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Biochem Biophys Res Commun. 2017 Dec 9;494(1-2):352-357. doi: 10.1016/j.bbrc.2017.10.019. Epub 2017 Oct 5.

A novel antimicrobial peptide isolated from centipede Scolopendra subspinipes mutilans stimulates neutrophil activity through formyl peptide receptor 2.

Author information

1
Department of Biological Sciences, Sungkyunkwan University, Suwon 16419, Republic of Korea.
2
Department of Agricultural Biology, National Academy of Agricultural Science, RDA, Wanju 55365, Republic of Korea.
3
Department of Biological Sciences, Sungkyunkwan University, Suwon 16419, Republic of Korea; Department of Health Sciences and Technology, SAIHST, Sungkyunkwan University, Seoul 06351, Republic of Korea. Electronic address: yoesik@skku.edu.

Abstract

In this study, we identified scolopendrasin X, a novel antimicrobial peptide (AMP), from centipede Scolopendra subspinipes mutilans. Scolopendrasin X strongly stimulated mouse neutrophils, resulting in intracellular calcium increase, chemotactic migration through pertussis toxin-sensitive G-protein and phospholipase C pathway, and increased superoxide anion production in neutrophils. Target receptor for scolopendrasin X, formyl peptide receptor (FPR)2 mediated scolopendrasin X-induced neutrophil activation. Moreover, scolopendrasin X significantly blocked inflammatory cytokine production induced by lipopolysaccharide in mouse neutrophils. Taken together, our results suggest that the novel AMP scolopendrasin X can be used as a material to regulate neutrophil activity through FPR2.

KEYWORDS:

Antimicrobial peptide; Chemotaxis; Formyl peptide receptor 2; Neutrophil; Scolopendra subspinipes mutilans; Superoxide anion

PMID:
28988115
DOI:
10.1016/j.bbrc.2017.10.019
[Indexed for MEDLINE]

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