Endothelin-1 binding to endothelin receptors in the rat anterior pituitary gland: interaction in the recognition of endothelin-1 between ETA and ETB receptors.

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.

journal_name

Cell Mol Neurobiol

authors

Himeno A,Shigematsu K,Taguchi T,Niwa M

doi

10.1023/a:1022557717481

subject

Has Abstract

pub_date

1998-08-01 00:00:00

pages

447-52

issue

4

eissn

0272-4340

issn

1573-6830

journal_volume

18

pub_type

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