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

FEBS Letters

Göke, Rüdiger²  Arnold, Rudolf²  Göke, Burkhard¹  Richter, Gerd² 

[1] Department of Physiology, University of Michigan, Ann Arbor, USA;Department of Internal Medicine, Philipps-University of Marburg, FRG

关键词: GLP-1(7–36)amide;    Receptor;    Lung;    Guanine nuclcotide;    Adenylate cyclase;   

DOI  :  10.1016/0014-5793(90)80292-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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-l(7–36)amide consistent with the presence of a single class of binding sites with a dissociation constant (K _d) of 1.67 ± 0.29 . 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 (k _d of 448 ± 93 ). Vasoactive intestinal polypeptide and peptide-histidine-isolcucine also displaced ¹²⁵I-labelled GLP-1(7–36)amide from the receptor concentration-dependently; the k _d was 4.31 ± 0.8 and 7.93 ± 4.79 . respectively. Guaninc nucleotides (GTP-γ-S, GDP-β-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.

【 授权许可】

Unknown