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There are two known receptors for the vasoactive intestinal peptide (VIP) termed VPAC1 and VPAC2.  These receptors bind both VIP and pituitary adenylate cyclase-activating polypeptide (PACAP) to some degree. Both receptors are members of the 7 transmembrane G protein-coupled receptor family.
Pituitary adenylate cyclase-activating polypeptide and its receptors: 20 years after the discovery. Vaudry D1, Falluel-Morel A, Bourgault S, Basille M, Burel D, Wurtz O, Fournier A, Chow BK, Hashimoto H, Galas L, Vaudry H.
Pituitary Adenylate Cyclase Activating Polypeptide (PACAP) is a gastrointestinal neuropeptide, which belongs to the family of regulatory peptides that also includes Vasoactive Intestinal Polypeptide (VIP), secretin, glucagon and GLP-1 hormones (38). It was identified in 1989 by Arimura and colleagues from ovine hypothalamus (24). This peptide occurs naturally as both a 27-amino acid or 38-amino acid biologically active forms that have equal biological activities and are thus, named PACAP-27 and PACAP-38, respectively (Figure 1).
Pituitary adenylate cyclase-activating polypeptide (PACAP) is a member of the vasoactive intestinal peptide (VIP)/secretin/glucagon family of peptides and represents the most potent activator of cAMP-dependent signaling pathways presently known. PACAP exists in two forms: PACAP-38, the predominant PACAP form in the nervous system, and PACAP-27, which comprises the 27 N-terminal amino acids of PACAP-38 (for review, see Arimura, 1998).
Pituitary adenylate cyclase-activating polypeptide also known as PACAP is a protein that in humans is encoded by the ADCYAP1 gene.  PACAP is similar to vasoactive intestinal peptide. One of its effects is to stimulate enterochromaffin-like cells. It binds to vasoactive intestinal peptide receptor and to the PACAP receptor.