Claudia Elena Sotomayor

TL;DR: Results presented here provide the first evidence for a role of Gal‐1 in acute inflammation and suggest that the anti‐inflammatory effect involves the inhibition of both soluble and cellular mediators of the inflammatory response.

TL;DR: Rat macrophage galectin was purified from activated macrophages by a single-step affinity chromatography on a lactosyl-Sepharose matrix and showed a definitive acidic pattern, and internal amino acid sequencing of selected peptides obtained by proteolytic cleavage revealed that this carbohydrate-binding protein shares all the absolutely preserved and critical residues found in other members of the mammalian galECTin-1 subfamily.

TL;DR: The first experimental evidence regarding AP-1 and Bcl-2 as targets of the signal transduction pathway triggered by Gal-1 are presented and set the basis for a more in depth understanding of the molecular mechanisms of T-cell death regulation.

TL;DR: This study provides an alternative cellular mechanism based on the modulation of L-arginine metabolism to understand the molecular basis of the anti-inflammatory properties displayed by this carbohydrate-binding protein.

TL;DR: Western blot assays suggest that this protein is localized mainly in the cytoplasmic compartment but also associated with the cell surface, and both stimuli involving protein kinase C activation pathway have been able not only to up‐regulate the total expression of this protein but also to modulate its subcellular localization.