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Characterization of receptors for glucagon‐like peptide‐1(7–36) amide on rat lung membranes
Author(s) -
Richter Gerd,
Göke Rüdiger,
Göke Burkhard,
Arnold Rudolf
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80292-q
Subject(s) - amide , membrane , receptor , chemistry , vasoactive intestinal peptide , gtp' , cyclase , adenylate kinase , peptide , dissociation constant , histidine , binding site , biochemistry , stereochemistry , amino acid , neuropeptide , enzyme
Specific binding of 125 I‐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 125 I‐labelled GLP‐1(7 36)amide to lung membranes ( k d of 448 ± 93). Vasoactive intestinal polypeptide and peptide‐histidine‐isolcucine also displaced 125 I‐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 125 I‐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.