Abstract
We have cloned and sequenced a cDNA isolated from a human SUP-T1 lymphoblast cell line library. It encoded a 457 amino acids protein having 87% identity with the rat PACAP type II, VIP2 receptor. Chinese hamster ovary (CHO) cells stably transfected with cloned cDNA expressed a specific binding of 125I[Acetyl-His1]PACAP-27. This binding was inhibited by GTP, and by the peptides helodermin, VIP, PACAP-27 and PACAP-38 that also stimulated adenylate cyclase activity. The order of potency was PACAP-38 > VIP > or = helodermin > or = PACAP-27. Comparison of the results in two cell lines expressing different receptor densities suggested that helodermin and PACAP-38 had a higher intrinsic activity than VIP and PACAP-27.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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CHO Cells
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Cell Line
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Cloning, Molecular
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Cricetinae
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DNA Primers / genetics
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DNA, Complementary / genetics
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Humans
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Intercellular Signaling Peptides and Proteins
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Lymphocytes / metabolism*
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Molecular Sequence Data
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Neuropeptides / metabolism
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Peptides / metabolism
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Pituitary Adenylate Cyclase-Activating Polypeptide
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Rats
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Receptors, Vasoactive Intestinal Peptide / genetics*
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Receptors, Vasoactive Intestinal Peptide / metabolism
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Receptors, Vasoactive Intestinal Peptide, Type II
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Sequence Homology, Amino Acid
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Transfection
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Vasoactive Intestinal Peptide / metabolism
Substances
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ADCYAP1 protein, human
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Adcyap1 protein, rat
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DNA Primers
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DNA, Complementary
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Intercellular Signaling Peptides and Proteins
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Neuropeptides
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Peptides
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Pituitary Adenylate Cyclase-Activating Polypeptide
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Receptors, Vasoactive Intestinal Peptide
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Receptors, Vasoactive Intestinal Peptide, Type II
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VIPR2 protein, human
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Vasoactive Intestinal Peptide
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heliodermin
Associated data
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GENBANK/L36566
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GENBANK/L40764