The universe of galectin-binding partners and their functions in health and disease

Bioactive Properties of Venoms Isolated from Whiptail Stingrays and the Search for Molecular Mechanisms and Targets

“…The proteomic identification of a galectin-like protein as the second-most abundant protein in N. kuhlii venom, and also reportedly present in teleost venom [ 11 , 16 ], is especially intriguing given the well-established multifunctional characteristics of vertebrate galectins [ 31 , 32 ]. Several galectins have also been identified in the venom of other marine stingrays, but currently are not classified as toxins or members of a venom toxin family [ 19 ].…”

“…In contrast, galectins are calcium-independent and are currently not classified as toxins, yet are known to mediate many of the biological effects observed in our SRV experiments and reported in the literature. Given their reported abundance in marine SRV, galectins appear poised to be an important SRV component contributing to the biological responses associated with envenomation [ 31 , 32 ].…”

“…Several of the H. sabinus galectin-like proteins encode protomer-type galectins (single CBD) with dimerization sequences at both N- and C-termini for homo-dimer formation. Both the H. sabinus galectin-8-like and galectin-9-like proteins are tandem repeat-type galectins, with each encoding two distinct CBDs separated by an amino acid linker sequence [ 31 , 32 ]. The venom-associated galectins may represent a distinct subfamily of galectin-like proteins.…”

“…Cell surface glycan differences have been attributed to changes in cell adhesion and growth that represent hallmark features in cancer biology. Fourteen known galectin genes in humans participate in a broad range of galectin-specific regulatory processes that are altered in several diseases [ 32 ]. Their utility in cancer diagnosis and prognosis has also gained considerable interest [ 37 ].…”

Galectins in epithelial-mesenchymal transition: roles and mechanisms contributing to tissue repair, fibrosis and cancer metastasis

“…As the structures conformed by glycans entail enormous versatility and are considered to constitute a “sugar code” susceptible to changes under physiological or pathological conditions [ 1 , 2 ], galectin functions also display variations accordingly with the glycan modifications [ 4 , 7 – 9 ]. Physiological processes such as cell proliferation, differentiation, phenotypic plasticity, apoptosis, angiogenesis and immune responses, as well as pathogenic conditions such as cancer, tissue fibrosis, chronic inflammation and autoimmune disorders, usually engage distinct members of the galectin family with complementary or redundant roles, acting across various tissues and cell types, such as endothelium, epithelium and immune cells [ 3 – 6 , 10 , 11 ].…”