| First Author | Grinninger C | Year | 2004 |
| Journal | J Biol Chem | Volume | 279 |
| Issue | 39 | Pages | 40259-62 |
| PubMed ID | 15302876 | Mgi Jnum | J:93346 |
| Mgi Id | MGI:3056878 | Doi | 10.1074/jbc.C400332200 |
| Citation | Grinninger C, et al. (2004) A natural variant type II G protein-coupled receptor for vasoactive intestinal peptide with altered function. J Biol Chem 279(39):40259-62 |
| abstractText | The vasoactive intestinal peptide (VIP) and its G protein-coupled receptors VPAC1 and VPAC2 prominently mediate diverse physiological functions in the neural, endocrine, and immune systems. A deletion variant of mouse VPAC2 has been identified in immune cells that lacks amino acids 367-380 at the carboxyl-terminal end of the seventh transmembrane domain. When expressed at equivalent levels in a human Jurkat T cell line, which has very low endogenous expression of human VPAC1 and VPAC2, wild-type and deletion-variant VPAC2 bound the same amount of 125I-VIP with similar affinity. Unlike wild-type VPAC2, however, deletion-variant VPAC2 did not transduce VIP-elicited increases in intracellular concentration of cyclic AMP, chemotaxis, or suppression of generation of interleukin-2. Natural deletion of part of the last transmembrane domain of VPAC2 thus abrogates signaling functions without apparent alterations of expression or ligand binding. |
