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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, Immune Systems, Their Diseases, and Possible Treatments
Published in Shamim I. Ahmad, Handbook of Mitochondrial Dysfunction, 2019
Elise Jacquin, Eric Hervouet, Michaël Boyer-Guittaut
Mitochondria, which are supposedly derived from proteobacteria, share some similarities with these organisms, one being the fact that mitochondria protein translation starts with N-formyl-methionine leading to the synthesis of N-formyl-peptides (NFP). These peptides, if released in the extracellular space can be recognized by neutrophils, monocytes, and DCs, thanks to their G-protein-coupled formyl-peptide receptor 1 (FPR1) which can lead to calcium mobilization, cell migration and innate immune response activation.26
Toxoplasma: Animal and In Vitro Models on Toxoplasmosis
Published in Dongyou Liu, Laboratory Models for Foodborne Infections, 2017
Renato Augusto DaMatta, Andrea Cristina Vetö Arnholdt, Farlen José Bebber Miranda
Mice models have recently been used to further explore the role of the microbiota and IL-17 in the gut upon T. gondii infection. Some models show that IL-17 is involved in the immunopathogenesis at the gut mucosal barrier.134,135 However, it has not been clearly identified whether IL-17 is produced by Th17 or ROR-γ innate lymphoid cells or both. Elimination of Paneth cells by IFN-γ produced by Th1 cells induces decreased amounts of antimicrobial peptides, leading to expansion of bacteria of the Enterobacteriaceae family, amplifying immunopathology at the gut after infection.136 On the other hand, mice models have also identified mechanisms of containment of spreading of microflora during infection. Translocation into the luminal space of inflammatory macrophages and neutrophils is observed early in T. gondii infection, where Fpr1 (N-formyl peptide receptor)-expressing neutrophils promote encapsulation of γ-proteobacteria,137 leading to bacterial death probably by NETosis.138
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
No impact of cancer and plague-relevant FPR1 polymorphisms on COVID-19
Published in OncoImmunology, 2020
Adriana Petrazzuolo, Julie Le Naour, Erika Vacchelli, Pascale Gaussem, Syrine Ellouze, Georges Jourdi, Eric Solary, Michaela Fontenay, David M. Smadja, Guido Kroemer
Formyl peptide receptor 1 (FPR1) is a pattern-recognition receptor (PRR)10 that is mostly expressed by myeloid cells including granulocytes, macrophages, and dendritic cells.11 Like other PRRs, FPR1 recognizes pathogen-associated molecular patterns (PAMPs), which are microbial structures, and danger-associated molecular patterns (DAMPs), which are host molecules displayed on, or released by, stressed and dying cells.12–15 As its name indicates, FPR1 recognizes formylated peptides, mostly peptides from bacteria that have undergone a prokaryote-specific post-translation protein modification called formylation.12 However, formylated peptides are also generated by mitochondria (which, in evolutionary terms, are relics of prokaryotes incorporated into the eukaryotic proto-organism).16,17 Moreover, FPR1 interacts with other endogenous ligands including annexin A1 (ANXA1), a ubiquitous protein contained in the cytosol of all nucleated cells that leak into the extracellular space when cells die.18–23 Thus, FPR1 plays a major role in the response to pathogens as well as in the regulation of immune and inflammatory responses.24
A major genetic accelerator of cancer diagnosis: rs867228 in FPR1
Published in OncoImmunology, 2021
Zsofia Sztupinszki, Julie Le Naour, Erika Vacchelli, Pierre Laurent-Puig, Suzette Delaloge, Zoltan Szallasi, Guido Kroemer
Formyl peptide receptor 1 (FPR1) is a pathogen recognition receptor that is activated by a promiscuous array of ligands from bacterial origin (such as formyl peptides) to ligands liberated by stressed cells such as annexin A1 (ANXA1), a ubiquitous cytosolic protein.5 When cancer cells die, for instance in the context of chemotherapies, they leak annexin A1 into the extracellular space.6 Here, ANXA1 acts on FPR1, a seven-transmembrane G protein-coupled receptor to guide the chemotactic movement of myeloid cells (granulocytes, macrophages and dendritic cells) toward the source of ANXA1. For this reason, in preclinical studies, chemotherapy becomes unable to induce a therapeutically relevant anticancer immune response when cancer cells are deficient in ANXA1 or when the immune system lacks functional FPR1.6 Indeed, in both cases, dying tumor cells fail to physically interact with dendritic cells (DCs), the professional antigen-presenting cells that are required to prime cytotoxic T lymphocytes for subsequent recognition and lysis of neoplastic cells.6 Moreover, FPR1-deficient DCs become unable to present major histocompatibility complex (MHC) class I-restricted antigens to CD8+ T lymphocytes. This defect in antigen presentation can be overcome by provision of the Toll-like receptor-3 (TLR3) ligand polyinosinic:polycytidylic acid (poly I:C) both in vitro and in vivo, in Fpr1−/- mice. Thus, chemotherapy with anthracyclines or oxaliplatin against established cancers fails to reduce tumor growth in FPR1-deficient mice unless poly I:C is injected.7