Reverse intrinsic activity of antagonists on G protein-coupled receptors

Trends Pharmacol Sci. 1992 Oct;13(10):376-80. doi: 10.1016/0165-6147(92)90116-n.

Abstract

Biological effects observed with an antagonist are usually interpreted as the result of its ability to block receptor activation produced by an endogenous agonist. In this Principles article, Wolfgang Schütz and Michael Freissmuth show how considerable evidence has now been accumulated for G protein-coupled receptors that antagonists not only bind to the receptor, but also induce a conformational change that favours uncoupling of the receptor from its G protein. The spontaneous activity of the unliganded receptor (i.e. the receptor not occupied by any ligand) is a well-established phenomenon in reconstituted systems with purified components. However, its physiological relevance needs to be verified in a more physiological environment before biological effect of antagonists can be primarily ascribed to negative intrinsic activity.

Publication types

  • Review

MeSH terms

  • Animals
  • GTP Phosphohydrolases / metabolism
  • GTP-Binding Proteins / metabolism*
  • Guanosine Triphosphate / metabolism
  • Humans
  • Receptors, Cell Surface / antagonists & inhibitors*
  • Receptors, Cell Surface / metabolism
  • Signal Transduction
  • Uncoupling Agents / pharmacology*

Substances

  • Receptors, Cell Surface
  • Uncoupling Agents
  • Guanosine Triphosphate
  • GTP Phosphohydrolases
  • GTP-Binding Proteins