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Fibronectin enhances in vitro lipopolysaccharide priming of
polymorphonuclear leukocytes
R Bortolussi, K Rajaraman, G Qing and R Rajaraman
Department of Pediatrics, Dalhousie University, Halifax, Nova Scotia,
Canada.
We investigated the role of humoral factors in lipopolysaccharide (LPS)
priming of polymorphonuclear leukocytes (PMN) using cells isolated from
adults and from neonates. Plasma from newborn infants had decreased priming
activity of adult plasma when mixed with LPS in studies measuring oxidative
radical production of PMN after stimulation with a formyl bacterial
oligopeptide (fMLP). This marked difference was not caused by LPS binding
protein (LBP) because the LBP concentration in newborn and adult plasma
were similar (138.4 +/- 12.9 U for adults, and 126.9 +/- 12.1 U for
neonates, P = .53). Therefore, we attempted to identify other plasma
factors that may contribute to LPS priming of PMN. We identified an LPS
priming factor for PMN that is present in plasma, heat stable (56 degrees C
for 30 minutes), enhanced by heparin, and concentrated in cold precipitates
of plasma. Because these properties resemble those of plasma fibronectin,
we assessed the role of fibronectin in LPS priming of PMN. Although
fibronectin in phosphate- buffered saline (PBS) had little effect on LPS
priming of PMN, fibronectin in combination with other plasma factors
appeared to play a role in LPS priming of PMN because (1) removing
fibronectin from adult plasma dramatically decreased LPS priming activity
from plasma (P < .005), (2) addition of fibronectin to
fibronectin-depleted plasma restored its LPS plasma priming activity (P
< .05), and (3) neutralizing fibronectin with antibody decreased the LPS
priming activity of plasma (60.3 +/- 1.3 v 30.2 +/- 2.2, P < .01). Thus,
plasma fibronectin plays a role in LPS priming of PMN in the presence of
other factors in plasma.
Volume 89,
Issue 11,
pp. 4182-4189,
06/01/1997
Copyright © 1997 by The American Society of Hematology

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