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Effect of Integrin ß₂ Subunit Truncations on LFA-1 (CD11a/CD18) and Mac-1 (CD11b/CD18) Assembly, Surface Expression, and Function¹

Medical Research Council Immunochemistry Unit, Department of Biochemistry, University of Oxford, Oxford, United Kingdom

LFA-1 (CD11a/CD18) and Mac-1 (CD11b/CD18) are members of the ß₂ integrins involved in leukocyte function during immune and inflammatory responses. We aimed to determine a minimized ß₂ subunit that forms functional LFA-1 and Mac-1. Using a series of truncated ß₂ variants, we showed that the subregion Q23-D300 of the ß₂ subunit is sufficient to combine with the _L and _M subunits intracellularly. However, only the ß₂ variants terminating after Q444 promote cell surface expression of LFA-1 and Mac-1. Thus, the major cysteine-rich region and the three highly conserved cysteine residues at positions 445, 447, and 449 of the ß₂ subunit are not required for LFA-1 and Mac-1 surface expression. The surface-expressed LFA-1 variants are constitutively active with respect to ICAM-1 adhesion and these variants express the activation reporter epitope of the mAb 24. In contrast, surface-expressed Mac-1, both the wild type and variants, require 0.5 mM MnCl₂ for adhesion to denatured BSA. These results suggest that the role of the ß₂ subunit in LFA-1- and Mac-1-mediated adhesion may be different.

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