[125I]海洛德明对大鼠肝细胞膜中高亲和力血管活性肠肽受体的特异性标记

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

作者信息

Robberecht P, Waelbroeck M, de Neef P, Camus J C, Vandermeers A, Vandermeers-Piret M C, Christophe J

出版信息

FEBS Lett. 1984 Jun 25;172(1):55-8. doi: 10.1016/0014-5793(84)80872-8.

Abstract

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 greater than helodermin greater than secretin greater than 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.

摘要

海洛德明是一种新从希拉毒蜥毒液中分离出的肽，在结构上与血管活性肠肽（VIP）和促胰液素相关。当用作放射性配体时，[125I]海洛德明能迅速且可逆地与大鼠肝脏粗膜结合，GTP可加速其解离。[125I]海洛德明和[125I]VIP与未标记肽的竞争结合曲线显示出亲和力递减顺序如下：VIP＞海洛德明＞促胰液素＞人胰高血糖素释放因子（1-29）-NH2。结合曲线的形状以及同时发生的腺苷酸环化酶激活情况与[125I]海洛德明对一类能够刺激腺苷酸环化酶的高亲和力VIP受体的特异性标记相符。