PRESENCE OF HIGHLY SELECTIVE RECEPTORS FOR PACAP (PITUITARY ADENYLATE-CYCLASE ACTIVATING PEPTIDE) IN MEMBRANES FROM THE RAT PANCREATIC ACINAR CELL-LINE AR-4-2J

We characterized highly selective receptors for PACAP, the pituitary adenylate cyclase activating peptide, in the tumoral acinar cell line AR 4-2J derived from the rat pancreas. PACAP, a novel hypothalamic peptide related to vasoactive intestinal peptide (VIP), was tested as the full natural 38-residue peptide (PACAP-38) and as an N-terminal amidated 27-residue derivative (PACAP-27). The binding sites showed considerable affinity for [125I]PACAP-27 (Kd =0.4 nM) and PACAP-38, while their affiity for VIP and the parent peptide helodemin was 1000-fold lower. These receptors were coupled to adenylate cyclase, the potency of PACAP-38 and PACAP-27 (Kact = 0.2 nM) being much higher than that of VIP (Kact= 100 nM) and helodemin (Kact = 30 nM). Chemical cross-linking of [125I]PACAP-27 followed by SDS-PAGE and autoradiography revealed a specifically cross-linked peptide with an Mr, of 68000 (including 3000 for one PACAP-27 molecule). © 1990.