Source:http://linkedlifedata.com/resource/pubmed/id/10945858
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
2000-9-12
|
pubmed:abstractText |
Endothelin (ET)-1 is a potent positive inotropic agent, the effects of which are mediated by increases in cytosolic Ca(2+) in the myocardium. The object of this study was to examine 1) the influence of ET(A) and ET(B) receptor subtypes, and 2) the role of the phospholipase C (PLC) pathway in mediating ET-1-induced contraction. Left ventricular cardiomyocytes were isolated from the hearts of New Zealand White rabbits (2-2.5 kg) by the use of Langendorff perfusion with collagenase. Cardiomyocyte function was examined during unloaded, electrically stimulated (0.5 Hz) contractions with a video-edge detection system. ET-1 increased cell shortening with greater potency than ET-3: mean EC(50) values were 1.1 x 10(-11) and 2.6 x 10(-10) M, respectively. With the same order of potency, ET-1 and ET-3 increased (P <.05) velocity of cell shortening. The ET(A) receptor-selective antagonist ABT-627 shifted the ET-1-induced cell shortening response curve to the right with a pA(2) value of 10.3. The ET(B) receptor-selective antagonist A-192621 (10(-8)-10(-7) M) did not alter the concentration-response of ET-1. Moreover, the ET(B) receptor-selective agonist sarafotoxin 6c did not have any effect on cell shortening over the concentration range of 10(-11) to 10(-7) M. ET-1 in the presence of the PLC inhibitor U-73122 did not alter the contractile amplitude. However, ET-1 in the presence of the protein kinase C inhibitor bisindolylmalemide increased cell shortening. These findings indicate that 1) the ET(A) receptor subtype, and not the ET(B) receptor subtype, mediates the positive inotropic effect of ET-1, and 2) the response of ET-1 is mediated by a PLC pathway, but not through protein kinase C, in ventricular cardiomyocytes isolated from rabbit myocardium.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endothelin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Endothelin-3,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Endothelin A,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Endothelin B,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Endothelin,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Viper Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/sarafotoxins s6
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0022-3565
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
294
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1047-52
|
pubmed:dateRevised |
2008-11-21
|
pubmed:meshHeading |
pubmed-meshheading:10945858-Animals,
pubmed-meshheading:10945858-Endothelin-1,
pubmed-meshheading:10945858-Endothelin-3,
pubmed-meshheading:10945858-Enzyme Inhibitors,
pubmed-meshheading:10945858-Heart Ventricles,
pubmed-meshheading:10945858-Male,
pubmed-meshheading:10945858-Myocardial Contraction,
pubmed-meshheading:10945858-Myocardium,
pubmed-meshheading:10945858-Protein Kinase C,
pubmed-meshheading:10945858-Rabbits,
pubmed-meshheading:10945858-Receptor, Endothelin A,
pubmed-meshheading:10945858-Receptor, Endothelin B,
pubmed-meshheading:10945858-Receptors, Endothelin,
pubmed-meshheading:10945858-Signal Transduction,
pubmed-meshheading:10945858-Type C Phospholipases,
pubmed-meshheading:10945858-Ventricular Function,
pubmed-meshheading:10945858-Viper Venoms
|
pubmed:year |
2000
|
pubmed:articleTitle |
Endothelin(A) receptor subtype mediates endothelin-induced contractility in left ventricular cardiomyocytes isolated from rabbit myocardium.
|
pubmed:affiliation |
Cardiovascular Pharmacology Group, Centre for Cardiovascular Research, School of Medicine, The Queen's University of Belfast, Northern Ireland, United Kingdom. e.kelso@qub.ac.uk
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|