| pubmed-article:8635215 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8635215 | lifeskim:mentions | umls-concept:C1257792 | lld:lifeskim |
| pubmed-article:8635215 | lifeskim:mentions | umls-concept:C0076552 | lld:lifeskim |
| pubmed-article:8635215 | lifeskim:mentions | umls-concept:C1257901 | lld:lifeskim |
| pubmed-article:8635215 | lifeskim:mentions | umls-concept:C0150312 | lld:lifeskim |
| pubmed-article:8635215 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:8635215 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8635215 | pubmed:dateCreated | 1996-7-11 | lld:pubmed |
| pubmed-article:8635215 | pubmed:abstractText | The thrombin receptor was the first cloned G protein-coupled receptor reported to be activated by proteolytic cleavage of its extracellular amino terminus. A second proteinase-activated receptor (PAR-2) was cloned recently and expressed in Xenopus laevis oocytes. PAR-2 was activated by trypsin and by a peptide (SLIGRL) derived from the new amino terminus. Since PAR-2 mRNA was detected in highly vascularized organs, we compared the physiological functions of the thrombin receptor and PAR-2 in vascular endothelium. Thrombin and trypsin both elicited endothelium-dependent relaxations in prostaglandin F2alpha (PGF2alpha)-contracted strips of porcine coronary artery. Whereas high doses of both thrombin or trypsin (10 U/mL) caused homologous desensitization, trypsin caused further relaxation of thrombin-desensitized tissues. Thrombin and PAR-2-derived peptides (SFLLRN and SLIGRL) both induced endothelium-dependent relaxations in PGF2alpha-contracted porcine coronary arteries. SFLLRN or SLIGRL (30 micronmol/L) also showed homologous desensitization but not cross desensitization. In the presence of the NO synthase inhibitor NG-monomethyl-L-arginine (1 mmol/L), both SFLLRN- and SLIGRL-induced relaxations were partially inhibited. SFLLRN elicited weak contraction in coronary arteries without endothelium, whereas SLIGRL had no effect. Intravenous injection of SFLLRN (1 mg/kg, bolus) into anesthetized rats elicited a transient depressor response followed by pronounced pressor response. In contrast, intravenous administration of SLIGRL (1 mg/kg, bolus) produced only a marked depressor response. Consistent with the in vivo data, SFLLRN contracted the endothelium-rubbed rat aortic rings and aggregated human platelets in vitro, whereas SLIGRL had no effect. The finding that both trypsin and SLIGRL induced endothelium-dependent relaxations indicates the presence of PAR-2 on endothelial cells. In addition, both trypsin and SLIGRL elicited relaxations in thrombin- or SFLLRN-desensitized tissue, suggesting that PAR-2 is distinct from thrombin receptor in vascular endothelium. The lack of PAR-2-mediated platelet aggregation or smooth muscle contraction suggested it might not share the pathogenic properties associated with the thrombin receptor in the vasculature. | lld:pubmed |
| pubmed-article:8635215 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8635215 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8635215 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8635215 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8635215 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8635215 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8635215 | pubmed:issn | 0009-7330 | lld:pubmed |
| pubmed-article:8635215 | pubmed:author | pubmed-author:WilliamsPP | lld:pubmed |
| pubmed-article:8635215 | pubmed:author | pubmed-author:ZhangRR | lld:pubmed |
| pubmed-article:8635215 | pubmed:author | pubmed-author:ChatterjeeMM | lld:pubmed |
| pubmed-article:8635215 | pubmed:author | pubmed-author:HwaJ JJJ | lld:pubmed |
| pubmed-article:8635215 | pubmed:author | pubmed-author:SybertzEE | lld:pubmed |
| pubmed-article:8635215 | pubmed:author | pubmed-author:ChintalaMM | lld:pubmed |
| pubmed-article:8635215 | pubmed:author | pubmed-author:GhibaudiLL | lld:pubmed |
| pubmed-article:8635215 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8635215 | pubmed:volume | 78 | lld:pubmed |
| pubmed-article:8635215 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8635215 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8635215 | pubmed:pagination | 581-8 | lld:pubmed |
| pubmed-article:8635215 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8635215 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8635215 | pubmed:articleTitle | Evidence for the presence of a proteinase-activated receptor distinct from the thrombin receptor in vascular endothelial cells. | lld:pubmed |
| pubmed-article:8635215 | pubmed:affiliation | Cardiovascular Pharmacology, Schering-Plough Research Institute, Kenilworth, NJ 07033-0530, USA. | lld:pubmed |
| pubmed-article:8635215 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8635215 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8635215 | pubmed:publicationType | In Vitro | lld:pubmed |
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