Expression, localization and function of galectin-8, a tandemrepeat lectin, in human tumors

ELOLA MT; FERRAGUT F; CÁRDENAS DELGADO VM; NUGNES LG; GENTILINI L; LADERACH D; TRONCOSO MF; COMPAGNO D; WOLFENSTEIN DE TODEL C; RABINOVICH GA

HISTOLOGY AND HISTOPATHOLOGY

F HERNANDEZ

Lugar: Madrid; Año: 2014 vol. 29 p. 1093 - 1105

0213-3911

Galectin-8 (Gal-8) is a ?tandem-repeat?-type galectin, which possesses twocarbohydrate recognition domains connected by a linker peptide. Gal-8 complexity isrelated to the alternative splicing of its mRNA precursor, which is known to generateisoforms. Regarding its carbohydrate-binding specificity, Gal-8 has a unique featureamong galectins, since its C-terminal domain has higher affinity for N-glycan-typebranched oligosaccharides, while its N-terminal domain shows strong affinity for beta2-3-sialylated or 3´-sulfated beta-galactosides. We integrate here the available information onGal-8 expression in different tumor types and attempt to elucidate associations of itsexpression and localization with tumor progression with the overarching goal ofanalyzing its potential applications in diagnosis and prognosis. Differential diagnosis isstill a prime concern in tumor pathology, and Gal-8 could be of great value in sometypes of primary or secondary tumors (i.e. papillary thyroid carcinoma, advanced coloncarcinoma from patients with distant metastases, or metastases from primary lungcarcinoma). The prognostic value of Gal-8 has been described for laryngeal carcinomaas well as advanced colon carcinoma. Further studies are needed to explain therelevance of Gal-8 and its isoforms in tumor pathology and their different intra- orextracellular roles (cytoplasmic, nuclear or extracellular) in tumor biology.