A new type of functional VIP receptor has an affinity for helodermin in human SUP‐T1 lymphoblasts

FEBS Letters

Christophe, Jean¹  Cogniaux, Jacqueline²  De Neef, Philippe¹  Tastenoy, Michèle¹  Waelbroeck, Magali¹  Gourlet, Philippe¹  Robberecht, Patrick¹ 

[1] Department of Biochemistry and Nutrition, Medical School, Université Libre de Bruxelles, 115, Bd de Waterloo, B-1000 Brussels Belgium;Department of Virology, Institut Pasteur du Brabant, 608, rue Engeland, B-1180 Brussels, Belgium

关键词: Helodermin receptor;    Vasoactive intestinal peptide;    (T-cell-derived culture line;    SUP-T1;    Human);   

DOI  :  10.1016/0014-5793(88)80030-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A new type of VIP receptor was characterized in human SUP-T1 lymphoblasts. The order of potency of unlabeled peptides in the presence of [¹²⁵I]helodermin, was: helodermin(1–35)-NH₂ = helodermin(1–27)-NH₂ > helospectin > VIP = PHI > [D-Ser²]VIP > [D-Asp³]VIP > [D-His¹]VIP ⩾ [D-Ala⁴]VIP 2̆ secretin = GRF. This specificity was distinct from that of all VIP receptors described so far in that: (i) the affinity for helodermin (K_d = 3 nM) was higher than that of VIP (K_d = 15 nM) and PHI (K_d = 20 nM); and (ii) position 4 played an important role in ligand binding. The labeled sites were likely to be functional receptors as adenylate cyclase in crude lymphoblastic membranes (200-10 000 × g pellets) was stimulated by peptides, in the presence of GTP, with the following order of potency: helodermin(1–35)-NH₂ > helo-dermin(1–27)-NH₂ > helospectin = VIP = PHI.

【 授权许可】

Unknown