Formyl peptide receptor 1: Difference between revisions

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Latest revision as of 13:03, 17 March 2025

Formyl peptide receptor 1 (FPR1) is a protein that in humans is encoded by the FPR1 gene. FPR1 is a member of the G protein-coupled receptor family, and it plays a crucial role in the immune system by regulating neutrophil migration.

Structure[edit]

FPR1 is a transmembrane protein that consists of seven transmembrane helices, an extracellular N-terminus, and an intracellular C-terminus. The protein is approximately 350 amino acids in length.

Function[edit]

FPR1 is primarily expressed on phagocytic cells such as neutrophils and monocytes. It is involved in the chemotactic activity towards site of inflammation. The receptor is activated by formyl peptides, which are produced by bacteria and mitochondria. Upon activation, FPR1 triggers a series of intracellular signaling pathways, leading to neutrophil migration, degranulation, and the production of reactive oxygen species.

Clinical significance[edit]

Alterations in FPR1 function have been associated with a variety of diseases, including chronic granulomatous disease, asthma, and Alzheimer's disease. In addition, FPR1 has been implicated in the progression of certain types of cancer, as it can be exploited by cancer cells to promote their growth and survival.

See also[edit]

References[edit]

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