The formyl peptide receptor (FPR) is a family of G protein-coupled receptors involved in chemotaxis and mediating immune cell response to infection. These receptors may also inhibit the immune system under certain conditions. Scientists have found a series of N-Formylmethionine-containing oligopeptides, including N-formyl-methionyl-leucyl-phenylalanine (FMLP or fMet-Leu-Phe), the most potent and best-known member of this family. They stimulated human and rabbit neutrophils through an apparent receptor-dependent mechanism to migrate in a directional mode in classical laboratory assays of chemotaxis. These oligopeptides are produced from bacteria or synthetic analogs of such products; thus, the N-formyl oligopeptides are considered to be important chemotactic factors. Their receptors are important chemotactic factor receptors that act as signaling and signal-recognizing elements, respectively, to initiate an inflammation response in order to defend against bacterial invasion.
Fig.1 FPR signaling pathways.
Here shows part of formyl peptide receptors in humans including FPR1, FPR2, and FPR3, which encoded by a separate gene (FPR1, FPR2, FPR3). These receptors were originally identified by their ability to bind N-formyl peptides such as N-formylmethionine produced by bacterial or host cell degradation. These three receptors have very different specificities and very different functions for the formyl oligopeptides. 1) The initiation of inflammatory responses to N-formyl peptides released not only by bacteria but also a multiplicity of elements released by host tissues. 2) Dampening and resolving inflammatory responses. 3) Contributing to the development of certain neurological cancers and a series of neurological diseases that are based on amyloid.
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