F2RL1

(redirected from proteinase-activated receptor-2)

F2RL1

A gene on chromosome 5q13 that encodes a widely expressed G protein-coupled receptor for trypsin and trypsin-like enzymes. F2RL1 helps recruit leukocytes to the sites of inflammation, and is the major protease-activated receptor (PAR) capable of modulating eosinophil function (e.g., proinflammatory cytokine secretion, superoxide production and degranulation). During inflammation, it promotes dendritic cell maturation, trafficking to the lymph nodes and subsequent T-cell activation. It is involved in antimicrobial response of innate immnune cells; activation enhances phagocytosis of gram-positive and killing of gram-negative bacteria. F2RL1 acts synergistically with IFN-gamma to enhance antiviral responses. It appears to play a role in inflammatory disorders of the joints, lungs, brain, GI tract, periodontium, skin and vascular systems, and in autoimmune disorders
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Molecular cloning, expression and potential functions of the human proteinase-activated receptor-2.
Cleavage and activation of proteinase-activated receptor-2 on human neutrophils by gingipain-R from Porphyromonas gingivalis.
Agonists of proteinase-activated receptor-2 modulate human neutrophil cytokine secretion, expression of cell adhesion molecules, and migration within 3-D collagen lattices.
Proinflammatory role of proteinase-activated receptor-2 in humans and mice during cutaneous inflammation in vivo .
Proteinase-activated receptor-2 in human skin: Tissue distribution and activation of keratinocytes by mast cell tryptase.
4),(9)-(11) Upregulated trypsin potentiates further viral multiplication in various organs and causes cellular dysfunction and fluid imbalance typically seen in the lungs through proteinase-activated receptor-2 (PAR-2) pathway.
2008) Induction of inflammatory cytokine release from human umbilical vein endothelial cells by agonists of proteinase-activated receptor-2.
Selective Tryptic Cleavage at the Tethered Ligand Site of the Amino Terminal Domain of Proteinase-Activated Receptor-2 in Intact Cells.
METHODS AND RESULTS: Using primary cultures of human respiratory epithelial (HRE) cells, we determined that these cells possess proteolytic signaling machinery, whereby proteinase-activated receptor-2 (PAR-2) activates [Ca.