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CD66b Regulates Adhesion and Activation of Human Eosinophils¹

Juhan Yoon^*, Akihiko Terada and Hirohito Kita^2,*,

^* Department of Immunology, and Department of Medicine, Division of Allergic Diseases, Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN 55905

Eosinophils and their products are likely important in the pathophysiology of allergic diseases, such as bronchial asthma, and in host immunity to parasitic organisms. However, the mechanisms for proinflammatory mediator release by eosinophils are poorly understood. CD66b (CEACAM8, CGM6, NCA-95) is a single chain, GPI-anchored, highly glycosylated protein belonging to the carcinoembryonic Ag supergene family. CD66b is an activation marker for human granulocytes; however, its biological functions are largely unknown in eosinophils. We found that CD66b is highly expressed on the surface of human peripheral blood eosinophils isolated from healthy individuals. Engagement of CD66b, but not CD66a, by mAb or a natural ligand, galectin-3, activated a Src kinase family molecule, hemopoietic cell kinase (Hck), and induced cellular adhesion, superoxide production, and degranulation of eosinophils. CD66b molecules were localized in lipid rafts, and disruption of lipid rafts or removal of the GPI anchor inhibited the adhesion and activation of eosinophils. Importantly, CD66b was constitutively and physically associated with a β₂ integrin, CD11b, and cross-linking of CD66b induced a striking clustering of CD11b molecules. Thus, CD66b molecules are involved in regulating adhesion and activation of eosinophils, possibly through their localization in lipid rafts and interaction with other cell surface molecules, such as CD11b. Binding of exogenous or endogenous carbohydrate ligands(s) to CD66b may be important in the release of proinflammatory mediators by human eosinophils.

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 Grant AI34486 and the Mayo Foundation.

² Address correspondence and reprint requests to Dr. Kita Hirohito, Departments of Immunology and Medicine, Division of Allergic Diseases, Mayo Clinic College of Medicine, 200 First Street Southwest, Rochester, MN 55905. E-mail address: kita.hirohito{at}mayo.edu

³ Abbreviations used in this paper: LIR/ILT, leukocyte Ig-like receptor/Ig-like transcript; CEA, carcinoembryonic antigen; MβCD, methyl β-cyclodextrin; MBP, myelin basic protein; PI-PLC, phosphatidylinositol-specific phospholipase C; EDN, eosinophil-derived neurotoxin.

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