title: Antimicrobial peptide scolopendrasin VII, derived from the centipede Scolopendra subspinipes mutilans, stimulates macrophage chemotaxis via formyl peptide receptor 1.
abstract: In this study, we report that one of the antimicrobial peptides scolopendrasin VII, derived from Scolopendra subspinipes mutilans, stimulates actin polymerization and the subsequent chemotactic migration of macrophages through the activation of ERK and protein kinase B (Akt) activity. The scolopendrasin VII-induced chemotactic migration of macrophages is inhibited by the formyl peptide receptor 1 (FPR1) antagonist cyclosporine H. We also found that scolopendrasin VII stimulate the chemotactic migration of FPR1-transfected RBL-2H3 cells, but not that of vector-transfected cells; moreover, scolopendrasin VII directly binds to FPR1. Our findings therefore suggest that the antimicrobial peptide scolopendrasin VII, derived from Scolopendra subspinipes mutilans, stimulates macrophages, resulting in chemotactic migration via FPR1 signaling, and the peptide can be useful in the study of FPR1-related biological responses.
authors.affiliation: Department of Biological Sciences, Sungkyunkwan University, Suwon 16419, Korea.
authors.forename: Yoo Jung
authors.initials: YJ
authors.lastname: Park
authors.affiliation: Department of Biological Sciences, Sungkyunkwan University, Suwon 16419; Mitochondria Hub Regulation Center, Dong-A University, Busan 49201, Korea.
authors.forename: Ha Young
authors.initials: HY
authors.lastname: Lee
authors.affiliation: Department of Biological Sciences, Sungkyunkwan University, Suwon 16419, Korea.
authors.forename: Young Su
authors.initials: YS
authors.lastname: Jung
authors.affiliation: Department of Hematology-Oncology, Ajou University School of Medicine, Suwon 16499, Korea.
authors.forename: Joon Seong
authors.initials: JS
authors.lastname: Park
authors.affiliation: Department of Agricultural Biology, National Academy of Agricultural Science, RDA, Wanju 55365, Korea.
authors.forename: Jae Sam
authors.initials: JS
authors.lastname: Hwang
authors.affiliation: Department of Biological Sciences, Sungkyunkwan University, Suwon 16419; Mitochondria Hub Regulation Center, Dong-A University, Busan 49201; Department of Health Sciences and Technology, SAIHST, Sungkyunkwan University, Seoul 06351, Korea.
authors.forename: Yoe-Sik
authors.initials: YS
authors.lastname: Bae
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology*; D001181:Arthropods / Q000737:chemistry; D002630:Chemotactic Factors / Q000494:pharmacology; D002633:Chemotaxis / Q000187:drug effects*; D048049:Extracellular Signal-Regulated MAP Kinases / Q000378:metabolism; D008264:Macrophages / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D051379:Mice; D008810:Mice, Inbred C57BL; D037342:Pertussis Toxin / Q000494:pharmacology; D051057:Proto-Oncogene Proteins c-akt / Q000378:metabolism; D044042:Receptors, Formyl Peptide; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism
chemical_list: D000199:Actins; D023181:Antimicrobial Cationic Peptides; D002630:Chemotactic Factors; D044042:Receptors, Formyl Peptide; D043562:Receptors, G-Protein-Coupled; D037342:Pertussis Toxin; D051057:Proto-Oncogene Proteins c-akt; D048049:Extracellular Signal-Regulated MAP Kinases