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 ET b receptors. Fibroblasts respond to bradykinin by large activations of phospholipase C and increases in [Ca 2+]i in a manner that was abolished by D-Arg, [Hyp 3,Thi 5,8,D-Phe 7]-bradykinin, thus indicating the presence of 132 kinin receptors. Finally, ATP, UTP and ADP increases [Ca 2+]i in aortic fibroblasts via a nucleotide receptor that has a higher affinity for ATP and UTP (3 μM) than for ADP (50 μM) and that is distinct from P2x and P2y purinoceptors.

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