The effect of helodermin in rat dispersed pancreatic acini

Junya Kashimura, Tooru Shimosegawa, Tohru Mochizuki, Noboru Yanaihara, Masaru Koizumi, Takayoshi Toyota

Research output: Contribution to journalArticlepeer-review


Helodermin is a 35 amino acid-residue peptide of the vasoactive intestinal polypeptide (VIP) family, which was originally isolated from the venom of Helo-derma suspectum on the basis of its capacity to stimulate adenylate cyclase in the rat pancreas. In the present study, using rat dispersed pancreatic acini, we examined the binding characteristics of helodermin, its action on amylase secretion, and the production of intracellular cyclic AMP (cAMP). Helodermin stimulated intracellular cAMP production dose dependently in a manner that was nearly identical to that of VIP. Helodermin stimulated amylase secretion dose dependently, showing an efficacy similar to that of VIP but with 100 times less potency thanVIP. Adding 0.5 mM 3-isobutyl-1-methylxanthine increased the potency of helodermin’s action on amylase secretion but did not change the efficacy. The binding study showed that the order of binding affinity to VIP receptors was VIP = helodermin > secretin, while the order of that to secretin receptors was secretin > helodermin > VIP. These results suggest that helodermin stimulated amylase secretion from rat dispersed pancreatic acini via VIP-preferring receptors that are coupled to the production of intracellular cAMP, but a part of the postreceptor mechanism for enzyme secretion is different from that of VIP.

Original languageEnglish
Pages (from-to)161-166
Number of pages6
Issue number2
Publication statusPublished - 1995 Mar
Externally publishedYes


  • Amylase release
  • Cyclic AMP production
  • Helodermin
  • Pancreas
  • Receptor

ASJC Scopus subject areas

  • Internal Medicine
  • Endocrinology, Diabetes and Metabolism
  • Hepatology
  • Endocrinology


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