Abstract
A human glucagon receptor has been cloned from human liver tissue. The 1578-bp cDNA clone encodes a protein of 477 amino acids with 82% identity to the rat glucagon receptor. The predicted secondary structure and homology to known proteins places this receptor within the superfamily of seven transmembrane domain G protein coupled receptors. Transfection of the human glucagon receptor into COS-7 cells confers upon them high affinity binding for [125I] glucagon. In membranes prepared from COS-7 cells transfected with the human glucagon receptor, the binding of [125I] glucagon is inhibited with the rank order of potency glucagon > oxyntomodulin > glucagon-like peptide 1 (7-36) amide >> glucagon-like peptide 2 = gastric inhibitory peptide = secretin.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Binding, Competitive
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Cell Line
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Cell Membrane / metabolism
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Chlorocebus aethiops
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Cloning, Molecular / methods
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DNA Primers
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DNA, Complementary / metabolism
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Gene Expression
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Glucagon / metabolism
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Humans
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Kidney
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Kinetics
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Liver / metabolism*
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Molecular Sequence Data
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Poly A / isolation & purification
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Poly A / metabolism
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Polymerase Chain Reaction / methods
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RNA / isolation & purification
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RNA / metabolism
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RNA, Messenger
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Rats
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Receptors, Glucagon / biosynthesis*
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Receptors, Glucagon / genetics
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Receptors, Glucagon / metabolism
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Transfection
Substances
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DNA Primers
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DNA, Complementary
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RNA, Messenger
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Receptors, Glucagon
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Recombinant Proteins
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Poly A
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RNA
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Glucagon