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Department of Physiology and Biophysics, and
The Price Institute of Surgical Research, Department of Surgery, University of Louisville, School of Medicine, Louisville, KY 40292; and
Health Care Discovery, Novo Nordisk, Novo Allé, Bagsvaerd, Denmark
Previous studies have shown that the neutrophil-derived
heparin-binding protein (HBP), also known as CAP37 or azurocidin,
potentiates the LPS-induced release of proinflammatory cytokines
(TNF-
, IL-1, and IL-6) from isolated human monocytes. To date, the
mechanisms by which HBP enhances LPS-induced monocyte activation have
not been elucidated, and it is not known whether HBP also increases the
LPS-induced production of other bioactive substances. We studied human
monocytes activated by recombinant human HBP and LPS and their
interaction with the LPS receptor CD14. We hypothesized that the
stimulatory effect of HBP on the LPS-induced release of proinflammatory
mediators from monocytes was mediated by specific binding of HBP to
monocytes, which resulted in an up-regulation of CD14. Our results
demonstrated that HBP alone (10 µg/ml) stimulated the production of
TNF- from isolated monocytes. In addition, HBP had an additive
effect on LPS-induced production of TNF- and PGE2,
suggesting a generalized monocyte activation. We used flow cytometry to
demonstrate that HBP had a high affinity to monocytes but not to the
LPS receptor CD14, and experiments performed at 4°C indicated an
energy-dependent step in this process. Confocal microscopy showed that
monocytes internalize HBP within 30 min. These data suggest that
mechanisms other than increased CD14 expression are responsible for the
enhanced release of TNF- or PGE2 in response to HBP and
LPS.
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