Evidence that helodermin, a newly extracted peptide from Gila monster venom, is a member of the secretin/VIP/PHI family of peptides with an original pattern of biological properties

FEBS Lett. 1984 Jan 30;166(2):277-82. doi: 10.1016/0014-5793(84)80095-2.

Abstract

Helodermin, a newly isolated peptide from the venom of Gila monster (Heloderma suspectum) was shown to stimulate the adenylate cyclase activity of rat pancreatic membranes as efficiently as secretin and VIP. It also increased cyclic AMP levels and inhibited [125I]VIP binding in rat pancreatic acini. Finally, helodermin activated adenylate cyclase in membranes from rat heart, rat brain, and human heart, showing properties analogous yet distinct from those of secretin, VIP and PHI.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenylyl Cyclases / metabolism
  • Animals
  • Biological Assay
  • Cell Membrane / enzymology
  • Cyclic AMP / metabolism
  • Enzyme Activation
  • Intercellular Signaling Peptides and Proteins
  • Kinetics
  • Lizards
  • Pancreas / metabolism
  • Peptides / pharmacology*
  • Rats
  • Secretin / pharmacology*
  • Vasoactive Intestinal Peptide / pharmacology*
  • Venoms / pharmacology*

Substances

  • Intercellular Signaling Peptides and Proteins
  • Peptides
  • Venoms
  • Secretin
  • Vasoactive Intestinal Peptide
  • heliodermin
  • Cyclic AMP
  • Adenylyl Cyclases