PT  - JOURNAL ARTICLE
AU  - Rao, Savita P.
AU  - Wang, Zhuangzhi
AU  - Zuberi, Riaz I.
AU  - Sikora, Lyudmila
AU  - Bahaie, Nooshin S.
AU  - Zuraw, Bruce L.
AU  - Liu, Fu-Tong
AU  - Sriramarao, P.
TI  - Galectin-3 Functions as an Adhesion Molecule to Support Eosinophil Rolling and Adhesion under Conditions of Flow
AID  - 10.4049/jimmunol.179.11.7800
DP  - 2007 Dec 01
TA  - The Journal of Immunology
PG  - 7800--7807
VI  - 179
IP  - 11
4099  - http://www.jimmunol.org/content/179/11/7800.short
4100  - http://www.jimmunol.org/content/179/11/7800.full
SO  - J. Immunol.2007 Dec 01; 179
AB  - 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) α4 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 α4 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.