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N‐formyl peptide receptor‐1 is important for homeostasis of intestinal epithelial cells
Author(s) -
Alam Ashfaqul,
Leoni Giovanna,
Wentworth Christy,
Nusrat Asma,
Neish Andrew
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.56.2
Subject(s) - receptor , microbiology and biotechnology , intestinal epithelium , biology , mapk/erk pathway , formyl peptide receptor , peptide , chemistry , chemotaxis , epithelium , signal transduction , biochemistry , genetics
N‐formyl peptide receptors (FPRs), which in humans include FPR1, FPR2 and FPR3, are an important family of pattern recognition receptors that bind an array of bacterial as well as host derived peptide and nonpeptide ligands. FPRs are G protein coupled surface receptors, which are well described in mediating phagocyte functions. We have demonstrated FPRs on the apical surface of intestinal epithelial cells (IEC) and have shown that in IECs FPR induces ROS generation in response to bacterial fMLF (a formylated tripeptide), viable Lactobacillus rhamnosus GG, and endogenous annexin A1 mimetic (Ac 2‐26). Furthermore, we showed that FPR‐elicited ROS activates the noninflammatory ERK MAPK pathway and enhances migration of IECs. We hypothesize that FPR1, the high‐affinity receptor, is important for motility of intestinal epithelia. Mice deficient in FPR1 demonstrates normal intestinal tissue architecture; however, intestinal crypts of the FPR1 null mouse contain more proliferating cells, and show slower migration along the crypt‐villus axis. These data suggest that FPR1 is important in maintaining homeostasis of the intestinal epithelia.