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- W2005484741 abstract "Abstract This study addresses the structural requirements for the intracellular processing and receptor binding properties of endothelin-1 (ET-1). Point mutants of preproendothelin-1 cDNA, with replacement of the codons for Lys 9 of ET-1 by ones for Ala and Glu and of Ile 20 and Trp 21 by ones encoding Ala, were expressed in COS-7 cells. Competitive binding experiments on rat vascular smooth muscle cells (A-10), which were shown to be an ET A receptor–rich cell line, between [ 125 I]ET-1 and synthetic ET-1, wild-type recombinant ET-1, and recombinant [Ala 9 ]ET-1, [Glu 9 ]ET-1, [Ala 20 ]ET-1, and [Ala 21 ]ET-1 yielded K i values of 0.2±0.02, 0.2±0.02, 0.04±0.01, 1.4±0.2, 1.6±0.2, and >50 nmol/L, respectively. In similar experiments with ET B receptor–rich human Girardi heart cells, the corresponding values were 0.2±0.03, 0.2±0.03, 0.2±0.04, 0.2±0.06, 1.4±0.4, and >50 nmol/L. The ET A receptor–mediated contractile responses to [Glu 9 ]ET-1 and [Ala 20 ]ET-1, measured by using canine coronary artery rings, were decreased approximately fourfold to fivefold compared with the response produced by synthetic or wild-type recombinant ET-1, whereas [Ala 9 ]ET-1 was found to be more potent, and [Ala 21 ]ET-1 did not produce any contraction. These results demonstrate that Ile 20 and Trp 21 are involved in binding to both receptor subtypes. Of considerable interest was the observation that [Glu 9 ]ET-1 also blunts the ET A receptor subtype–mediated contractile response to ET-1 stimulus." @default.
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- W2005484741 date "1995-12-01" @default.
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- W2005484741 title "Identification of Receptor Binding and Activation Sites in Endothelin-1 by Use of Site-Directed Mutagenesis" @default.
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- W2005484741 doi "https://doi.org/10.1161/01.res.77.6.1087" @default.
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