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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Functional splice variants of the type II G protein-coupled receptor (VPAC2) for vasoactive intestinal peptide in mouse and human lymphocytes.

A PCR-based search for splice variants of the VPAC2 G protein- coupled receptor for vasoactive intestinal peptide (VIP) revealed: (a) a short-deletion variant in mouse lymphocytes termed VPAC2de367-380, that lacks 14 amino acids in the seventh transmembrane domain, and (b) a long-deletion variant in human lymphocytes termed VPAC2de325-438(i325-334), that lacks 114 amino acids beginning with the carboxyl-terminal end of the third cytoplasmic loop and has 10 new carboxy-terminal amino acids. VPAC2de367-380 binds VIP normally, but shows reduced VIP-evoked signaling and effects on immune functions, whereas VPAC2de325-438(i325-334) shows reduced binding affinity for VIP and a complex pattern of functional differences. These splice variants may modify the immunoregulatory contributions of the VIP-VPAC2 axis.[1]

References

  1. Functional splice variants of the type II G protein-coupled receptor (VPAC2) for vasoactive intestinal peptide in mouse and human lymphocytes. Miller, A.L., Verma, D., Grinninger, C., Huang, M.C., Goetzl, E.J. Ann. N. Y. Acad. Sci. (2006) [Pubmed]
 
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