大鼠肺膜上胰高血糖素样肽-1（7-36）酰胺受体的特性研究

Characterization of receptors for glucagon-like peptide-1(7-36)amide on rat lung membranes.

作者信息

Richter G, Göke R, Göke B, Arnold R

机构信息

Department of Internal Medicine, Philipps-University of Marburg, FRG.

出版信息

FEBS Lett. 1990 Jul 2;267(1):78-80. doi: 10.1016/0014-5793(90)80292-q.

DOI:10.1016/0014-5793(90)80292-q

PMID:2163902

Abstract

Specific binding of 125I-labelled GLP-1(7-36)amide to rat lung membranes was dependent upon time and temperature and was proportional to membrane protein concentration. Binding was inhibited in a concentration-dependent manner by unlabelled GLP-1(7-36)amide consistent with the presence of a single class of binding sites with a dissociation constant (Kd) of 1.67 +/- 0.29 nmol/l. GLP-1(1-36)amide was 260 times less potent in inhibiting the binding of 125I-labelled GLP-1(7-36)amide to lung membranes (Kd of 448 +/- 93 nmol/l). Vasoactive intestinal polypeptide and peptide-histidine-isoleucine also displaced 125I-labelled GLP-1(7-36)amide from the receptor concentration-dependently; the Kd was 4.31 +/- 0.8 and 7.93 +/- 4.79 nmol/l, respectively. Guanine nucleotides (GTP-gamma-S, GDP-beta-S) decreased the binding of 125I-labelled GLP-1(7-36)amide to rat lung membranes as was found for GLP-1(7-36)amide receptors in RINm5F cells which were also shown to be coupled to the adenylate cyclase system.

摘要

125I标记的胰高血糖素样肽-1（7-36）酰胺与大鼠肺膜的特异性结合依赖于时间和温度，且与膜蛋白浓度成正比。未标记的胰高血糖素样肽-1（7-36）酰胺以浓度依赖性方式抑制结合，这与存在一类解离常数（Kd）为1.67±0.29 nmol/l的结合位点一致。胰高血糖素样肽-1（1-36）酰胺在抑制125I标记的胰高血糖素样肽-1（7-36）酰胺与肺膜结合方面的效力低260倍（Kd为448±93 nmol/l）。血管活性肠肽和肽-组氨酸-异亮氨酸也以浓度依赖性方式从受体上取代125I标记的胰高血糖素样肽-1（7-36）酰胺；Kd分别为4.31±0.8和7.93±4.79 nmol/l。鸟嘌呤核苷酸（GTP-γ-S、GDP-β-S）降低了125I标记的胰高血糖素样肽-1（7-36）酰胺与大鼠肺膜的结合，这与RINm5F细胞中胰高血糖素样肽-1（7-36）酰胺受体的情况相同，后者也被证明与腺苷酸环化酶系统偶联。