This basic science study identifies the primary structure of human preproendothelin, demonstrating that human endothelin is identical to porcine endothelin.
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Supports molecular studies of human endothelin; extends porcine homology data and leaves open clinical translation.
A cDNA encoding a human endothelium-derived vasoconstrictor peptide, endothelin, was isolated from a human placenta cDNA library. The nucleotide sequence of this cDNA clone showed that the primary structure of the human preproendothelin has 212 amino acid residues and is highly homologous to porcine preproendothelin, and that human endothelin is identical with porcine endothelin.
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Itoh et al. (1988) studied this question.
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