The two forms of the pituitary adenylate cyclase activating polypeptide (PACAP (1–27) and PACAP (1–38)) interact with distinct receptors on rat pancreatic AR 4‐2J cell membranes

FEBS Letters

Vandermeers, André¹  Vandermeers-Piret, Marie-Claire¹  Buscail, Louis¹  Christophe, Jean¹  De Neef, Philippe¹  Gourlet, Philippe¹  Woussen-Colle, Marie-Claire¹  Robberecht, Patrick¹ 

[1] Department of Biochemistry and Nutrition, Medical School, Université Libre de Bruxelles, B-1000 Brussels, Belgium

关键词: Pituitary adenylate cyclase activating polypeptide (PACAP) receptor;    Adenylate cyclase;    Rat pancreatic acinar cell line AR 4-2J;    PACAP-38 and PACAP-27;    pituitary adenylate cyclase activating polypeptides in;    respectively;    the long version (the amidated 38-residue peptide(1–38)) and the N-terminal amidated 27-residue derivative version(1–27);    VIP;    vasoactive intestinal peptide;    rat PHI and PHV;    rat peptide histidine-isoleucinamide(1–27) and rat peptide histidine valinamide(1–44);   

DOI  :  10.1016/0014-5793(91)80958-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The existence of specific receptors for the two PACAPs (Pituirary Adenylate Cyclase Activating Peptides of 27 and 38 amino acids) was previously demonstrated on membranes from the pancreatic acinar cell line AR 4-2J (Buscail et al., FEBS Lett. 202, 77–81, 1990) by [¹²⁵I]PACAP-27 binding. Here we demonstrate, by comparing Scatchard analysis of saturation curves and competition binding curves obtained with [¹²⁵I]PACAP-27 and [¹²⁵I]PACAP-38 as radioligands, the coexistence of two classes of receptors : 1/ PACAP-A receptors that recognize PACAP-27 and PACAP-38 with the same high affinity (K _d 0.3 nM) and 2/ PACAP-B receptors that recognize PACAP-38 with a high affinity (K _d 0.3 nM) and PACAP-27 with a lower affinity (K _d 30 nM). These two receptors are coupled to adenylate cyclase but can be clearly distinguished by the ability of PACAP(6–27) to specifically inhibit PACAP-27 adenylate cyclase activation.

【 授权许可】

Unknown