Yy. Le et al., Novel pathophysiological role of classical chemotactic peptide receptors and their communications with chemokine receptors, IMMUNOL REV, 177, 2000, pp. 185-194
The bacterial N-formylpeptides, such as N-formyl-Met-Leu-Phe (fMLF), are so
me of the first identified and most potent chemoattractants for phagocytic
leukocytes. Two fMLF receptors, the high affinity formyl peptide receptor (
FPR) and its low affinity variant FPR-like I (FPRL1), belong to the seven-t
ransmembrane, Gi protein-coupled receptor superfamily which also includes c
hemokine receptors. Despite their reaction with bacterial chemotactic pepti
des, the physiological role of these receptors in humans remains unclear Ou
r recent studies have identified novel exogenous as well as host-derived ag
onists for FPR and FPRL1. Furthermore, activation of these receptors by the
ir agonists results in desensitization of the receptors for other chemoattr
actants, including two chemokine receptors, CCR5 and CXCR4, which serve as
major co-receptors for HIV-1. These results suggest that FPR and FPRL1 may
play important roles not only in host defense and immunological responses b
ut also in the fine tuning of cell activation in the presence of multiple s
timuli.