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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1989-10-20
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pubmed:abstractText |
Functional receptors for the peptides of the endothelin (ET) and sarafotoxin (SRTX) family were characterized in newborn rat heart myocytes using human and rat endothelins (ET-1 and ET-3, respectively), SRTX-b and SRTX-c. Binding studies in intact cells and homogenates revealed significantly higher affinities of ET-1 and SRTX-b than of ET-3 and SRTX-c towards these receptors. This binding profile of ET/SRTX peptides points to their interaction with the receptor subtype designated E-S alpha. All four peptides induced time- and dose-dependent phosphoinositide hydrolysis with the following rank order of potency: ET-1 greater than SRTX-b greater than SRTX-c greater than ET-3. Thus, ET-3 which possesses an intermediate affinity toward the receptor was the least effective with regard to this response. These results confirm and extend our earlier report that the ET/SRTX peptides interact with a newly characterized receptor(s) associated with phosphoinositide metabolism and Ca2+ mobilization. The initiation of inositol phosphate formation is largely independent of extracellular Ca2+, verapamil and nifedipine, indicating that the ET/SRTX peptides are not agonists for the voltage-dependent Ca2+-channels.
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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/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Endothelins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cholinergic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Endothelin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide,
http://linkedlifedata.com/resource/pubmed/chemical/Viper Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/sarafotoxin receptor,
http://linkedlifedata.com/resource/pubmed/chemical/sarafotoxins s6
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
163
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
936-43
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:2551278-Animals,
pubmed-meshheading:2551278-Calcium,
pubmed-meshheading:2551278-Endothelins,
pubmed-meshheading:2551278-Endothelium, Vascular,
pubmed-meshheading:2551278-Humans,
pubmed-meshheading:2551278-Myocardium,
pubmed-meshheading:2551278-Peptides,
pubmed-meshheading:2551278-Rats,
pubmed-meshheading:2551278-Receptors, Cell Surface,
pubmed-meshheading:2551278-Receptors, Cholinergic,
pubmed-meshheading:2551278-Receptors, Endothelin,
pubmed-meshheading:2551278-Receptors, Peptide,
pubmed-meshheading:2551278-Structure-Activity Relationship,
pubmed-meshheading:2551278-Viper Venoms
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pubmed:year |
1989
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pubmed:articleTitle |
Functional endothelin/sarafotoxin receptors in rat heart myocytes: structure-activity relationships and receptor subtypes.
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pubmed:affiliation |
Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel.
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pubmed:publicationType |
Journal Article
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