Human LGALS3 ELISA Matched Antibody Pair

Preoperative diagnosis of thyroid nodules reduces unnecessary surgery. Circulating tumor cells (CTCs) may contain information of primary tumor(s). We asked whether the peripheral blood expression of genes specific for circulating tumor cells (CTCs) differentiates benign thyroid nodules from malignant nodules. Peripheral blood mononuclear cells from thyroid nodule patients (n = 20) were isolated preoperatively and the expression of seven CTC-associated genes was measured in patients with thyroid nodule(s) (n = 20). Among the tested genes, the expression of SLC5A5 and LGALS3 were validated in a larger number of patients (n = 64) and our results show that SLC5A5 expression differentiated follicular adenomas from follicular carcinomas (area under the curve (AUC) = 0.831). The expression of SLC5A5 in CTCs may preoperatively distinguish thyroid follicular adenomas from follicular carcinomas.

Recent studies have shown that galectin-3 (Gal-3; also known as LGALS3), a beta-galactoside-binding lectin, promotes cell migration during re-epithelialization of corneal wounds. The goal of this study was to characterize the molecular mechanism by which Gal-3 stimulates cell migration. We demonstrate here that exogenous Gal-3, but not Gal-1 or Gal-8, promotes cell scattering and formation of lamellipodia in human corneal epithelial cells in a beta-lactose-inhibitable manner alpha 3 beta 1 integrin was identified as the major Gal-3-binding protein in corneal epithelial cells by affinity chromatography of cell lysates on a Gal-3-Sepharose column. Preincubation of cells with anti-alpha 3 integrin function-blocking antibody significantly inhibited the induction of lamellipodia by Gal-3. Furthermore, exogenous Gal-3 activated both focal adhesion kinase, a key regulator of integrin-dependent intracellular signaling, and Rac1 GTPase, a member of the family of Rho GTPases, well known for its role in the reorganization of the actin cytoskeleton and formation of lamellipodial extensions. Experiments involving knockdown of beta-1,6-N-acetylglucosaminytransferase V, an enzyme that synthesizes high-affinity glycan ligands for Gal-3, revealed that carbohydrate-mediated interaction between Gal-3 and complex N-glycans on alpha 3 beta 1 integrin plays a key role in Gal-3-induced lamellipodia formation. We propose that Gal-3 promotes epithelial cell migration by cross-linking MGAT5-modified complex N-glycans on alpha 3 beta 1 integrin and subsequently activating alpha 3 beta 1-integrin-Rac1 signaling to promote lamellipodia formation.