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CUTTING EDGE |
*
Pulmonary and Critical Care Medicine Division, Department of Internal Medicine,
Department of Pediatrics and Communicable Diseases, University of Michigan, Ann Arbor MI 48109; and
Department of Biological Sciences, Wayne State University, Detroit, MI 48202
Leukocyte urokinase plasminogen activator receptors
(uPARs) cluster at adhesion interfaces and at migratory fronts where
they participate in adhesion, chemotaxis, and proteolysis. uPAR
aggregation triggers activation signaling even though this
glycolipid-anchored protein must associate with membrane-spanning
proteins to access the cell interior. This study demonstrates a novel
partnership between uPAR and L-selectin in human polymorphonuclear
neutrophils. Fluorescence resonance energy transfer demonstrated a
direct physical association between uPAR and L-selectin. To examine the
role of L-selectin in uPAR-mediated signaling, uPAR was cross-linked
and intracellular Ca2+ concentrations were measured
by spectrofluorometry. A mAb reactive against the carbohydrate
binding domain (CBD) of L-selectin substantially inhibited
uPAR-mediated Ca2+ mobilization, whereas mAbs against the
2 integrin complement receptor 3 (CR3), another
uPAR-binding adhesion protein, had no effect. Similarly, fucoidan, a
sulfated polysaccharide that binds to L-selectin CBD, inhibited the
Ca2+ signal. We conclude that uPAR associates with the CBD
region of L-selectin to form a functional signaling
complex.
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