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Galectin-3 Functions as an Adhesion Molecule to Support Eosinophil Rolling and Adhesion under Conditions of Flow¹

Savita P. Rao^*,, Zhuangzhi Wang^*, Riaz I. Zuberi^*, Lyudmila Sikora^*, Nooshin S. Bahaie^*,, Bruce L. Zuraw, Fu-Tong Liu and P. Sriramarao^2,*,

^* Division of Vascular Biology, La Jolla Institute for Molecular Medicine, San Diego, CA 92121; Department of Medicine, University of California San Diego, La Jolla, CA 92093; Department of Dermatology, School of Medicine, University of California Davis, Sacramento, CA 95817; and Department of Veterinary and Biomedical Sciences, University of Minnesota, St. Paul, MN 55108

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) 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 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.

The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ This work was supported by National Institutes of Health Grants AI 35796, HL 079304, and AI 50498 (to P.S.).

² Address correspondence and reprint requests to Dr. P. Sriramarao, Department of Veterinary and Biomedical Sciences, University of Minnesota, 1365 Gortner Avenue, St. Paul, MN 55108. E-mail address: psrao{at}umn.edu

³ Abbreviations used in this paper: Gal-3, galectin-3; CRD, carbohydrate recognition domain; EC, endothelial cell; ECM, extracellular matrix; hpf, high power field; rh, recombinant human.

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