A natural variant type II G protein-coupled receptor for vasoactive intestinal peptide with altered function.

Abstract

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.

Cite this paper

@article{Grinninger2004ANV, title={A natural variant type II G protein-coupled receptor for vasoactive intestinal peptide with altered function.}, author={Carola Grinninger and Wengang Wang and Kaveh Bastani Oskoui and Julia K Voice and Edward J Goetzl}, journal={The Journal of biological chemistry}, year={2004}, volume={279 39}, pages={40259-62} }