Abstract
The structural requirements of vasoactive intestinal polypeptide (VIP) for receptor binding and cAMP production were studied in a cell line stable transfected with the cDNA for rat VIP receptor 1 (rVIPR 1). Using a number of chimeric constructs of VIP and the homologue peptide secretin, it was found that the N-terminal half of VIP (1-11) can be exchanged with the corresponding sequences in secretin with only modest influence on binding and activation, whereas the opposite chimeras with N-terminal VIP and C-terminal secretin were unable to bind to the VIP receptor. The data suggest that the C-terminal region of VIP is important for receptor binding and activation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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1-Methyl-3-isobutylxanthine / pharmacology
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Adenylyl Cyclases / metabolism
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Amino Acid Sequence
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Animals
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Binding, Competitive
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CHO Cells
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Cricetinae
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Cyclic AMP / metabolism
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Enzyme Activation
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Kinetics
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Molecular Sequence Data
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Peptide Fragments / chemical synthesis
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Peptide Fragments / chemistry
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Peptide Fragments / pharmacology
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Rats
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Receptors, Vasoactive Intestinal Peptide / biosynthesis
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Receptors, Vasoactive Intestinal Peptide / physiology*
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Receptors, Vasoactive Intestinal Polypeptide, Type I
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Recombinant Fusion Proteins / pharmacology
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Recombinant Proteins / biosynthesis
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Secretin / chemistry
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Transfection
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Vasoactive Intestinal Peptide / chemistry
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Vasoactive Intestinal Peptide / metabolism*
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Vasoactive Intestinal Peptide / pharmacology*
Substances
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Peptide Fragments
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Receptors, Vasoactive Intestinal Peptide
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Receptors, Vasoactive Intestinal Polypeptide, Type I
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Recombinant Fusion Proteins
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Recombinant Proteins
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Secretin
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Vasoactive Intestinal Peptide
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Cyclic AMP
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Adenylyl Cyclases
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1-Methyl-3-isobutylxanthine