These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Endothelin receptor subtypes and stimulation of aldosterone secretion.
    Author: Gomez-Sanchez CE, Cozza EN, Foecking MF, Chiou S, Ferris MW.
    Journal: Hypertension; 1990 Jun; 15(6 Pt 2):744-7. PubMed ID: 2161792.
    Abstract:
    Endothelins (ETs) are 21-amino acid peptides with two disulfide bonds that have powerful vasoactive properties. We have previously shown the presence of a specific, high-affinity, saturable receptor for porcine or human endothelin (ET-1) in cultured calf zona glomerulosa cells. ET-1 was a stimulator of aldosterone secretion although not as powerful as angiotensin II. Incubations of cultured calf zona glomerulosa cells with Sarafotoxin S6b (S6b), a snake venom that has a structure highly homologous to ET-1, stimulated aldosterone secretion with a potency similar to that of ET-1. Binding of [125I]ET-1 to the adrenal receptor gave a Kd of 0.17 +/- 0.05 nM and a Bmax of 36 +/- 8.5 fmol/well (n = 4). Displacement of [125I]ET-1 by unlabeled ETs and S6b showed that the concentrations needed to displace 50% of the tracer were 0.3 nM for ET-1, 0.3 nM for ET-2, 10 nM for S6b, and 100 nM for ET-3. Binding of [125I]S6b to cultured adrenal cells revealed a receptor with a Kd of 0.05 +/- 0.01 nM and a Bmax of 8 +/- 2 fmol/well (n = 4). Displacement of [125I]S6b by unlabeled ETs and S6b showed that the concentrations needed to displace 50% of the tracer were 0.03 nM for S6b, 0.06 nM for ET-1, 0.04 nM for ET-2, and 0.05 nM for ET-3. Unlabeled ET-1 and ET-2 preferentially down-regulated the binding of [125I]ET-1, and S6b preferentially down-regulated the binding of [125I]S6b.(ABSTRACT TRUNCATED AT 250 WORDS)
    [Abstract] [Full Text] [Related] [New Search]