Article: Full-length article Endothelium-derived hyperpolarizing factor mediated relaxations in pig coronary arteries do not involve Gi/o proteins
| Title | Full-length article Endothelium-derived hyperpolarizing factor mediated relaxations in pig coronary arteries do not involve Gi/o proteins | ||||
|---|---|---|---|---|---|
| Authors | Ng, KFJ1 Leung, SWS1 Man, RYK1 Vanhoutte, PM1 | ||||
| Keywords | Endothelium-derived hyperpolarizing factor Gi/o protein Pertussis toxin Pig coronary artery | ||||
| Issue Date | 2008 | ||||
| Publisher | Nature Publishing Group. The Journal's web site is located at http://www.nature.com/aps/index.html | ||||
| Citation | Acta Pharmacologica Sinica, 2008, v. 29 n. 12, p. 1419-1424 [How to Cite?] DOI: http://dx.doi.org/10.1111/j.1745-7254.2008.00905.x | ||||
| Abstract | Aim: Endothelium-dependent relaxations to certain neurohumoral substances are mediated by pertussis toxin-sensitive Gi/o protein. Our experiments were designed to determine the role, if any, of pertussis toxin-sensitive G-proteins in relaxations attributed to endothelium-derived hyperpolarizing factor (EDHF). Methods: Pig coronary arterial rings with endothelia were suspended in organ chambers flled with Krebs-Ringer bicarbonate solution maintained at 37 °C and continuously aerated with 95%O2 and 5% CO2. Isometric tension was measured during contractions to prostaglandin F2α in the presence of indomethacin and NΩnitro-L-arginine methyl ester (L-NAME). Results: Thrombin, the thrombin receptor-activating peptide SFLLRN, bradykinin, substance P, and calcimycin produced dose-dependent relaxations. These relaxations were not inhibited by prior incubation with pertussis toxin, but were abolished upon the addition of charybdotoxin plus apamin. Relaxations to the α2-adrenergic agonist UK14304 and those to serotonin were abolished in the presence of indomethacin and L-NAME. Conclusion: Unlike nitric oxide-mediated relaxations, EDHF-mediated relaxations of pig coronary arteries do not involve pertussis toxin-sensitive pathways and are Gi/o protein independent. | ||||
| ISSN | 1671-4083 2011 Impact Factor: 1.953 2011 SCImago Journal Rankings: 0.136 | ||||
| DOI | http://dx.doi.org/10.1111/j.1745-7254.2008.00905.x | ||||
| ISI Accession Number ID | WOS:000261710300003
Funding Information: This study is supported in part by a CRCG grant from the University of Hong Kong (No 21374077) and in part by departmental funds. | ||||
| References | References in Scopus |
| dc.contributor.author | Ng, KFJ | ||||
|---|---|---|---|---|---|
| dc.contributor.author | Leung, SWS | ||||
| dc.contributor.author | Man, RYK | ||||
| dc.contributor.author | Vanhoutte, PM | ||||
| dc.date.accessioned | 2010-09-06T05:53:41Z | ||||
| dc.date.available | 2010-09-06T05:53:41Z | ||||
| dc.date.issued | 2008 | ||||
| dc.description.abstract | Aim: Endothelium-dependent relaxations to certain neurohumoral substances are mediated by pertussis toxin-sensitive Gi/o protein. Our experiments were designed to determine the role, if any, of pertussis toxin-sensitive G-proteins in relaxations attributed to endothelium-derived hyperpolarizing factor (EDHF). Methods: Pig coronary arterial rings with endothelia were suspended in organ chambers flled with Krebs-Ringer bicarbonate solution maintained at 37 °C and continuously aerated with 95%O2 and 5% CO2. Isometric tension was measured during contractions to prostaglandin F2α in the presence of indomethacin and NΩnitro-L-arginine methyl ester (L-NAME). Results: Thrombin, the thrombin receptor-activating peptide SFLLRN, bradykinin, substance P, and calcimycin produced dose-dependent relaxations. These relaxations were not inhibited by prior incubation with pertussis toxin, but were abolished upon the addition of charybdotoxin plus apamin. Relaxations to the α2-adrenergic agonist UK14304 and those to serotonin were abolished in the presence of indomethacin and L-NAME. Conclusion: Unlike nitric oxide-mediated relaxations, EDHF-mediated relaxations of pig coronary arteries do not involve pertussis toxin-sensitive pathways and are Gi/o protein independent. | ||||
| dc.description.nature | Link_to_subscribed_fulltext | ||||
| dc.identifier.citation | Acta Pharmacologica Sinica, 2008, v. 29 n. 12, p. 1419-1424 [How to Cite?] DOI: http://dx.doi.org/10.1111/j.1745-7254.2008.00905.x | ||||
| dc.identifier.citeulike | 3804483 | ||||
| dc.identifier.doi | http://dx.doi.org/10.1111/j.1745-7254.2008.00905.x | ||||
| dc.identifier.epage | 1424 | ||||
| dc.identifier.hkuros | 168517 | ||||
| dc.identifier.isi | WOS:000261710300003
Funding Information: This study is supported in part by a CRCG grant from the University of Hong Kong (No 21374077) and in part by departmental funds. | ||||
| dc.identifier.issn | 1671-4083 2011 Impact Factor: 1.953 2011 SCImago Journal Rankings: 0.136 | ||||
| dc.identifier.issue | 12 | ||||
| dc.identifier.openurl | ![]() | ||||
| dc.identifier.pmid | 19026160 | ||||
| dc.identifier.scopus | eid_2-s2.0-64549097688 | ||||
| dc.identifier.spage | 1419 | ||||
| dc.identifier.uri | http://hdl.handle.net/10722/67291 | ||||
| dc.identifier.volume | 29 | ||||
| dc.language | eng | ||||
| dc.publisher | Nature Publishing Group. The Journal's web site is located at http://www.nature.com/aps/index.html | ||||
| dc.publisher.place | United States | ||||
| dc.relation.ispartof | Acta Pharmacologica Sinica | ||||
| dc.relation.references | References in Scopus | ||||
| dc.subject.mesh | Biological Factors - pharmacology | ||||
| dc.subject.mesh | Coronary Vessels - drug effects - physiology | ||||
| dc.subject.mesh | Endothelium-Dependent Relaxing Factors - pharmacology | ||||
| dc.subject.mesh | GTP-Binding Protein alpha Subunits, Gi-Go - metabolism | ||||
| dc.subject.mesh | Muscle Relaxation - drug effects | ||||
| dc.subject | Endothelium-derived hyperpolarizing factor | ||||
| dc.subject | Gi/o protein | ||||
| dc.subject | Pertussis toxin | ||||
| dc.subject | Pig coronary artery | ||||
| dc.title | Full-length article Endothelium-derived hyperpolarizing factor mediated relaxations in pig coronary arteries do not involve Gi/o proteins | ||||
| dc.type | Article |
Author Affiliations
- The University of Hong Kong


