A RECOMBINANT AMINO-TERMINAL FRAGMENT OF BACTERICIDAL PERMEABILITY-INCREASING PROTEIN (RBPI23) INHIBITS SOLUBLE CD14-MEDIATED LIPOPOLYSACCHARIDE-INDUCED ENDOTHELIAL ADHERENCE FOR HUMAN NEUTROPHILS
K. Huang et al., A RECOMBINANT AMINO-TERMINAL FRAGMENT OF BACTERICIDAL PERMEABILITY-INCREASING PROTEIN (RBPI23) INHIBITS SOLUBLE CD14-MEDIATED LIPOPOLYSACCHARIDE-INDUCED ENDOTHELIAL ADHERENCE FOR HUMAN NEUTROPHILS, Shock, 1(2), 1994, pp. 81-86
Exposure of cultured human umbilical vein endothelial cells (HUVEC) to
lipopolysaccharide (LPS) or interleukin 1 (IL-1) causes increased exp
ression of adhesion molecules such as E-selectin and CD54 by HUVEC and
consequently increased adherence of peripheral blood neutrophils. A r
ecombinant amino-terminal fragment of bactericidal/permeability increa
sing protein (rBPI23) was shown to specifically block the LPS-induced
adhesiveness of HUVEC for neutrophils. rBPI23 also prevented the LPS-
but not IL-1beta-induced upregulation on HUVEC of E-selectin and CD54.
Furthermore, this inhibition was evident even when the endothelial ce
lls were exposed to LPS for up to 1-2 h prior to rBPI23 addition. The
inhibitory effects of an anti-CD14 monoclonal antibodies (mAb) were si
milar to those of rBPI23. Combination of the anti-CD14 mAb and rBPI23
resulted inhibition greater than either one used alone. These studies
demonstrate that rBPI23 acts as a specific and potent inhibitor of sol
uble CD14-mediated LPS induction.