Galectin-8, also known as Gal-8, is a member of the galectin family, which are beta-galactoside-binding animal lectins with conserved carbohydrate recognition domains (CRDs). Galectin-8 is a tandem-repeat type galectin, containing two CRDs connected by a linker peptide . This protein is expressed in various tissues and has been implicated in numerous biological processes, including cell adhesion, migration, and angiogenesis .
Galectin-8 was initially cloned from a rat liver cDNA library and is composed of 316 amino acids, with a molecular weight of approximately 35 kDa . The N- and C-terminal domains of Galectin-8 share 35% homology and contain sequence motifs conserved among most CRDs of galectins . The mouse recombinant version of Galectin-8 is expressed in Escherichia coli and has a purity of over 90%, making it suitable for various applications such as SDS-PAGE and mass spectrometry .
Galectin-8 plays a crucial role in various biological processes. It is involved in the regulation of vascular and lymphatic angiogenesis, which is the formation of new blood and lymphatic vessels . This protein has been shown to control capillary-tube formation, endothelial cell (EC) migration, and in vivo angiogenesis . Additionally, Galectin-8 interacts with specific ligands such as podoplanin in lymphatic vessels and CD166 (ALCAM) in vascular ECs .
Galectin-8 has significant implications in tumor biology. It is expressed in both normal and tumor-associated blood vessels, as well as in lymphatic endothelial cells . The protein’s role in tumor angiogenesis and metastasis is of particular interest, as modulating Galectin-8-glycan interactions could potentially block lymphatic-vascular connections vital for metastasis . Furthermore, Galectin-8 has been shown to restrict the proliferation of infecting pathogens by targeting them for autophagy, making it a potential therapeutic target for infectious diseases .