Protease-activated receptors: protease signaling in the gastrointestinal tract.
Serine proteases from the circulation, inflammatory cells, digestive glands and microorganisms can signal to cells by cleaving protease-activated receptors (PARs), a family of four G-protein-coupled receptors. Proteases cleave PARs at specific sites to expose tethered ligand domains that bind to and activate the cleaved receptors. Despite this irreversible mechanism of activation, PAR signaling is tightly regulated to prevent the uncontrolled stimulation of cells. Although PARs are found in all organ systems, protease signaling is of particular interest in the gastrointestinal tract, where proteases regulate neurotransmission, secretion, motility, epithelial permeability and intestinal inflammation, and can thus contribute to disease.
Amadesi
Silvia
S
University of California San Francisco, 521 Parnassus Avenue, Room C317, San Francisco, California 94143-0660, USA.
Bunnett
Nigel
N
D000818:Animals; D041981:Gastrointestinal Tract / Q000187:drug effects / Q000382:microbiology / Q000502:physiology*; D006801:Humans; D015212:Inflammatory Bowel Diseases / Q000378:metabolism / Q000503:physiopathology; D008954:Models, Biological; D044462:Receptors, Proteinase-Activated / Q000187:drug effects / Q000502:physiology*; D012697:Serine Endopeptidases / Q000494:pharmacology / Q000502:physiology*; D015398:Signal Transduction / Q000187:drug effects*
D044462:Receptors, Proteinase-Activated; D012697:Serine Endopeptidases