AI Article Synopsis

  • Galectin-3 (Gal-3) is key in the recruitment of eosinophils during allergic inflammation, particularly in the lungs.
  • Eosinophils from allergic individuals show higher levels of Gal-3 and increased ability to roll and adhere to both VCAM-1 and Gal-3 in flowing conditions.
  • Research revealed that Gal-3 facilitates eosinophil interactions with endothelial cells through specific mechanisms involving alpha(4) integrin and its own carbohydrate recognition domain, highlighting its role as an adhesion molecule.

Article Abstract

Allergic inflammation involves the mobilization and trafficking of eosinophils to sites of inflammation. Galectin-3 (Gal-3) has been shown to play a critical role in eosinophil recruitment and airway allergic inflammation in vivo. The role played by Gal-3 in human eosinophil trafficking was investigated. Eosinophils from allergic donors expressed elevated levels of Gal-3 and demonstrated significantly increased rolling and firm adhesion on immobilized VCAM-1 and, more surprisingly, on Gal-3 under conditions of flow. Inhibition studies with specific mAbs as well as lactose demonstrated that: 1) eosinophil-expressed Gal-3 mediates rolling and adhesion on VCAM-1; 2) alpha(4) integrin mediates eosinophil rolling on immobilized Gal-3; and 3) eosinophil-expressed Gal-3 interacts with immobilized Gal-3 through the carbohydrate recognition domain of Gal-3 during eosinophil trafficking. These findings were further confirmed using inflamed endothelial cells. Interestingly, Gal-3 was found to bind to alpha(4) integrin by ELISA, and the two molecules exhibited colocalized expression on the cell surface of eosinophils from allergic donors. These findings suggest that Gal-3 functions as a cell surface adhesion molecule to support eosinophil rolling and adhesion under conditions of flow.

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http://dx.doi.org/10.4049/jimmunol.179.11.7800DOI Listing

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