The Leukocyte Chemotactic Receptor FPR1 Is Functionally Expressed on Human Lens Epithelial Cells

Schneider, Erich H.; Weaver, Joseph D.; Gaur, Sonia; Tripathi, Brajendra K.; Jesaitis, Algirdas J.; Zelenka, Peggy S.; Gao, Ji-Liang; Murphy, Philip M.

doi:10.1074/jbc.m112.411181

Cited by 13 publications

(13 citation statements)

References 40 publications

(47 reference statements)

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“…3 ). Similar effects of FPR1 stimulation have recently been described in both normal and tumor cells [ 18 , 20 , 26 , 27 ]. Calcium is a ubiquitous second messenger and in cancer it has been implicated in numerous important features of tumorigenesis, including angiogenesis, motility, proliferation and migration [ 28 ].…”

Section: Discussionsupporting

confidence: 74%

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The role of formyl peptide receptor 1 (FPR1) in neuroblastoma tumorigenesis

et al. 2016

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BackgroundFormyl peptide receptor 1 (FPR1) is a G protein-coupled receptor mainly expressed by the cells of myeloid origin, where it mediates the innate immune response to bacterial formylated peptides. High expression of FPR1 has been detected in various cancers but the function of FPR1 in tumorigenesis is poorly understood.MethodsExpression of FPR1 in neuroblastoma cell lines and primary tumors was studied using RT-PCR, western blotting, immunofluorescence and immunohistochemistry. Calcium mobilization assays and western blots with phospho-specific antibodies were used to assess the functional activity of FPR1 in neuroblastoma. The tumorigenic capacity of FPR1 was assessed by xenografting of neuroblastoma cells expressing inducible FPR1 shRNA, FPR1 cDNA or control shRNA in nude mice.ResultsFPR1 is expressed in neuroblastoma primary tumors and cell lines. High expression of FPR1 corresponds with high-risk disease and poor patient survival. Stimulation of FPR1 in neuroblastoma cells using fMLP, a selective FPR1 agonist, induced intracellular calcium mobilization and activation of MAPK/Erk, PI3K/Akt and P38-MAPK signal transduction pathways that were inhibited by using Cyclosporin H, a selective receptor antagonist for FPR1. shRNA knock-down of FPR1 in neuroblastoma cells conferred a delayed xenograft tumor development in nude mice, whereas an ectopic overexpression of FPR1 promoted augmented tumorigenesis in nude mice.ConclusionOur data demonstrate that FPR1 is involved in neuroblastoma development and could represent a therapy option for the treatment of neuroblastoma.Electronic supplementary materialThe online version of this article (doi:10.1186/s12885-016-2545-1) contains supplementary material, which is available to authorized users.

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Section: Discussionsupporting

confidence: 74%

“…More recently, FPR1 has also been detected in cells of non-myeloid origin such as, smooth muscle cells, lens epithelial cells, fibroblasts, etc. indicating the involvement of the receptor in a wide variety of inflammatory responses [ 5 , 16 , 18 , 19 ].…”

Section: Discussionmentioning

confidence: 99%

The role of formyl peptide receptor 1 (FPR1) in neuroblastoma tumorigenesis

et al. 2016

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“…A wide range of molecular weights of FPR2 on SDS–PAGE gels has been reported in the literature, ranging from 38 to 100 kDa, which is attributed to glycosylation or dimerization [ 25 , 48 , 49 ]. More than a single band of protein is also found in Western blots of FPR1, which is attributed to a mixture of non-glycosylated and differently-glycosylated forms of the receptor [ 50 , 51 ]. Glycosylation is necessary for the proper folding of FPR1 [ 51 ], and this is likely also for FPR2.…”

Section: Discussionmentioning

confidence: 99%

Localisation of Formyl-Peptide Receptor 2 in the Rat Central Nervous System and Its Role in Axonal and Dendritic Outgrowth

Ismail

Koh

et al. 2018

Neurochem Res

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Arachidonic acid and docosahexaenoic acid (DHA) released by the action of phospholipases A2 (PLA2) on membrane phospholipids may be metabolized by lipoxygenases to the anti-inflammatory mediators lipoxin A4 (LXA4) and resolvin D1 (RvD1), and these can bind to a common receptor, formyl-peptide receptor 2 (FPR2). The contribution of this receptor to axonal or dendritic outgrowth is unknown. The present study was carried out to elucidate the distribution of FPR2 in the rat CNS and its role in outgrowth of neuronal processes. FPR2 mRNA expression was greatest in the brainstem, followed by the spinal cord, thalamus/hypothalamus, cerebral neocortex, hippocampus, cerebellum and striatum. The brainstem and spinal cord also contained high levels of FPR2 protein. The cerebral neocortex was moderately immunolabelled for FPR2, with staining mostly present as puncta in the neuropil. Dentate granule neurons and their axons (mossy fibres) in the hippocampus were very densely labelled. The cerebellar cortex was lightly stained, but the deep cerebellar nuclei, inferior olivary nucleus, vestibular nuclei, spinal trigeminal nucleus and dorsal horn of the spinal cord were densely labelled. Electron microscopy of the prefrontal cortex showed FPR2 immunolabel mostly in immature axon terminals or ‘pre-terminals’, that did not form synapses with dendrites. Treatment of primary hippocampal neurons with the FPR2 inhibitors, PBP10 or WRW4, resulted in reduced lengths of axons and dendrites. The CNS distribution of FPR2 suggests important functions in learning and memory, balance and nociception. This might be due to an effect of FPR2 in mediating arachidonic acid/LXA4 or DHA/RvD1-induced axonal or dendritic outgrowth.

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“…Fluorescein isothiocyanate (FITC) can be used to investigate the fMLF receptors by flow cytometry according to Schneider et al . . As such, the effects of RvE1 on the expression level of the fMLF receptor was investigated by flow cytometry using FITC‐fMLF.…”

Section: Methodsmentioning

confidence: 99%

Resolvin E1, but not resolvins E2 and E3, promotes fMLF‐induced ROS generation in human neutrophils

et al. 2018

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E-series resolvins are biosynthesized from eicosapentaenoic acid during the resolution phase of acute inflammation and enhance inflammation resolution. However, the role of E-series resolvins in inflammation resolution is not yet known. Herein, we show that in human polymorphonuclear neutrophils (PMNs), resolvin E1 (RvE1) selectively enhances reactive oxygen species (ROS) generation induced by N-formylmethionyl-leucyl-phenylalanine. The RvE1-mediated enhancement is eliminated by a pan-antagonist of leukotriene B4 (LTB4) receptors, LY255283, or an NADPH oxidase inhibitor, diphenyleneiodonium. Thus, RvE1 enhances NADPH oxidase-mediated ROS generation via LTB4 receptors. Unlike RvE1, resolvins E2 and E3 do not show such activation of PMNs. Our findings suggest that RvE1 contributes to regulation of ROS generation, in accordance with the inflammatory state of the host.

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The Leukocyte Chemotactic Receptor FPR1 Is Functionally Expressed on Human Lens Epithelial Cells

Cited by 13 publications

References 40 publications

The role of formyl peptide receptor 1 (FPR1) in neuroblastoma tumorigenesis

The role of formyl peptide receptor 1 (FPR1) in neuroblastoma tumorigenesis

Localisation of Formyl-Peptide Receptor 2 in the Rat Central Nervous System and Its Role in Axonal and Dendritic Outgrowth

Resolvin E1, but not resolvins E2 and E3, promotes fMLF‐induced ROS generation in human neutrophils

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