Abstract
1. 125I-Endothelin (ET)-1 binding to the rat anterior pituitary gland was saturable and single, with a Kd of 71 pM and a Bmax of 120 fmol/mg. 2. When 1.0 microM BQ-123 (ETA antagonist) was added to the incubation buffer, the binding parameters were 8.3 pM and 8.0 fmol/mg, whereas 10 nM sarafotoxin S6c (ETB agonist) exerted little change in these binding parameters (Kd, 72 pM; Bmax, 110 fmol/mg). 3. ETB receptor-related compounds such as sarafotoxin S6c, ET-3, IRL1620, and BQ-788 competitively inhibited 125I-ET-1 binding, only when 1.0 microM BQ-123 was present in the incubation buffer. 4. Thus, the ETB receptor is capable of binding ET-1 when the ETA receptor is being occupied by BQ-123. A collaboration mechanism between the ETA and the ETB receptor may function in the recognition of ET-1, a typical "bivalent" ligand.