Honokiol suppresses formyl peptide-induced human neutrophil activation by blocking formyl peptide receptor 1

Abstract Formyl peptide receptor 1 (FPR1) mediates bacterial and mitochondrial N-formyl peptides-induced neutrophil activation. Therefore, FPR1 is an important therapeutic target for drugs to treat septic or sterile inflammatory diseases. Honokiol, a major bioactive compound of Magnoliaceae plants,...

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Autores principales:	Fu-Chao Liu, Huang-Ping Yu, Yu-Ting Syu, Jia-You Fang, Chwan-Fwu Lin, Shih-Hsin Chang, Yen-Tung Lee, Tsong-Long Hwang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5e76b5a87cc04a5e801e9ff57c6aee21
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spelling	oai:doaj.org-article:5e76b5a87cc04a5e801e9ff57c6aee212021-12-02T11:52:21ZHonokiol suppresses formyl peptide-induced human neutrophil activation by blocking formyl peptide receptor 110.1038/s41598-017-07131-w2045-2322https://doaj.org/article/5e76b5a87cc04a5e801e9ff57c6aee212017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-07131-whttps://doaj.org/toc/2045-2322Abstract Formyl peptide receptor 1 (FPR1) mediates bacterial and mitochondrial N-formyl peptides-induced neutrophil activation. Therefore, FPR1 is an important therapeutic target for drugs to treat septic or sterile inflammatory diseases. Honokiol, a major bioactive compound of Magnoliaceae plants, possesses several anti-inflammatory activities. Here, we show that honokiol exhibits an inhibitory effect on FPR1 binding in human neutrophils. Honokiol inhibited superoxide anion generation, reactive oxygen species formation, and elastase release in bacterial or mitochondrial N-formyl peptides (FPR1 agonists)-activated human neutrophils. Adhesion of FPR1-induced human neutrophils to cerebral endothelial cells was also reduced by honokiol. The receptor-binding results revealed that honokiol repressed FPR1-specific ligand N-formyl-Nle-Leu-Phe-Nle-Tyr-Lys-fluorescein binding to FPR1 in human neutrophils, neutrophil-like THP-1 cells, and hFPR1-transfected HEK293 cells. However, honokiol did not inhibit FPR2-specific ligand binding to FPR2 in human neutrophils. Furthermore, honokiol inhibited FPR1 agonist-induced calcium mobilization as well as phosphorylation of p38 MAPK, ERK, and JNK in human neutrophils. In conclusion, our data demonstrate that honokiol may have therapeutic potential for treating FPR1-mediated inflammatory diseases.Fu-Chao LiuHuang-Ping YuYu-Ting SyuJia-You FangChwan-Fwu LinShih-Hsin ChangYen-Tung LeeTsong-Long HwangNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Fu-Chao Liu Huang-Ping Yu Yu-Ting Syu Jia-You Fang Chwan-Fwu Lin Shih-Hsin Chang Yen-Tung Lee Tsong-Long Hwang Honokiol suppresses formyl peptide-induced human neutrophil activation by blocking formyl peptide receptor 1
description	Abstract Formyl peptide receptor 1 (FPR1) mediates bacterial and mitochondrial N-formyl peptides-induced neutrophil activation. Therefore, FPR1 is an important therapeutic target for drugs to treat septic or sterile inflammatory diseases. Honokiol, a major bioactive compound of Magnoliaceae plants, possesses several anti-inflammatory activities. Here, we show that honokiol exhibits an inhibitory effect on FPR1 binding in human neutrophils. Honokiol inhibited superoxide anion generation, reactive oxygen species formation, and elastase release in bacterial or mitochondrial N-formyl peptides (FPR1 agonists)-activated human neutrophils. Adhesion of FPR1-induced human neutrophils to cerebral endothelial cells was also reduced by honokiol. The receptor-binding results revealed that honokiol repressed FPR1-specific ligand N-formyl-Nle-Leu-Phe-Nle-Tyr-Lys-fluorescein binding to FPR1 in human neutrophils, neutrophil-like THP-1 cells, and hFPR1-transfected HEK293 cells. However, honokiol did not inhibit FPR2-specific ligand binding to FPR2 in human neutrophils. Furthermore, honokiol inhibited FPR1 agonist-induced calcium mobilization as well as phosphorylation of p38 MAPK, ERK, and JNK in human neutrophils. In conclusion, our data demonstrate that honokiol may have therapeutic potential for treating FPR1-mediated inflammatory diseases.
format	article
author	Fu-Chao Liu Huang-Ping Yu Yu-Ting Syu Jia-You Fang Chwan-Fwu Lin Shih-Hsin Chang Yen-Tung Lee Tsong-Long Hwang
author_facet	Fu-Chao Liu Huang-Ping Yu Yu-Ting Syu Jia-You Fang Chwan-Fwu Lin Shih-Hsin Chang Yen-Tung Lee Tsong-Long Hwang
author_sort	Fu-Chao Liu
title	Honokiol suppresses formyl peptide-induced human neutrophil activation by blocking formyl peptide receptor 1
title_short	Honokiol suppresses formyl peptide-induced human neutrophil activation by blocking formyl peptide receptor 1
title_full	Honokiol suppresses formyl peptide-induced human neutrophil activation by blocking formyl peptide receptor 1
title_fullStr	Honokiol suppresses formyl peptide-induced human neutrophil activation by blocking formyl peptide receptor 1
title_full_unstemmed	Honokiol suppresses formyl peptide-induced human neutrophil activation by blocking formyl peptide receptor 1
title_sort	honokiol suppresses formyl peptide-induced human neutrophil activation by blocking formyl peptide receptor 1
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/5e76b5a87cc04a5e801e9ff57c6aee21
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Honokiol suppresses formyl peptide-induced human neutrophil activation by blocking formyl peptide receptor 1

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