Premium
Expression and functional role of formyl peptide receptor in human bone marrow‐derived mesenchymal stem cells
Author(s) -
Kim Mi-Kyoung,
Min Do Sik,
Park Yoon Jeong,
Kim Jae Ho,
Ryu Sung Ho,
Bae Yoe-Sik
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.03.078
Subject(s) - mesenchymal stem cell , formyl peptide receptor , chemotaxis , microbiology and biotechnology , pertussis toxin , n formylmethionine leucyl phenylalanine , kinase , chemistry , biology , receptor , signal transduction , biochemistry , g protein
We investigated the expression of formyl peptide receptor (FPR) and its functional role in human bone marrow‐derived mesenchymal stem cells (MSCs). We analyzed the expression of FPR by using ligand‐binding assay with radio‐labeled N ‐formyl‐met‐leu‐phe (fMLF), and found that MSCs express FPR. FMLF stimulated intracellular calcium increase, mitogen‐activated protein kinases activation, and Akt activation, which were mediated by G i proteins. MSCs were chemotactically migrated to fMLF. FMLF‐induced MSC chemotaxis was also completely inhibited by pertussis toxin, LY294002, and PD98059, indicating the role of G i proteins, phosphoinositide 3‐kinase, and extracellular signal regulated protein kinase. N‐terminal fragment of annexin‐1, Anx‐1(2–26), an endogenous agonist for FPR, also induced chemotactic migration of MSCs. Thus MSCs express functional FPR, suggesting a new (patho)physiological role of FPR and its ligands in regulating MSC trafficking during induction of injured tissue repair.