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Galectin-1 sensitizes carcinoma cells to anoikis via the fibronectin receptor ?5?1-integrin.

ABSTRACT: Anoikis resistance is a hallmark of transformed epithelial cells. Here, we show that treatment of anoikis-resistant carcinoma cell lines with the endogenous lectin galectin-1 (Gal-1) promoted apoptosis via interaction with the unligated fibronectin receptor ?(5)?(1)-integrin. Gal-1 efficiency correlated with expression of ?(5)?(1)-integrin, and transfection of the ?(5)-subunit into deficient cell lines conferred Gal-1 binding and anoikis stimulation. Furthermore, Gal-1 and the ?(5)- and ?(1)-integrin subunits co-precipitated in Gal-1-stimulated cells undergoing anoikis. Other members of the galectin family failed to be active. The functional interaction between Gal-1 and ?(5)?(1)-integrin was glycan dependent with ?2,6-sialylation representing a switch-off signal. Desialylation of cell surface glycans resulted in increased electrophoretic mobility of ?(5)?(1)-integrin and facilitated Gal-1 binding and anoikis stimulation. On the level of signaling, Gal-1-stimulated anoikis was prevented by filipin, which impaired the internalization of ?(5)?(1)-integrin via cholesterol-enriched microdomains, and by pretreatment with a caspase-8 inhibitor. We propose that Gal-1/?(5)?(1)-integrin interaction participates in the control of epithelial integrity and integrin sialylation may enable carcinoma cells to evade this Gal-1-dependent control mechanism.

SUBMITTER: Sanchez-Ruderisch H 

PROVIDER: S-EPMC3131929 | BioStudies | 2011-01-01T00:00:00Z

REPOSITORIES: biostudies

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