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| Content Provider | PubMed Central |
|---|---|
| Author | Perret, J. Vertongen, P. Solano, R. M. Cnudde, J. Robberecht, P. Waelbroeck, M. Langer, I. |
| Copyright Year | 2002 |
| Abstract | We investigated the human vasoactive intestinal polypeptide (VIP) receptors VPAC1 and VPAC2 mutated at conserved tyrosine residues in the first transmembrane helix (VPAC1 receptor Y146A and Y150A and VPAC2 receptor Y130A and Y134A). [125I]-Acetyl-His1 [D-Phe2, K15, R16, L27]-VIP (1–7)/GRF (8–27) (referred to as [125I]-VPAC1 antagonist) labelled VPAC1 binding sites, that displayed high and low affinities for VIP (IC50 values and per cent of high affinity binding sites: wild-type, 1 nM (57±9%) and 160 nM; Y146A, 30 nM (40±8%) and 800 nM; Y150A, 4 nM (27±8%) and 300 nM). [R16]-VIP behaved as a ‘super agonist' at both mutated VPAC1 receptors and the efficacies of VIP analogues modified in positions 1, 3 and 6 were significantly decreased. VIP was less potent at the Y130A and Y134A mutated VPAC2 receptors (EC50 200 and 400 nM, respectively) than at the wild-type VPAC2 receptor (EC50 7 nM). Furthermore, [hexanoyl-His1]-VIP behaved as a ‘super agonist' at the two mutated VPAC2 receptors, and VIP analogues modified in positions 1, 3 and 6 were less potent and efficient at the mutated than at wild-type VPAC2 receptors. However, the Y130A and Y134A mutants could not be studied in binding assays Our results suggest that the conserved tyrosine residues do not interact directly with the VIP His1, Asp3 or Phe6 residues (that are necessary for receptor activation), but stabilize the correct active receptor conformation. |
| Related Links | http://dx.doi.org/10.1038/sj.bjp.0704802 |
| Ending Page | 1048 |
| Page Count | 7 |
| Starting Page | 1042 |
| File Format | |
| ISSN | 00071188 |
| Journal | British Journal of Pharmacology |
| Issue Number | 7 |
| Volume Number | 136 |
| Language | English |
| Publisher Date | 2002-08-01 |
| Access Restriction | Open |
| Subject Keyword | Pharmacology Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Pharmacology |
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