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Vol. 56, Issue 5, 926-932, November 1999
2 Integrins
Department of Pharmacology, The University of Illinois College of
Medicine, Chicago, Illinois
We studied the basis of inhibition of polymorphonuclear leukocyte (PMN)
adhesion induced by neutrophil inhibitory factor (NIF), a 41-kDa
CD11/CD18 
2 integrin-binding protein isolated from the canine hookworm (Ancylostoma caninum). NIF blocked PMN
adhesion in a concentration-dependent manner with complete blockade
occurring at ~10 nM NIF. Because CD11a and CD11b 2
integrins are functionally active on stimulated PMNs, and yet NIF is
postulated to inhibit only CD11b integrin by binding to its I domain,
we evaluated the contributions of CD11a and CD11b 2
integrins in the mechanism of inhibition of PMN adhesion to endothelial
cells. We observed an additive inhibitory effect (>90% inhibition) of
PMN adhesion to endothelial cells when NIF was used in combination with
anti-CD11b monoclonal antibodies, which alone at saturating
concentrations reduced PMN adhesion by only 50%. NIF also prevented
aggregation of phorbol ester-stimulated JY lymphoblastoid cells
that expressed only the functionally active CD11a, suggesting that NIF
also can inhibit CD11a-dependent response. We transduced the NIF cDNA
into human dermal microvessel endothelial cells in which NIF synthesis and release prevented PMN adhesion to the transduced human dermal microvessel endothelial cells. These data indicated that the
potent antiadhesive effect of NIF may be the result of inhibition of CD11a and CD11b 2 integrins on PMNs. Moreover, the
strategy of NIF release from transduced endothelial cells suggests the
feasibility of blocking the CD11a- and CD11b 2
integrin-dependent PMN adhesion and PMN migration responses
specifically at sites of endothelial cell activation.
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