Your browser doesn't support javascript.
loading
: 20 | 50 | 100
1 - 1 de 1
1.
Biol Res ; 57(1): 14, 2024 Apr 04.
Article En | MEDLINE | ID: mdl-38570874

Galectins are soluble glycan-binding proteins that interact with a wide range of glycoproteins and glycolipids and modulate a broad spectrum of physiological and pathological processes. The expression and subcellular localization of different galectins vary among tissues and cell types and change during processes of tissue repair, fibrosis and cancer where epithelial cells loss differentiation while acquiring migratory mesenchymal phenotypes. The epithelial-mesenchymal transition (EMT) that occurs in the context of these processes can include modifications of glycosylation patterns of glycolipids and glycoproteins affecting their interactions with galectins. Moreover, overexpression of certain galectins has been involved in the development and different outcomes of EMT. This review focuses on the roles and mechanisms of Galectin-1 (Gal-1), Gal-3, Gal-4, Gal-7 and Gal-8, which have been involved in physiologic and pathogenic EMT contexts.


Galectins , Neoplasms , Humans , Galectins/genetics , Galectins/metabolism , Fibrosis , Glycoproteins , Epithelial-Mesenchymal Transition , Glycolipids
...