Add time:08/06/2019         Source:sciencedirect.com

Endothelin-1-(1–31) is a new bioactive 31-amino-acid-length peptide generated from big endothelin-1 by chymase or other chymotrypsin-type proteases with various pathophysiologic functions. In this study, we have detected the specific and monophasic binding of [125I]endothelin-1-(1–31) in porcine lung membranes. Competition studies of [125I]endothelin-1-(1–31) binding by unlabeled endothelin-1-(1–31), endothelin-1, endothelin-3, and antagonists and agonists of endothelin ETA and ETB receptors suggest that the binding protein is an endothelin ETB or ETB-like receptor rather than an endothelin ETA receptor in porcine lungs. Kinetic studies showed that the affinity of endothelin-1-(1–31) to its receptor was approximately one order of magnitude lower than that of endothelin-1, and that the specific binding of endothelin-1-(1–31) was about 19% of endothelin-1 binding. The binding of [125I]endothelin-1-(1–31) was extremely slow, slower even than that of endothelin-1, and nearly irreversible. This unique quasi-irreversibility may explain the slow-onset and long-lasting biologic effects of this peptide in vivo.

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