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,
*
Institute of Cell Signaling and School of Biomedical Sciences, University of Nottingham Medical School, Queen’s Medical Centre, Nottingham, United Kingdom;
Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, United Kingdom; and
SmithKline Beecham Pharmaceuticals, Harlow, Essex, United Kingdom
Cells undergoing apoptosis are cleared rapidly by phagocytes, thus
preventing tissue damage caused by loss of plasma membrane integrity.
In this study, we show that the surface of leukocytes is altered during
apoptosis such that the first Ig-like domain of ICAM-3 (CD50) can
participate in the recognition and phagocytosis of the apoptotic cells
by macrophages. Macrophage recognition of apoptotic cell-associated
ICAM-3 was demonstrated both on leukocytes and, following transfection
of exogenous ICAM-3, on nonleukocytes. The change in ICAM-3 was a
consistent consequence of apoptosis triggered by various stimuli,
suggesting that it occurs as part of a final common pathway of
apoptosis. Alteration of ICAM-3 on apoptotic cells permitting
recognition by macrophages resulted in a switch in ICAM-3-binding
preference from the prototypic ICAM-3 counterreceptor, LFA-1, to an
alternative macrophage receptor. Using mAbs to block
macrophage/apoptotic cell interactions, we were unable to obtain
evidence that either the alternative ICAM-3 counterreceptor
dß2 or the apoptotic cell receptor
vß3 was involved in the recognition of
ICAM-3. By contrast, mAb blockade of macrophage CD14 inhibited
ICAM-3-dependent recognition of apoptotic cells. These results show
that ICAM-3 can function as a phagocytic marker of apoptotic leukocytes
on which it acquires altered macrophage receptor-binding
activity.
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