Wulff B, Møller Knudsen S, Adelhorst K, Fahrenkrug J
Department of Molecular Pharmacology, Novo-Nordisk Park, Måløv, Denmark.
FEBS Lett. 1997 Aug 25;413(3):405-8. doi: 10.1016/s0014-5793(97)00942-3.
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.
利用稳定转染大鼠血管活性肠肽受体1（rVIPR 1）cDNA的细胞系，研究了血管活性肠肽（VIP）与受体结合及产生环磷酸腺苷（cAMP）的结构要求。使用多种VIP与同源肽促胰液素的嵌合构建体，发现VIP的N端一半（1-11）可与促胰液素中的相应序列交换，对结合和激活的影响较小，而N端为VIP、C端为促胰液素的反向嵌合体则无法与VIP受体结合。数据表明，VIP的C端区域对受体结合和激活很重要。
