Protease-activated receptors: How proteases signal to cells

Fabien Schmidlin, Nigel W. Bunnett

Research output: Contribution to journalReview articlepeer-review


Certain proteases from the circulation, mast cells and elsewhere signal directly to cells by cleaving protease-activated receptors (PARs), members of a new subfamily of G-protein-coupled receptor. Cleavage exposes a tethered ligand domain that binds to and activates the cleaved receptors. Advances in the past year have improved our understanding of the molecular mechanisms of this signaling and how it is switched off. It is now recognized that PARs play important roles in 'emergency situations' - such as trauma, when there is generation or release of proteases - and are involved in coagulation, inflammation, pain, healing and protection. Selective antagonists or agonists of these receptors may be useful therapeutic agents for the treatment of human diseases.

Original languageEnglish (US)
Pages (from-to)575-582
Number of pages8
JournalCurrent Opinion in Pharmacology
Issue number6
StatePublished - Dec 1 2001


  • Inflammation
  • Molecular Medicine
  • Pharmacology
  • Protease-activated receptors
  • Proteases
  • Thrombin
  • Trypsin
  • Tryptase

ASJC Scopus subject areas

  • Pharmacology
  • Drug Discovery


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