Isolation of a neuropeptide corresponding to the N-terminal 27 residues of the pituitary adenylate cyclase activating polypeptide with 38 residues (PACAP38)

Biochem Biophys Res Commun. 1990 Jul 31;170(2):643-8. doi: 10.1016/0006-291x(90)92140-u.


A novel neuropeptide with 38 residues (PACAP38) was isolated from ovine hypothalamic tissues using the pituitary adenylate cyclase activation in rat pituitary cell cultures as a parameter of the biological activity (Miyata et al, Biochem. Biophys. Res. Commun. 164, 567-574, 1989). From the side fractions obtained during the purification of PACAP38, a shorter form peptide with 27 residues corresponding to the N-terminal 27 amino acids of PACAP38 and amidated C-terminus was isolated and named as PACAP27. Synthetic PACAP27 showed a biological activity of adenylate cyclase stimulation comparable to PACAP38. Moreover PACAP27 which shows a considerable homology with vasoactive intestinal polypeptide (VIP) demonstrated a similar vasodepressor activity as VIP, but the adenylate cyclase stimulating activity was about 1000 times greater than VIP.

Publication types

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

MeSH terms

  • Adenylyl Cyclases / isolation & purification*
  • Amino Acid Sequence
  • Animals
  • Cells, Cultured
  • Enzyme Activation
  • Hypothalamus / analysis
  • Molecular Sequence Data
  • Neuropeptides / isolation & purification*
  • Neuropeptides / metabolism*
  • Peptides / chemical synthesis
  • Peptides / metabolism*
  • Pituitary Adenylate Cyclase-Activating Polypeptide
  • Pituitary Gland / enzymology*
  • Sheep
  • Vasoactive Intestinal Peptide / metabolism


  • Neuropeptides
  • Peptides
  • Pituitary Adenylate Cyclase-Activating Polypeptide
  • Vasoactive Intestinal Peptide
  • Adenylyl Cyclases