Annexin 1 exerts anti-nociceptive effects after peripheral inflammatory pain through formyl-peptide-receptor-like 1 in rat dorsal root ganglion

Pei, Lei; Zhang, J.; Zhao, Fujie; Su, Tangfeng; Huang, Wei; Tian, Jie; Li, Man; Shi, Jing

doi:10.1093/bja/aer299

Cited by 42 publications

(43 citation statements)

References 29 publications

(26 reference statements)

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“…This effect was dampened by Boc-1, demonstrating that the activation of nFPRs mediated this process. Moreover, in previous in vivo experiments, our lab showed that Ac2-26 could attenuate neuropathic pain by interacting with Fpr2 (Pei et al, 2011), providing additional evidence that nFPRs could be a potent candidate for the treatment of inflammatory neuropathies.…”

Section: Discussionmentioning

confidence: 79%

Enhancing the interaction between annexin-1 and formyl peptide receptors regulates microglial activation to protect neurons from ischemia-like injury

Luo

Gao

Sun

et al. 2014

Journal of Neuroimmunology

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Section: Discussionmentioning

confidence: 79%

Enhancing the interaction between annexin-1 and formyl peptide receptors regulates microglial activation to protect neurons from ischemia-like injury

Luo

Gao

Sun

et al. 2014

Journal of Neuroimmunology

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“…Control sections were incubated without the primary antibody, and no staining was observed. Double immunofluorescence staining of ganglion sections was described previously [32]. Mounted NG sections were thawed at room temperature, and indirect immunofluorescence was used to detect P2X1, P2X2, P2X3, and P2X4.…”

Section: Methodsmentioning

confidence: 99%

Comparative Analysis of P2X1, P2X2, P2X3, and P2X4 Receptor Subunits in Rat Nodose Ganglion Neurons

et al. 2014

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Nodose ganglion (NG) neurons are visceral primary sensory neurons. The transmission and regulation of visceral sensation is mediated mainly by the P2X purinoceptor (P2X receptor). Although the characteristics of different P2X receptor subunits in the NG have been studied previously, comprehensive analyses have not been performed. In this study, we used immunohistochemistry, immunocytochemistry, and whole cell patch clamp techniques to compare the expression and function of P2X1, P2X2, P2X3, and P2X4 receptor subunits in adult rat NG neurons. Polyclonal antibodies against the four P2X subunits labeled different subpopulations of NG neurons. P2X1 and P2X3 were expressed mainly in small-to-medium sized NG neurons, whereas P2X2 and P2X4 were located mostly in medium- and larger-sized NG neurons. Over 36% of NG neurons were P2X3 positive, which was higher than the other three P2X subunits. In addition, different types of currents were recorded from neurons expressing different P2X subunits. The fast type of ATP current was recorded from neurons containing P2X1–4 subunits, the intermediate type of current was recorded from neurons containing the P2X1, P2X3, and P2X4 subunits, the slow type was recorded from neurons expressing P2X1–3, and/or P2X4 subunits, whereas the very slow type was recorded from neurons containing the P2X2 and P2X3 subunits. These comparative results provide an anatomical verification of the different subunits in NG neurons, and offer direct support for the idea that various functional NG populations have distinct responses to ATP, which might be in part due to the different expression profiles of diverse P2X subunits.

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“…FPRs have homologs in fish and rodents [13,14]. For example, Fpr2, a homolog of human FPR2, is localized in rat satellite glial cells and neurons of dorsal root ganglions [15]. Expression of Fpr1 and Fpr2 was also reported in rat neuronal stem cells [16].…”

Section: Introductionmentioning

confidence: 99%

Novel ureidopropanamide based N-formyl peptide receptor 2 (FPR2) agonists with potential application for central nervous system disorders characterized by neuroinflammation

Stama

Ślusarczyk

Lacivita

et al. 2017

European Journal of Medicinal Chemistry

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Formyl peptide receptor-2 (FPR2) is a G-protein coupled receptor that plays critical roles in inflammatory reactions. FPR2-specific interaction can be possibly used to facilitate the resolution of pathological inflammatory responses by enhancing endogenous anti-inflammation systems. Starting from our lead agonist 5, we designed new ureidopropanamides derivatives able to activate FPR2 in transfected cells and human neutrophils. The new FPR2 agonists showed good stability towards oxidative metabolism in vitro. Moreover, selected compounds showed anti-inflammatory properties in LPS-stimulated rat primary microglial cells. (S)-3-(4-Cyanophenyl)-N-[[1-(3-chloro-4-fluorophenyl)cyclopropyl]methyl]-2-[3-(4-fluorophenyl)ureido]propanamide ((S)-17) emerged as prospective pharmacological tool to study the effects of FPR2 activation in the central nervous system (CNS) being able to reduce IL-1β and TNF-α levels in LPS-stimulated microglial cells and showing good permeation rate in hCMEC/D3 cells, an in vitro model of blood brain barrier. These results are very promising and can open new therapeutic perspectives in the treatment of CNS disorders characterized by neuroinflammation.

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Annexin 1 exerts anti-nociceptive effects after peripheral inflammatory pain through formyl-peptide-receptor-like 1 in rat dorsal root ganglion

Abstract: Endogenous ANXA1 expression at the DRG level is involved in CFA-induced inflammatory pain, and i.t. ANXA1 20 µg µl(-1) produces its anti-nociceptive effect through FPR2/ALX.

Cited by 42 publications

References 29 publications

Enhancing the interaction between annexin-1 and formyl peptide receptors regulates microglial activation to protect neurons from ischemia-like injury

Enhancing the interaction between annexin-1 and formyl peptide receptors regulates microglial activation to protect neurons from ischemia-like injury

Comparative Analysis of P2X1, P2X2, P2X3, and P2X4 Receptor Subunits in Rat Nodose Ganglion Neurons

Novel ureidopropanamide based N-formyl peptide receptor 2 (FPR2) agonists with potential application for central nervous system disorders characterized by neuroinflammation

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