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Presence of highly selective receptors for PACAP (pituitary adenylate cyclase activating peptide) in membranes from the rat pancreatic acinar cell line AR 4‐2J
Author(s) -
Buscail Louis,
Gourlet Philippe,
Cauvin Annick,
De Neef Philippe,
Gossen Denis,
Arimura Akira,
Miyata Atsuro,
Coy David H.,
Robberecht Patrick,
Christophe Jean
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80158-f
Subject(s) - adenylate kinase , cyclase , pituitary adenylate cyclase activating peptide , receptor , chemistry , vasoactive intestinal peptide , membrane , peptide , endocrinology , biochemistry , medicine , microbiology and biotechnology , biology , neuropeptide
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 [ 125 I]PACAP‐27 ( K d =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 ( K act = 0.2 nM) being much higher than that of VIP ( K act = 100 nM) and helodemin ( K act = 30 nM). Chemical cross‐linking of [ 125 I]PACAP‐27 followed by SDS‐PAGE and autoradiography revealed a specifically cross‐linked peptide with an M r , of 68000 (including 3000 for one PACAP‐27 molecule).