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

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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.

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Formyl peptide receptors: a promiscuous subfamily of G protein-coupled receptors controlling immune responses.

Marc Parmentier, David Communi, Isabelle Migeotte (2006)

The formyl peptide receptor (FPR) family is involved in host defence against pathogens, but also in sensing internal molecules that may constitute signals of cellular dysfunction. It includes three subtypes in human and other primates. FPR responds to formyl peptides derived from bacterial and mitochondrial proteins. FPRL1 displays a large array of exogenous and endogenous ligands, including the chemokine variant sCKbeta8-1, the neuroprotective peptide humanin, and lipoxin A4. Two high affinity agonists (F2L and humanin) were recently described for FPRL2. In mouse, eight FPR-related receptors have been described. Fpr1 is the ortholog of human FPR, while fpr2 appears to share many ligands with human FPRL1. Altogether, the physiological role of the FPR family is still incompletely understood, due in part to the large variety of ligands, the redundancy with other chemoattractant agents, and the lack of clear orthologs between human and mouse receptors. Newly developed tools will allow to study further this family of receptors.

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Formyl-peptide receptors revisited.

Y. Le, P. Murphy, J. Wang (2002)

Leukocytes accumulate at sites of inflammation and microbial infection in direct response to locally produced chemotactic factors, which signal through specific G protein-coupled receptors. The first chemotactic factors to be structurally defined were the N-formyl peptides. Unlike other leukocyte chemoattractants, N-formyl peptides could originate from either an endogenous source, such as the mitochondrial proteins of ruptured host cells, or an exogenous source, such as the proteins of invading pathogens. This suggests that the formyl-peptide receptor (FPR) and its variant FPRL1 (FPR-like 1) are involved in host defense against bacterial infection and in the clearance of damaged cells. Recently, additional, more complex, roles for these receptors have been proposed because FPR, and to a greater extent FPRL1, have been found to interact with a menagerie of structurally diverse pro- and anti-inflammatory ligands associated with different diseases, including amyloidosis, Alzheimer's disease, prion disease and HIV. How these receptors recognize such diverse ligands, which are the most important in vivo, and how they contribute to disease pathogenesis and host defense are basic questions currently under investigation that could lead to new therapeutic targets.

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The role of formylated peptides and formyl peptide receptor 1 in governing neutrophil function during acute inflammation.

David Dorward, Christopher D. Lucas, Gavin Chapman … (2015)

Neutrophil migration to sites of inflammation and the subsequent execution of multiple functions are designed to contain and kill invading pathogens. These highly regulated and orchestrated processes are controlled by interactions between numerous receptors and their cognate ligands. Unraveling and identifying those that are central to inflammatory processes may represent novel therapeutic targets for the treatment of neutrophil-dominant inflammatory disorders in which dysregulated neutrophil recruitment, function, and elimination serve to potentiate rather than resolve an initial inflammatory insult. The first G protein-coupled receptor to be described on human neutrophils, formyl peptide receptor 1 (FPR1), is one such receptor that plays a significant role in the execution of these functions through multiple intracellular signaling pathways. Recent work has highlighted important observations with regard to both receptor function and the importance and functional relevance of FPR1 in the pathogenesis of a range of both sterile and infective inflammatory conditions. In this review, we explore the multiple components of neutrophil migration and function in both health and disease, with a focus on the role of FPR1 in these processes. The current understanding of FPR1 structure, function, and signaling is examined, alongside discussion of the potential importance of FPR1 in inflammatory diseases suggesting that FPR1 is a key regulator of the inflammatory environment.

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Author and article information

Contributors

Tsong-Long Hwang: htl@mail.cgu.edu.tw

Journal

Journal ID (nlm-ta): Sci Rep

Journal ID (iso-abbrev): Sci Rep

Title: Scientific Reports

Publisher: Nature Publishing Group UK (London )

ISSN (Electronic): 2045-2322

Publication date (Electronic): 27 July 2017

Publication date PMC-release: 27 July 2017

Publication date Collection: 2017

Volume: 7

Electronic Location Identifier: 6718

Affiliations

[1 ]Department of Anesthesiology, Chang Gung Memorial Hospital, Taoyuan, 333 Taiwan

[2 ]GRID grid.145695.a, School of Medicine, College of Medicine, , Chang Gung University, ; Taoyuan, 333 Taiwan

[3 ]GRID grid.145695.a, Graduate Institute of Natural Products, , College of Medicine, Chang Gung University, ; Taoyuan, 333 Taiwan

[4 ]GRID grid.145695.a, Chinese Herbal Medicine Research Team, , Healthy Aging Research Center, Chang Gung University, ; Taoyuan, 333 Taiwan

[5 ]GRID grid.418428.3, Department of Cosmetic Science, College of Human Ecology, , Chang Gung University of Science and Technology, ; Taoyuan, 333 Taiwan

[6 ]GRID grid.418428.3, Research Center for Chinese Herbal Medicine, Research Center for Food and Cosmetic Safety, and Graduate Institute of Health Industry Technology, , College of Human Ecology, Chang Gung University of Science and Technology, ; Taoyuan, 333 Taiwan

[7 ]GRID grid.145695.a, Division of Natural Products, Graduate Institute of Biomedical Sciences, , College of Medicine, Chang Gung University, ; Taoyuan, 333 Taiwan

Article

Publisher ID: 7131

DOI: 10.1038/s41598-017-07131-w

PMC ID: 5532207

PubMed ID: 28751674

SO-VID: 3f43d5fb-c8b1-4dad-afbd-e33b6080303d

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Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

History

Date received : 8 November 2016

Date accepted : 23 June 2017

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

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Most cited references 46

Formyl peptide receptors: a promiscuous subfamily of G protein-coupled receptors controlling immune responses.

Formyl-peptide receptors revisited.

The role of formylated peptides and formyl peptide receptor 1 in governing neutrophil function during acute inflammation.

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Cited by 9

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