Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Type

Journal article

Journal

J Exp Med

Publication Date

29/08/1997

Volume

186

Pages

719 - 730

Keywords

Animals, Antibodies, Monoclonal, Antigens, CD, Antigens, Differentiation, Binding Sites, Binding, Competitive, Blotting, Western, Cell Adhesion, Cell Adhesion Molecules, Cell Line, Cell Movement, Cloning, Molecular, Cricetinae, Glycosylphosphatidylinositols, Intercellular Adhesion Molecule-1, Lymphocyte Function-Associated Antigen-1, Magnesium, Microscopy, Video, Phosphatidylinositol Diacylglycerol-Lyase, T-Lymphocytes, Tumor Cells, Cultured, Type C Phospholipases