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From the Center for Immmunology and Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110

The I domain of lymphocyte function–associated antigen (LFA)-1 contains an intercellular adhesion molecule (ICAM)-1 and ICAM-3 binding site, but the relationship of this site to regulated adhesion is unknown. To study the adhesive properties of the LFA-1 I domain, we stably expressed a GPI-anchored form of this I domain (I-GPI) on the surface of baby hamster kidney cells. I-GPI cells bound soluble ICAM-1 (sICAM-1) with a low avidity and affinity. Flow cell experiments demonstrated a specific rolling interaction of I-GPI cells on bilayers containing purified full length ICAM-1 or ICAM-3. The LFA-1 activating antibody MEM-83, or its Fab fragment, decreased the rolling velocity of I-GPI cells on ICAM-1–containing membranes. In contrast, the interaction of I-GPI cells with ICAM-3 was blocked by MEM-83. Rolling of I-GPI cells was dependent on the presence of Mg²⁺. Mn²⁺ only partially substituted for Mg²⁺, giving rise to a small fraction of rolling cells and increased rolling velocity. This suggests that the I domain acts as a transient, Mg²⁺-dependent binding module that cooperates with another Mn²⁺-stimulated site in LFA-1 to give rise to the stable interaction of intact LFA-1 with ICAM-1.

¹ Abbreviations used in this paper: BHK, baby hamster kidney; I-GPI, GPI anchored form of the LFA-1 I domain; ICAM, intercellular adhesion molecule; LFA, lymphocyte function–associated antigen; PIPLC, phosphatidylinositol-specific phospholipase C.

Portions of this work were previously presented at the meeting of the American Association for Immunologists (AAI) on 3-6 June 1996 in New Orleans, LA.

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