Agents and Actions

, Volume 40, Issue 3, pp 129–134

Guanine nucleotides and pertussis toxin reduce the affinity of histamine H3 receptors on AtT-20 cells

  • Mike A. Clark
  • Alexandra Korte
  • Robert W. Egan
Allergy and Histamine

DOI: 10.1007/BF01984051

Cite this article as:
Clark, M.A., Korte, A. & Egan, R.W. Agents and Actions (1993) 40: 129. doi:10.1007/BF01984051

Abstract

Agonist occupancy of high affinity histamine H3 receptors on AtT-20 cells induces increased ACTH release. However, the signal transduction process by which this occurs is presently unknown. As a first step in characterizing this pathway, we have examined the effects of a variety of nucleotides and nucleotide analogs on Na-methylhistamine binding to these receptors. Nonhydrolyzable guanine nucleotide analogs inhibit up to 40% of the [3H]Na-methylhistamine binding by increasing the dissociation rate of the ligand from the receptor and thereby, reducing receptor affinity. Pertussis toxin also decreases the affinity of the H3 receptors and ADP ribosylates a 41 kDa protein. Neither GTPγS nor pertussis toxin changeBmax. These data indicate that the H3 receptors on these cells are coupled to a G protein of the Gi subclass.

Copyright information

© Birkhäuser Verlag 1993

Authors and Affiliations

  • Mike A. Clark
    • 1
  • Alexandra Korte
    • 1
  • Robert W. Egan
    • 1
  1. 1.Schering Plough Research InstituteKenilworthUSA