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Blood, 15 April 2001, Vol. 97, No. 8, pp. 2478-2486
PHAGOCYTES
Mac-1 (CD11b/CD18) is essential for Fc receptor-mediated
neutrophil cytotoxicity and immunologic synapse formation
Annemiek B. van Spriel,
Jeanette H. W. Leusen,
Marjolein van Egmond,
Henry B. P. M. Dijkman,
Karel J. M. Assmann,
Tanya N. Mayadas, and
Jan G. J. van de Winkel
From the Immunotherapy Laboratory and Medarex Europe,
University Medical Center Utrecht, Utrecht, The Netherlands; Department
of Pathology, University Hospital, Nijmegen, The Netherlands; and
Department of Pathology, Harvard Medical School, Boston, MA.
Receptors for human immunoglobulin (Ig)G and IgA initiate potent
cytolysis of antibody (Ab)-coated targets by polymorphonuclear leukocytes (PMNs). Mac-1 (complement receptor type 3, CD11b/CD18) has
previously been implicated in receptor cooperation with Fc receptors
(FcRs). The role of Mac-1 in FcR-mediated lysis of tumor cells was
characterized by studying normal human PMNs, Mac-1-deficient mouse
PMNs, and mouse PMNs transgenic for human FcR. All PMNs efficiently
phagocytosed Ab-coated particles. However, antibody-dependent cellular cytotoxicity (ADCC) was abrogated in
Mac-1 / PMNs and in human PMNs blocked with anti-Mac-1
monoclonal Ab (mAb). Mac-1/ PMNs were unable to spread
on Ab-opsonized target cells and other Ab-coated surfaces.
Confocal laser scanning and electron microscopy revealed a striking
difference in immunologic synapse formation between
Mac-1/ and wild-type PMNs. Also, respiratory burst
activity could be measured outside membrane-enclosed compartments by
using Mac-1/ PMNs bound to Ab-coated tumor cells, in
contrast to wild-type PMNs. In summary, these data document an absolute
requirement of Mac-1 for FcR-mediated PMN cytotoxicity toward tumor
targets. Mac-1/ PMNs exhibit defective spreading on
Ab-coated targets, impaired formation of immunologic synapses, and
absent tumor cytolysis.
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