Abstract
Cultured aortic fibroblasts express high affinity Et-1 binding sites that poorly discriminate between Et-1 and Et-3. Both endothelins activate phospholipase C hence indicating the presence of ETB receptors. Fibroblasts respond to bradykinin by large activations of phospholipase C and increases in [Ca2+]i in a manner that was abolished by D-Arg, [Hyp3,Thi5,8,D-Phe7]-bradykinin, thus indicating the presence of B2 kinin receptors. Finally, ATP, UTP and ADP increases [Ca2+]i in aortic fibroblasts via a nucleotide receptor that has a higher affinity for ATP and UTP (3 microM) than for ADP (50 microM) and that is distinct from P2x and P2y purinoceptors.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Diphosphate / pharmacology*
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Adenosine Triphosphate / pharmacology*
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Animals
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Aorta, Thoracic / metabolism*
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Bradykinin / pharmacology*
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Calcium / metabolism*
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Cells, Cultured
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Endothelins / metabolism
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Endothelins / pharmacology*
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Fibroblasts / drug effects
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Fibroblasts / metabolism
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Kinetics
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Muscle, Smooth, Vascular / metabolism*
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Rats
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Rats, Inbred WKY
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Receptors, Endothelin / metabolism
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Type C Phospholipases / metabolism*
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Uridine Triphosphate / pharmacology*
Substances
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Endothelins
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Receptors, Endothelin
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Adenosine Diphosphate
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Adenosine Triphosphate
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Type C Phospholipases
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Bradykinin
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Calcium
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Uridine Triphosphate