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The C‐terminal part of VIP is important for receptor binding and activation, as evidenced by chimeric constructs of VIP/secretin
Author(s) -
Wulff Birgitte,
Møller Knudsen Sanne,
Adelhorst Kim,
Fahrenkrug Jan
Publication year - 1997
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/s0014-5793(97)00942-3
Subject(s) - secretin , vasoactive intestinal peptide , secretin family , receptor , complementary dna , chemistry , transfection , microbiology and biotechnology , biology , neuropeptide , biochemistry , gene , pancreas
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.