Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-2-17
pubmed:abstractText
Trypsin and mast cell tryptase cleave proteinase-activated receptor 2 and, by unknown mechanisms, induce widespread inflammation. We found that a large proportion of primary spinal afferent neurons, which express proteinase-activated receptor 2, also contain the proinflammatory neuropeptides calcitonin gene-related peptide and substance P. Trypsin and tryptase directly signal to neurons to stimulate release of these neuropeptides, which mediate inflammatory edema induced by agonists of proteinase-activated receptor 2. This new mechanism of protease-induced neurogenic inflammation may contribute to the proinflammatory effects of mast cells in human disease. Thus, tryptase inhibitors and antagonists of proteinase-activated receptor 2 may be useful anti-inflammatory agents.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcitonin Gene-Related Peptide, http://linkedlifedata.com/resource/pubmed/chemical/Chymases, http://linkedlifedata.com/resource/pubmed/chemical/DNA Probes, http://linkedlifedata.com/resource/pubmed/chemical/Mcpt6 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, PAR-2, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thrombin, http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Substance P, http://linkedlifedata.com/resource/pubmed/chemical/TPSB1 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Trypsin, http://linkedlifedata.com/resource/pubmed/chemical/Tryptases, http://linkedlifedata.com/resource/pubmed/chemical/chymase 2
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1078-8956
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
151-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10655102-Animals, pubmed-meshheading:10655102-Base Sequence, pubmed-meshheading:10655102-Calcitonin Gene-Related Peptide, pubmed-meshheading:10655102-Chymases, pubmed-meshheading:10655102-DNA Probes, pubmed-meshheading:10655102-Ganglia, Spinal, pubmed-meshheading:10655102-Humans, pubmed-meshheading:10655102-In Situ Hybridization, pubmed-meshheading:10655102-Inflammation, pubmed-meshheading:10655102-Male, pubmed-meshheading:10655102-Neurons, pubmed-meshheading:10655102-Rats, pubmed-meshheading:10655102-Rats, Sprague-Dawley, pubmed-meshheading:10655102-Rats, Wistar, pubmed-meshheading:10655102-Receptor, PAR-2, pubmed-meshheading:10655102-Receptors, Thrombin, pubmed-meshheading:10655102-Serine Endopeptidases, pubmed-meshheading:10655102-Signal Transduction, pubmed-meshheading:10655102-Substance P, pubmed-meshheading:10655102-Trypsin, pubmed-meshheading:10655102-Tryptases
pubmed:year
2000
pubmed:articleTitle
Agonists of proteinase-activated receptor 2 induce inflammation by a neurogenic mechanism.
pubmed:affiliation
Department of Surgery and Physiology, University of California, San Francisco, CA 94143, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't