Interaction of GRF with VIP receptors and stimulation of adenylate cyclase in rat and human intestinal epithelial membranes

FEBS Letters

Amiranoff, B.³  Laburthe, M.³  Boige, N.³  Rouyer-Fessard, C.³  Moroder, L.¹  Tatemoto, K.² 

[1] Max Planck Institut für Biochemie, Abteilung Peptidchemie, 8033 Martinsried, FRG;Department of Biochemistry II, Karolinska Institutet, S-104 01 Stockholm, Sweden;CNRS ERA 494, INSERM U.55, Equipe de Recherche sur le Mécanisme d'Action des Hormones et Neuropeptides Digestifs, Hôpital Saint-Antoine, 75571 Paris Cedex 12, France

关键词: VIP receptor;    Intestinal epithelial membrane;    Adenylate cyclase;    GRF;    PHI;    Secretin;    GRF;    growth hormone releasing factor;    PHI;    porcine intestinal peptide having N-terminal histidine and C-terminal isoleucine amide;    VIP;    vasoactive intestinal peptide;   

DOI  :  10.1016/0014-5793(83)80422-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

GRF (10⁻⁸–10⁻⁵ M) is shown to inhibit competitively the binding of [¹²⁵I]VIP to human and rat intestinal epithelial membranes. The affinity of GRF for VIP receptor is 700–800-times lower than that of VIP in both species. The order of affinity of different peptides is VIP > PHI > secretin > GRF in rat, and VIP > GRF > PHI > secretin in man. The important species specificity of VIP receptors in recognizing PHI and secretin does not occur in the case of GRF. GRF stimulates adenylate cyclase through its interaction with VIP receptors in rat and human membranes. However, while GRF behaves as a VIP agonist in human tissue, it is a partial agonist/antagonist of VIP in the rat.

【 授权许可】

Unknown