Specific labelling by [125I]helodermin of high‐affinity VIP receptors in rat liver membranes

FEBS Letters

Vandermeers, André¹  Vandermeers-Piret, Marie-Claire¹  Christophe, Jean¹  De Neef, Philippe¹  Waelbroeck, Magali¹  Camus, Jean-Claude¹  Robberecht, Patrick¹ 

[1] Department of Biochemistry and Nutrition, Medical School, Université Libre de Bruxelles, Bid de Waterloo 115, B-1000 Brussels, Belgium

关键词: Gila Monster venom Helodermin Vasoactive intestinal peptide Secretin Growth hormone releasing factor Adenylate cyclase Rat liver membrane;    VIP;    vasoactive intestinal peptide;    GRF;    growth hormone releasing factor;    PHI;    porcine peptide having N-terminal histidine and C-terminal isoleucineamide;    hpGRF;    human pancreatic growth hormone releasing factor;   

DOI  :  10.1016/0014-5793(84)80872-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Helodermin, a newly isolated peptide from Gila Monster venom, is structurally related to VIP and secretin. When used as radioligand, [¹²⁵I]helodermin bound rapidly and reversibly to crude rat liver membranes, the dissociation being accelerated by GTP. Competition binding curves of [¹²⁵I]helodermin and [¹²⁵I]VIP with unlabelled peptides showed the following order of decreasing affinity: VIP > helodermin > secretin > hpGRF(1–29)-NH₂. The shape of binding curves and of concurrent adenylate cyclase activation is compatible with the specific labelling, by [¹²⁵I]helodermin, of a class of high-affinity VIP receptors that is capable to stimulate adenylate cyclase.

【 授权许可】

Unknown