**2.3.4 Galectin-8: Several isoforms of a tandem-repeat galectin**

The specific properties of galectin-8 are also implied in its structure and the different isoforms arising from it. At least 6 different isoforms are described so far of which some only consist of the N-terminal CRD with an extension and others consist of both CRDs linked by different hinge domains (Bidon et al., 2001; Delgado et al., 2011; Zick et al., 2004). The two galectin-8 CRDs show approximately 35% sequence similarity but reveal different fine specificity for glycan structures. Therefore galectin-8 can act as "hetero-bifunctional crosslinking agent" (Zick et al., 2004). The length and structure of the linker domain has direct influence on the biological function (Levy et al., 2006). Moreover the linker domain regulates susceptibility to protease cleavage. It was for example shown that a long linker can be cleaved by thrombin while shorter linker variants are not substrate for this protease (Nishi et al., 2006).
