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Division of Infectious Diseases, University of Colorado Health Sciences Center, Denver, CO 80262
The IL-1R accessory protein (IL-1RAcP) plays a role in IL-1R
signaling by forming a complex with IL-1RI bound to the IL-1 ligand. We
identified four hydrophilic peptide regions of the extracellular
IL-1RAcP that may be available for complex formation (peptide 1, 71–83
domain I; peptide 2, 204–211 domain II; peptide 3, 282–292 domain
III; and peptide 4, 304–314 domain III). These peptides were
synthesized, coupled to keyhole limpet hemocyanin, and used to produce
rabbit antisera. Each affinity-purified antiserum showed specificity
for the respective peptide without cross-reactivity. Anti-peptide 2, 3,
and 4 recognized surface expression of IL-1RAcP on the Th2 D10S cells
by FACS and inhibited IL-1-driven proliferation. Anti-peptide 4
recognized intact IL-1RAcP and soluble IL-1RAcP. Anti-IL-1RAcP-peptide
4, which targets the terminal segment of domain III, inhibited 80% of
IL-1ß-driven proliferation of D10S cells. However, these IL-1RAcP Abs
had no effect on the activity of human or mouse IL-1
. Whereas
IL-1ß down-regulated IL-1RI surface expression
(p < 0.05), there was no change in the
surface expression of IL-1RAcP. Moreover, murine IL-10 increased
surface expression of IL-1RI, but did not affect expression of IL-1RAcP
or the proliferation of D10S cells. Steady state levels of mRNA for
IL-1RAcP and IL-1RI in D10S cells showed a similar pattern to that of
surface expression of the respective receptors. We conclude that 1)
blocking IL-1RAcP inhibits IL-1 signaling in D10S cells, 2) domains-II
and III may be involved in complex formation with IL-1RI, 3) IL-1RAcP
is not regulated as is IL-1RI in the same cells, and 4) IL-1
responsiveness is dependent on the expression of IL-1RI, not IL-1RAcP.
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