pubmed-article:10781015 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10781015 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
pubmed-article:10781015 | lifeskim:mentions | umls-concept:C0205042 | lld:lifeskim |
pubmed-article:10781015 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:10781015 | lifeskim:mentions | umls-concept:C0040018 | lld:lifeskim |
pubmed-article:10781015 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:10781015 | lifeskim:mentions | umls-concept:C0019409 | lld:lifeskim |
pubmed-article:10781015 | lifeskim:mentions | umls-concept:C0035028 | lld:lifeskim |
pubmed-article:10781015 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:10781015 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:10781015 | pubmed:dateCreated | 2000-6-27 | lld:pubmed |
pubmed-article:10781015 | pubmed:abstractText | 1. Mechanisms of protease-activated receptor-1 (PAR1)- and PAR2-induced relaxation were investigated in pre-contracted porcine coronary artery ring preparations. 2. Thrombin (0.01 - 0.3 u ml(-1)) and the PAR1-activating peptide SFLLRN (0.1 - 10 microM) caused concentration- and endothelium-dependent relaxation. pEC(50)s (-log u ml(-1) for enzymes, -log M for peptides) and maximum relaxations (R(max), %) for thrombin were 1.8+/-0.1 and 93.5+/-2.8% respectively, and for SFLLRN 6.8+/-0.1 and 90.8+/-1.3%. Similar concentration- and endothelium-dependent relaxations occurred with trypsin (pEC(50) 2.3+/-0.2; R(max) 94.1+/-1.9%) and the PAR2-activating peptide SLIGRL (pEC(50) 6.5+/-0.2; R(max) 92.4+/-1.6%). 3. Relaxations to thrombin, SFLLRN, trypsin and SLIGRL were significantly inhibited (P<0.05) to similar extents by the nitric oxide (NO) synthase inhibitor N(G)-nitro-L-arginine (L-NOARG; 100 microM) and the NO scavenger oxyhaemoglobin (20 microM), both separately and in combination. 4. In the presence of the L-type voltage-operated calcium channel (L-VOCC) inhibitor nifedipine (0.3 microM), K(+) (67 mM) abolished the L-NOARG-resistant relaxations to thrombin, SFLLRN, trypsin and SLIGRL. However, nifedipine alone significantly (P<0.05) reduced the pEC(50) (1.5+/-0.1) and R(max) (77.5+/-7.0%) for thrombin but had no effect on relaxations to SFLLRN, trypsin or SLIGRL. Furthermore, L-NOARG-resistant relaxations to thrombin were abolished by nifedipine, whereas relaxations to SFLLRN, trypsin or SLIGRL were not further inhibited by combined treatment with nifedipine and L-NOARG, than they were with L-NOARG treatment alone. 5. Similar selective inhibition of the L-NOARG-resistant relaxation to thrombin, but not SFLLRN, occurred with verapamil (1 microM) and diltiazem (3 microM). 6. Our results suggest heterogeneous mechanisms in the NO-independent relaxation to thrombin and peptide activators of PAR1 in the porcine coronary artery. | lld:pubmed |
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pubmed-article:10781015 | pubmed:language | eng | lld:pubmed |
pubmed-article:10781015 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10781015 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10781015 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10781015 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10781015 | pubmed:month | May | lld:pubmed |
pubmed-article:10781015 | pubmed:issn | 0007-1188 | lld:pubmed |
pubmed-article:10781015 | pubmed:author | pubmed-author:HamiltonJ RJR | lld:pubmed |
pubmed-article:10781015 | pubmed:author | pubmed-author:CocksT MTM | lld:pubmed |
pubmed-article:10781015 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10781015 | pubmed:volume | 130 | lld:pubmed |
pubmed-article:10781015 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10781015 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10781015 | pubmed:pagination | 181-8 | lld:pubmed |
pubmed-article:10781015 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:10781015 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10781015 | pubmed:articleTitle | Heterogeneous mechanisms of endothelium-dependent relaxation for thrombin and peptide activators of protease-activated receptor-1 in porcine isolated coronary artery. | lld:pubmed |
pubmed-article:10781015 | pubmed:affiliation | Department of Pharmacology, University of Melbourne, Victoria 3010, Australia. | lld:pubmed |
pubmed-article:10781015 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10781015 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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