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*
Laboratory of Molecular Immunoregulation, Division of Basic Sciences, and
Intramural Research Support Program, Scientific Applications International Corporation-Frederick, National Cancer Institute, Frederick, MD 21702; and
Rega Institute, University of Leuven, Leuven, Belgium
Receptors for the bacterial chemotactic peptide fMLP are
implicated in inflammation and host defense against microbial
infection. We investigated the expression and function of fMLPR in
microglial cells, which share characteristics of mononuclear phagocytes
and play an important role in proinflammatory responses in the CNS. The
expression of the genes encoding formyl peptide receptor (FPR)1 and
FPR2, the high- and low-affinity fMLPR, was detected in a murine
microglial cell line N9, but these cells did not respond to chemotactic
agonists known for these receptors. N9 cells incubated with bacterial
LPS increased the expression of fMLPR genes and developed a species of
specific, but low-affinity, binding sites for fMLP, in association with
marked calcium mobilization and chemotaxis responses to fMLP in a
concentration range that typically activated the low-affinity receptor
FPR2. In addition, LPS-treated N9 cells were chemoattracted by two
FPR2-specific agonists, the HIV-1 envelope-derived V3 peptide, and the
42 aa form of the amyloid 
peptide which is a pathogenic agent in
Alzheimer’s disease. Primary murine microglial cells also expressed
FPR1 and FPR2 genes, but similar
to N9 cells, exhibited FPR2-mediated activation only after LPS
treatment. In contrast to its effect on the function of FPR2, LPS
reduced N9 cell binding and biological responses to the chemokine
stromal cell-derived factor-1
. Thus, LPS selectively modulates the
function of chemoattractant receptors in microglia and may promote host
response in inflammatory diseases in the CNS.
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