoproteins and form a lattice structure on the cellular surface and to promote cell-cell and cell-matrix interactions. The associations between glycoproteins created by galectins can trigger intracellular signaling and potentiate or modulate certain biologic and pathologic effects.
While galectins are normally expressed in small amounts in many different cell types, secreted galectins are markedly increased and have important roles in a wide variety of pathological processes involved in immune regulation, inflammation, fibrogenesis and tumor cell biology. Our drug compounds are designed to bind to and inhibit the function of secreted galectins. With these characteristics, our drugs have the potential to modulate and treat diseases where increased galectins promote or potentiate the pathological situation.
In recent years there has been an exponential growth in the number of scientific and medical publications on normal and pathological functions of galectins. Galectin Therapeutics designs drug compounds to bind to and inhibit the function of secreted galectins.
Galectin Therapeutics’ contributions and leadership in this area are highlighted by the textbook, Galectins, edited by Galectin Therapeutics’ Chief Scientific Officer, Dr. Anatole Klyosov.