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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1992-5-12
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pubmed:abstractText |
Endothelins (ETs) are a family of vasoactive peptides with profound biological actions in diverse cell systems. Among its varied actions, ET stimulates phospholipase C (PLC) in cultured mesangial cells. We investigated the presence of specific ET receptors in rat mesangial cells in culture, and studied the role of GTP-binding proteins (G proteins) in coupling PLC to the endothelin receptor. [125I]ET binding was time- and temperature-dependent, and Scatchard analysis of saturation data showed a single class of high-affinity binding sites. Heterologous displacement with two related peptides, ET-3 and sarafotoxin (SFTX), revealed the presence of two binding sites for these isopeptides. Preincubation of cells with ET-1 reduced the receptor number without affecting Kd, and this effect was not prevented by protein kinase C inhibition or downregulation. We confirmed the presence of a 41- to 43-kDa pertussis toxin substrate in rat mesangial cell membranes in an ADP ribosylation assay. ET-1 inhibits and GDP beta S enhances toxin-catalyzed transfer of ADP-ribose to this substrate. ET-1 potentiated GTP gamma S-induced phosphatidylinositol (PI) hydrolysis in a concentration-dependent manner. In addition, pertussis toxin partially inhibited ET-stimulated PI hydrolysis in intact mesangial cells. Pertussis toxin also reduced the magnitude of ET-stimulated intracellular free calcium [( Ca2+ )i]. Thus, ET-1 binds to specific receptors on rat mesangial cells and activates PLC, in part, through a pertussis toxin-sensitive G-protein.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Endothelins,
http://linkedlifedata.com/resource/pubmed/chemical/Fura-2,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate),
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Endothelin,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella
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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 |
S79-84
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1725439-Adenosine Diphosphate Ribose,
pubmed-meshheading:1725439-Animals,
pubmed-meshheading:1725439-Endothelins,
pubmed-meshheading:1725439-Enzyme Activation,
pubmed-meshheading:1725439-Fura-2,
pubmed-meshheading:1725439-GTP-Binding Proteins,
pubmed-meshheading:1725439-Glomerular Mesangium,
pubmed-meshheading:1725439-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:1725439-Kinetics,
pubmed-meshheading:1725439-Pertussis Toxin,
pubmed-meshheading:1725439-Rats,
pubmed-meshheading:1725439-Rats, Inbred Strains,
pubmed-meshheading:1725439-Receptors, Cell Surface,
pubmed-meshheading:1725439-Receptors, Endothelin,
pubmed-meshheading:1725439-Temperature,
pubmed-meshheading:1725439-Type C Phospholipases,
pubmed-meshheading:1725439-Virulence Factors, Bordetella
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pubmed:year |
1991
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pubmed:articleTitle |
Endothelin receptors and coupled GTP-binding proteins in glomerular mesangial cells.
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pubmed:affiliation |
Department of Medicine, Case Western Reserve University, Cleveland, Ohio.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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