The receptors for endothelins and their analogues in SK-N-MC neuroblastoma cells.

The potency order of peptides to inhibit [125I]endothelin-1 binding and to stimulate phosphatidylinositol phosphate (PtdInsP) turnover in SK-N-MC cells was consistent with the presence of ETA-endothelin receptors. Divalent cations enhanced [125I]endothelin-1 binding by, in the case of Mn2+, increasing radioligand affinity. Mn2+ did not induce conformational changes in endothelin-1, and its effect was maintained in solubilized receptors. Hence, metal ions may directly interact with endothelin receptors. The effects of BQ-123 and [Ala1,3,11,15]endothelin-1 on PtdInsP turnover were investigated. Concentration-response curves of endothelins were modeled by a second-order equation that assumes pseudoirreversible ligand binding.