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Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader
Published on: May 24, 2024
Protease-activated receptor 2 signaling in inflammation
Andrea S Rothmeier1, Wolfram Ruf
1Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA.
Seminars in Immunopathology
|October 6, 2011
Summary
Protease-activated receptor 2 (PAR2) acts as a sensor for proteases, regulating key functions like inflammation and immunity. This review highlights PAR2
Area of Science:
- Biochemistry
- Cell Biology
- Physiology
Background:
- Protease-activated receptors (PARs) are G protein-coupled receptors activated by protease cleavage.
- PARs function as critical sensors for extracellular proteases in various physiological processes.
Purpose of the Study:
- To review the diverse roles of PAR2 beyond hemostasis.
- To emphasize the involvement of coagulation and other protease pathways in PAR2-mediated functions.
Main Methods:
- Review of existing literature on PAR2.
- Analysis of studies using PAR2-specific agonists/antagonists and knockout models.
Main Results:
- PAR2 is activated by numerous serine proteases in both vascular and extravascular locations.
- PAR2 plays critical roles in development, inflammation, immunity, and angiogenesis.
- Coagulation proteases and other extracellular proteases cleave PAR2 in various cell types.
Conclusions:
- PAR2 is a versatile receptor involved in numerous physiological and pathophysiological processes.
- Extracellular proteases, including coagulation factors, significantly influence PAR2 activity and downstream signaling.
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