人肺膜中血管活性肠肽受体的药理学特性
Pharmacological characterization of VIP receptors in human lung membranes.
作者信息
Robberecht P, Waelbroeck M, de Neef P, Camus J C, Coy D H, Christophe J
机构信息
Department of Biochemistry and Nutrition, Medical School, Université Libre de Bruxelles, Belgium.
出版信息
Peptides. 1988 Mar-Apr;9(2):339-45. doi: 10.1016/0196-9781(88)90270-7.
The ability of VIP, PHI, secretin, helodermin, and seven N-terminally D-amino monosubstituted VIP and PHI analogs to occupy (125I)iodo-VIP labeled receptors and to activate adenylate cyclase was tested on human lung membranes purified by the method of Schachter et al. Best fitted Kd, Kact and % of max. values suggested the coexistence, in near equal proportions, of two classes of VIP-preferring binding sites coupled to adenylate cyclase that showed similar decreasing affinity for: VIP greater than (D-Ala4)-VIP greater than (D-Asp3)-VIP = (D-Ser2)-VIP greater than (D-His1)-VIP greater than PHI greater than (D-Phe2)-VIP greater than (D-Phe4)-VIP. (D-Arg2)-VIP was a non-selective agonist. A third receptor type, coupled to adenylate cyclase and showing high affinity for secretin and helodermin but not for VIP, was also detected.
采用Schachter等人的方法纯化人肺膜，检测了血管活性肠肽（VIP）、胰高血糖素样肽（PHI）、促胰液素、蛙皮素以及7种N端D - 氨基酸单取代的VIP和PHI类似物占据（125I）碘化VIP标记受体并激活腺苷酸环化酶的能力。最佳拟合的解离常数（Kd）、激活常数（Kact）和最大值百分比表明，两类与腺苷酸环化酶偶联的优先结合VIP的位点以近乎相等的比例共存，它们对以下物质表现出相似的递减亲和力：VIP＞（D - Ala4）-VIP＞（D - Asp3）-VIP = （D - Ser2）-VIP＞（D - His1）-VIP＞PHI＞（D - Phe2）-VIP＞（D - Phe4）-VIP。（D - Arg2）-VIP是一种非选择性激动剂。还检测到了第三种受体类型，它与腺苷酸环化酶偶联，对促胰液素和蛙皮素具有高亲和力，但对VIP没有亲和力。
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