血管活性肠肽（VIP）与分离的牛甲状腺质膜的相互作用。

The interaction of vasoactive intestinal peptide (VIP) with isolated bovine thyroid plasma membranes.

作者信息

Molinero P, Calvo J R, Goberna R, Guerrero J M

出版信息

Biochem Biophys Res Commun. 1985 May 16;128(3):1336-41. doi: 10.1016/0006-291x(85)91087-3.

Abstract

The binding of vasoactive intestinal peptide (VIP) and stimulation of adenylate cyclase were studied in bovine thyroid plasma membranes. The binding depended on time, temperature and was saturable and specific. Binding studies suggested the presence of two classes of binding sites: a class with high affinity (Kd = 13 nM) and low capacity (6411 sites/pg), and a class with low affinity (Kd = 480 nm) and high capacity (105,300 sites/pg) at 15 degrees C. Secretin, glucagon, insulin and somatostatin did not displace the tracer from the membranes. VIP stimulated cyclic AMP production. Maximal cyclic AMP production (2-fold above basal values) was observed with 100 nM VIP and half-maximal response was obtained at 5 nM VIP at 15 degrees C.

摘要

对牛甲状腺质膜中血管活性肠肽（VIP）的结合及腺苷酸环化酶的刺激作用进行了研究。该结合作用依赖于时间、温度，具有饱和性和特异性。结合研究表明存在两类结合位点：在15℃时，一类具有高亲和力（解离常数Kd = 13 nM）和低容量（6411个位点/皮克），另一类具有低亲和力（Kd = 480 nM）和高容量（105,300个位点/皮克）。促胰液素、胰高血糖素、胰岛素和生长抑素不能使示踪剂从膜上置换下来。VIP刺激环磷酸腺苷（cAMP）的产生。在15℃时，100 nM的VIP可使cAMP产生达到最大值（比基础值高2倍），5 nM的VIP可产生半数最大反应。