par Cauvin, Annick 
;Buscail, Louis ;Gourlet, Philippe ;De Neef, Philippe ;Gossen, Denis ;Arimura, Akira;Miyata, A.;Coy, D H;Robberecht, Patrick ;Christophe, Jean
Référence Peptides, 11, 4, page (773-777)
Publication Publié, 1990
;Buscail, Louis ;Gourlet, Philippe ;De Neef, Philippe ;Gossen, Denis ;Arimura, Akira;Miyata, A.;Coy, D H;Robberecht, Patrick ;Christophe, Jean Référence Peptides, 11, 4, page (773-777)
Publication Publié, 1990
Article révisé par les pairs
| Résumé : | We investigated the ability of two forms of Pituitary Adenylate Cyclase Activating Polypeptide [PACAP-38, the 38 amino acid peptide isolated from ovine hypothalamus, and PACAP-27, a shorter N-terminal (1-27) amidated version] to interact with specific receptors in membranes from the human neuroblastoma cell line NB-OK. [125I]PACAP-27 bound rapidly and specifically to one class of high affinity sites (K(d) 0.5 nM). VIP inhibited [125I]PACAP-27 binding 300- to 1000-fold less potently than PACAP-27 and PACAP-38. One μM PHI prevented tracer binding only partially and secretin, glucagon and GRF(1-29)NH2 were ineffective in this respect. PACAP-27 and PACAP-38 stimulated adenylate cyclase activity dose dependently and with similar efficacy (K(act) 0.2-0.3 nM), this activation being compatible with the occupancy of specific high affinity PACAP receptors. VIP was markedly less potent and less efficient on this enzyme than PACAP. Chemical cross-linking of [125I]PACAP-27 followed by SDS-PAGE and autoradiography revealed specific cross-linking with a 68 kDa protein. |
