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* Chemoattractant Group of the James Graham Brown Cancer Center, Departments of Pathology, and of Microbiology and Immunology, University of Louisville, Louisville, KY 40202;
Department of Biological Sciences, Wayne State University, Detroit, MI 48202; and
Division of Hematology/Oncology, Department of Internal Medicine, Comprehensive Cancer Center, University of Michigan, Ann Arbor, MI 48109
A lectin function within CD11b mediates both cytotoxic priming of
Mac-1/complement receptor type 3 (CR3) by 
-glucan and the formation
of transmembrane signaling complexes with GPI-anchored glycoproteins
such as CD16b (Fc
RIIIb). A requirement for GPI-anchored urokinase
plasminogen activator receptor (uPAR; CD87) in neutrophil adhesion and
diapedesis has been demonstrated with uPAR-knockout mice. In this
study, neutrophil activation conditions generating high-affinity
(H-AFN) or low-affinity (L-AFN) 2 integrin adhesion were
explored. A role for the Mac-1/CR3 lectin domain and uPAR in mediating
H-AFN or L-AFN adhesion was suggested by the inhibition of
Mac-1/CR3-dependent adhesion to ICAM-1 or fibrinogen by -glucan or
anti-uPAR. The formation of uPAR complexes with Mac-1/CR3 activated
for L-AFN adhesion was demonstrated by fluorescence resonance energy
transfer. Conversely, Jurkat cell LFA-1 H-AFN-adhesion to ICAM-1 was
not associated with uPAR/LFA-1 complexes, any requirement for
GPI-anchored glycoproteins, or inhibition by -glucan. A single CD11b
lectin site for -glucan and uPAR was suggested because the binding
of either -glucan or uPAR to Mac-1/CR3 selectively masked two CD11b
epitopes adjacent to the transmembrane domain. Moreover, treatment with
phosphatidylinositol-specific phospholipase C that removed
GPI-anchored proteins increased CD11b-specific binding of
125I-labeled -glucan by 3-fold and this was reversed
with soluble recombinant uPAR. Conversely, neutrophil activation for
generation of Mac-1/CR3/uPAR complexes inhibited CD11b-dependent
binding of 125I-labeled -glucan by 75%. These data
indicate that the same lectin domain within CD11b regulates both the
cytotoxic and adhesion functions of Mac-1/CR3.
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