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Molecular characterization of the EMR2 receptor signaling pathways in human neutrophils

The EGF‐TM7 receptors belong to a subfamily of adhesion‐GPCRs that are predominantly expressed on myeloid leukocytes. We have recently shown that ligation of EMR2, one of the EGF‐TM7 members, by 2A1 mAb primes numerous neutrophil functions, including cell adhesion, migration, release of reactive oxygen species and degranulation (FASEB J. 22(3):741‐751, 2008). However, the precise signaling mechanism mediated by EMR2 remains elusive. Herein, we examined the activation status and kinetics of signalling molecules well known in neutrophil activation. Our results show rapid increased phosphorylation of mitogen‐activated protein kinases (MAPK), p38, ERK, and JNK, in neutrophils upon EMR2 ligation. In addition, ligation of EMR2 by 2A1 was shown to reduce the LPS‐mediated inhibitory effect on spontaneous neutrophil apoptosis. Taken together, our results suggested that the function of EMR2 receptor in neutrophil is most likely signaled via MAPKs. (Research support: CMRPD330083)