G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides

Trends Pharmacol Sci. 1990 Sep;11(9):358-62. doi: 10.1016/0165-6147(90)90179-c.

Abstract

The neuropeptide substance P, the venom peptide mastoparan and the synthetic polyamine compound 48/80 activate rat peritoneal mast cells, leading to rapid histamine release by exocytosis. Although these effects are inhibited by pertussis toxin and involve a transient increase in IP3, no selective membrane receptors have been identified. However, it has recently been shown that these compounds activate G proteins in vitro. Here Yves Landry and colleagues discuss the proposal that direct activation of G protein is the physiological mechanism of action of substance P on rat peritoneal mast cells, this mechanism being mimicked by mastoparan and 48/80, and possibly by other cationic amphiphilic peptides such as kinins. These compounds might be of help in defining the interaction between membrane receptors and G proteins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biotransformation
  • GTP-Binding Proteins / metabolism*
  • Humans
  • Intercellular Signaling Peptides and Proteins
  • Molecular Sequence Data
  • Neuropeptides / chemistry
  • Neuropeptides / pharmacology*
  • Peptides
  • Wasp Venoms / chemistry
  • Wasp Venoms / pharmacology*

Substances

  • Intercellular Signaling Peptides and Proteins
  • Neuropeptides
  • Peptides
  • Wasp Venoms
  • mastoparan
  • GTP-Binding Proteins