Abstract
Formyl-peptide receptors (FPR) are expressed in several cell types including phagocytic leukocytes, and a wide variety of agonists of FPR and of its FPRL1 variant have been identified. These ligands interact with their specific receptors on the cellular membrane, and activate specific biological functions through a G-protein-coupled pathway. In nonphagocytic cells, agonist/FPR binding also induces transactivation of the constitutive membrane receptors PDGF-R, EGF-R and uPAR that in turn trigger specific, characteristic intracellular signal transduction pathways. The second messengers resulting from the interaction between ligands and formyl-peptide receptors act on various intracellular kinases (mitogen-activated protein kinases, protein kinases C and B, Jun kinase and some tyrosine kinases). Activation of NADPH oxidase expressed in nonphagocytic cells, and phosphorylation and nuclear translocation of regulatory transcriptional factors may be the downstream targets of this signaling cascade. The activated signal transduction pathways also lead to various biochemical cellular responses that can contribute to cell proliferation, and can protect against cell death and the malignant behavior of several human cancer cell lines. Dissection of the signaling cascade triggered by different agonists will shed light on the role of FPRs in nonphagocytic cells in both human physiology and diseases.
Keywords: Formyl-peptide receptors, NADPH oxidase, reactive oxygen species, transduction signals, kinases, nonphagocytic cells
Current Signal Transduction Therapy
Title: Intracellular Signaling Triggered by Formyl-Peptide Receptors in Nonphagocytic Cells
Volume: 3 Issue: 2
Author(s): Annalisa Iaccio, Antonella Angiolillo and Rosario Ammendola
Affiliation:
Keywords: Formyl-peptide receptors, NADPH oxidase, reactive oxygen species, transduction signals, kinases, nonphagocytic cells
Abstract: Formyl-peptide receptors (FPR) are expressed in several cell types including phagocytic leukocytes, and a wide variety of agonists of FPR and of its FPRL1 variant have been identified. These ligands interact with their specific receptors on the cellular membrane, and activate specific biological functions through a G-protein-coupled pathway. In nonphagocytic cells, agonist/FPR binding also induces transactivation of the constitutive membrane receptors PDGF-R, EGF-R and uPAR that in turn trigger specific, characteristic intracellular signal transduction pathways. The second messengers resulting from the interaction between ligands and formyl-peptide receptors act on various intracellular kinases (mitogen-activated protein kinases, protein kinases C and B, Jun kinase and some tyrosine kinases). Activation of NADPH oxidase expressed in nonphagocytic cells, and phosphorylation and nuclear translocation of regulatory transcriptional factors may be the downstream targets of this signaling cascade. The activated signal transduction pathways also lead to various biochemical cellular responses that can contribute to cell proliferation, and can protect against cell death and the malignant behavior of several human cancer cell lines. Dissection of the signaling cascade triggered by different agonists will shed light on the role of FPRs in nonphagocytic cells in both human physiology and diseases.
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Cite this article as:
Iaccio Annalisa, Angiolillo Antonella and Ammendola Rosario, Intracellular Signaling Triggered by Formyl-Peptide Receptors in Nonphagocytic Cells, Current Signal Transduction Therapy 2008; 3 (2) . https://dx.doi.org/10.2174/157436208784223152
DOI https://dx.doi.org/10.2174/157436208784223152 |
Print ISSN 1574-3624 |
Publisher Name Bentham Science Publisher |
Online ISSN 2212-389X |
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