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Immune Responses Regulated by Exosomal Mechanisms in Cardiovascular Disease
Published in Shyam S. Bansal, Immune Cells, Inflammation, and Cardiovascular Diseases, 2022
Brooke Lee, Ioannis D. Kyriazis, Ruturaj Patil, Syed Baseeruddin Alvi, Amit Kumar Rai, Mahmood Khan, Venkata Naga Srikanth Garikipati
Additionally, formylated peptides resemble bacterial DNA and can be detected by formyl peptide receptor 1, a chemoattractant that can also activate neutrophils (Oka, Hikoso et al. 2012). Neutrophil activation may be induced by the state of cardiac endothelial cells, which allow neutrophils to pass through their barrier to treat the injured cell (Singh and Saini 2003). It has recently been identified that activated neutrophils release exosomes that express neutrophil elastase extracellularly and that have the ability to attach to the extracellular matrix to further provoke the development of chronic obstructive pulmonary disease (COPD) (Genschmer, Russell et al. 2019). The work done by Genschmer et al. can serve as a platform for investigating the pathophysiological correlation between COPD and CVD, as they commonly coexist (Rabe, Hurst et al. 2018).
Mitochondrial Dysfunction and Allergic Disease
Published in Shamim I. Ahmad, Handbook of Mitochondrial Dysfunction, 2019
Kritika Khanna, Anurag Agrawal
Akin to bacteria, mitochondria initiate protein synthesis with N-formyl methionine instead of methionine residue (Smith and Marcker 1968). Such N-formyl peptides (NFPs) are recognized by formyl peptide receptors that are expressed by immune cells and endothelial cells. Binding of these NFPs activates these cells, subsequently driving inflammatory cytokine secretion, promoting chemotaxis and increasing oxidative burst in the target cells (Panaro et al. 2006; Crouser et al. 2009).
Formyl peptide receptor-1 (FPR1) represses intestinal oncogenesis
Published in OncoImmunology, 2023
Julie Le Naour, Léa Montégut, Yuhong Pan, Sarah Adriana Scuderi, Pierre Cordier, Adrien Joseph, Allan Sauvat, Valerio Iebba, Juliette Paillet, Gladys Ferrere, Ludivine Brechard, Claire Mulot, Grégory Dubourg, Laurence Zitvogel, Jonathan G. Pol, Erika Vacchelli, Pierre-Laurent Puig, Guido Kroemer
Formyl peptide receptors (FPRs) are pattern recognition receptors known to play important roles in diverse physiological processes, including host defense and inflammation.5 FPRs recognize peptides bearing a particular post-translational modification, namely N-formylation, that is only catalyzed by enzymes present in bacteria and in mitochondria. Hence, these N-formylated peptides consist of microbial pathogen-associated molecular patterns (MAMPs) or danger-associated molecular patterns (DAMPs) derived from dying cells spilling mitochondrial content.6,7 Furthermore, FPR1 recognizes non-formylated proteins such as (i) cathepsin G,8 (ii) family with sequence similarity 19 (chemokine (C–C motif)-like), member A4 (FAM19A4),9 and (iii) annexin A1 (ANXA1) that is released from the cytosolic compartment of dying and dead cells, hence constituting yet another DAMP.7,10
An independent predictor of poor prognosis in locally advanced rectal cancer: rs867228 in formyl peptide receptor 1 (FPR1)
Published in OncoImmunology, 2021
Shu-Fen Chiang, Kevin Chih-Yang Huang, William Tzu-Liang Chen, Tsung-Wei Chen, Tao-Wei Ke, K. S. Clifford Chao
Formyl peptide receptor 1 FPR1 is a G-protein-coupled receptor (GPCR) mostly expressed in dendritic cell (DC) progenitor and other myeloid cells and plays several important roles in immune responses. For example, FPR1 mediates neutrophil activation and migration in innate immunity, DC positioning, and maturation in adaptive immunity and antitumor immunity.7 Several single nucleotide polymorphisms (SNPs) were reported to influence the functions of FPR1. Among these SNPs, E346A (rs867228, c. 1037 A > C) is a loss-of-function SNP that affects the extreme C-terminus of FPR1, thus altering the interaction with Gi-proteins and causing defective signal transduction.8,9 The primary ligands for FPR1 are bacterial and mitochondrial N-formylated peptides which were actively released from dead and dying pathogens or host cells. In addition, FPR1 is the PRR for ANXA1, which is necessary for chemotherapy-induced antitumor immunity. Knockout or inhibition of FPR1 resulted in deficient interactions of DCs with dead cancer cells, leading to decreased T cell infiltration in tumor and attenuating the therapeutic efficacy of chemotherapy. FPR1-E346A was also reported to have a negative influence on the prognosis of breast patients treated with anthracycline-based chemotherapy, colorectal cancer patients treated with oxaliplatin-based chemotherapy.7,10
Enterobactin induces the chemokine, interleukin-8, from intestinal epithelia by chelating intracellular iron
Published in Gut Microbes, 2020
Piu Saha, Beng San Yeoh, Xia Xiao, Rachel M. Golonka, Ahmed A. Abokor, Camilla F. Wenceslau, Yatrik M. Shah, Bina Joe, Matam Vijay-Kumar
Formyl peptide receptors (FPRs) are expressed by various non-hematopoietic cells, including IECs, and have important roles in maintaining mucosal homeostasis and facilitating inflammatory responses.46 These FPRs are known to be activated via N-formyl peptides uniquely expressed by bacteria and mitochondria. We considered the possibility that Ent could interact with FPRs given that the cyclic structure of Ent contains a tri-ester lactone of 2,3-dihydroxybenzoylserine, which is formed by an amide linkage of three 2,3-dihydroxybenzoic acid groups to three L-serine units.47 To elucidate the role of FPRs in Ent-induced IL-8 secretion in IECs, we sought to inhibit FPR1/FPR2 signaling by using the pan-FPR antagonist, N-tert-butyloxycarbonyl-Phe-Leu-Phe-Leu-Phe (Boc2).48 Pre-treating HT29 cells with Boc2 at either 1, 10 or 50 µM concentrations were sufficient in preventing Ent-induced IL-8 secretion in HT29 cells (Figure 6(a,b)). The inhibitory effect of 10 µM Boc2 was not averted despite increasing the concentration of Ent from 1 to 50 µM (Figure 6(b)). To differentiate whether FPR1 or FPR2 could be the potential receptor for Ent, we next used cyclosporin H (CspH), a potent and selective competitive antagonist for the FPR1 isoform. Pre-treating HT29 cells with CspH dose-dependently inhibited Ent-induced IL-8 secretion (Figure 6(c)). The inhibitory effects of CspH, however, could be rescued by increasing the concentration of Ent, suggesting that both compounds may be competing for FPR1 binding (Figure 6(d)).