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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1992-5-12
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pubmed:abstractText |
To characterize the properties and the distribution of endothelin (ET) receptor subtypes, we have examined the ligand selectivity and the molecular weight (Mr) of [125I]ET-1 and [125I]ET-3 binding sites in various tissues of human and pigs. ET-1 and ET-2 showed almost identical potencies in displacing the bound [125I]ET-1 in all of the tissues examined. ET-3, sarafotoxin S6b (SRTX-b), and sarafotoxin S6C (SRTX-c) displaced the [125I]ET-1 with nearly the same sensitivity as ET-1 (IC50 = 0.07-3.0 nM) in brain, kidney, liver, and adrenal, whereas the three peptides showed very weak competition (IC50 = 40-500 nM) against [125I]ET-1 binding in atria, aorta, lung, stomach, and uterus. The Bmax value for [125I]ET-3 was 83% of that for [125I]ET-1 in human liver membranes, whereas the Bmax for [125I]ET-3 was only 12% of that for [125I]ET-1 in human atrial membranes. [125I]ET-3 bound to liver and atrial membranes was displaced by ET/SRTX isopeptides almost equipotently. Two proteins with Mr of 110 and 50 kDa were specifically affinity-labeled with [125I]ET-1 in porcine lung membranes. The above findings indicated that two distinct subclasses of ET receptors, namely ET-1/ET-2-specific and ET/SRT family common receptors, were distributed in various proportions in mammalian tissues.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Affinity Labels,
http://linkedlifedata.com/resource/pubmed/chemical/Endothelins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Endothelin,
http://linkedlifedata.com/resource/pubmed/chemical/Viper Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/sarafotoxins s6
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pubmed:status |
MEDLINE
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pubmed:issn |
0160-2446
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
17 Suppl 7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
S127-30
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1725306-Affinity Labels,
pubmed-meshheading:1725306-Animals,
pubmed-meshheading:1725306-Binding, Competitive,
pubmed-meshheading:1725306-Endothelins,
pubmed-meshheading:1725306-Humans,
pubmed-meshheading:1725306-Kinetics,
pubmed-meshheading:1725306-Ligands,
pubmed-meshheading:1725306-Molecular Weight,
pubmed-meshheading:1725306-Protein Binding,
pubmed-meshheading:1725306-Receptors, Cell Surface,
pubmed-meshheading:1725306-Receptors, Endothelin,
pubmed-meshheading:1725306-Swine,
pubmed-meshheading:1725306-Tissue Distribution,
pubmed-meshheading:1725306-Viper Venoms
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pubmed:year |
1991
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pubmed:articleTitle |
Multiple subtypes of endothelin receptors in human and porcine tissues: characterization by ligand binding, affinity labeling, and regional distribution.
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pubmed:affiliation |
Third Department of Internal Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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