Abstract
// Zhongyu Zhang 1 , Yuan Guan 1 , Xiyao Yu 1 , Hairong Cheng 1 , Yifa Zhou 1 and Guihua Tai 1 1 School of Life Sciences, Northeast Normal University, Changchun, PR China Correspondence to: Guihua Tai, email: taigh477@nenu.edu.cn Keywords : galectin-3; CRD; migration; HMEC-1; β1 integrin Received: August 18, 2017 Accepted: January 02, 2018 Epub: January 11, 2018 Abstract Galectin-3 (Gal-3) is composed of a long N-terminal tail (NT) connected to its conserved carbohydrate recognition domain (CRD). The NT is degraded by matrix metalloproteinases and prostate-specific antigen. Here, we demonstrate that NT-truncated Gal-3 variants with deletion of the first 12 or 68 residues, or the entire 110-residues NT, triggers migration of human microvascular endothelial cells (HMEC- 1). Using mass spectrometry and pull-down analysis, we show that the Gal-3 CRD binds to and activates cell surface β1 integrin promoting phosphorylation of FAK. Antibody blocking assays suggested that α2, α4, and α6 integrins are involved, with α2 and β1 forming a heterodimer. shRNA knockdown or antibody-mediated inhibition of β1 integrin function inhibited CRD-induced cell migration and attenuated FAK phosphorylation. FAK-specific inhibitors also inhibited Gal-3 CRD-induced cell migration. Interestingly, full-length Gal-3 and its CRD promoted similar effects. These findings highlight the need to reconsider Gal-3 NT cleavage in formulating strategies to address tumor angiogenesis.
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