Interaction of GRF with VIP receptors and stimulation of adenylate cyclase in rat and human intestinal epithelial membranes. Comparison with PHI and secretin

FEBS Lett. 1983 Aug 8;159(1-2):89-92. doi: 10.1016/0014-5793(83)80422-0.


GRF (10(-8) - 10(-5) M) is shown to inhibit competitively the binding of [125I]VIP to human and rat intestinal epithelial membranes. The affinity of GRF for VIP receptor is 700-800-times lower than that of VIP in both species. The order of affinity of different peptides is VIP greater than PHI greater than secretin greater than GRF in rat, and VIP greater than GRF greater than PHI greater than secretin in man. The important species specificity of VIP receptors in recognizing PHI and secretin does not occur in the case of GRF. GRF stimulates adenylate cyclase through its interaction with VIP receptors in rat and human membranes. However, while GRF behaves as a VIP agonist in human tissue, it is a partial agonist/antagonist of VIP in the rat.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenylyl Cyclases / metabolism*
  • Animals
  • Binding, Competitive
  • Cell Membrane / metabolism
  • Epithelium / enzymology
  • Growth Hormone-Releasing Hormone / metabolism*
  • Humans
  • Intestines / enzymology*
  • Peptide PHI
  • Peptides / metabolism*
  • Rats
  • Receptors, Cell Surface / metabolism*
  • Receptors, Vasoactive Intestinal Peptide
  • Secretin / metabolism*


  • Peptide PHI
  • Peptides
  • Receptors, Cell Surface
  • Receptors, Vasoactive Intestinal Peptide
  • Secretin
  • Growth Hormone-Releasing Hormone
  • Adenylyl Cyclases