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Detection of the Five Transmembrane Vasoactive Intestinal Peptide Receptor‐1 Isoform in Mouse Tissue
Author(s) -
Hermann Rebecca,
Palmer Megan,
Dorsam Glenn
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.1044.10
Subject(s) - gene isoform , vasoactive intestinal peptide , g protein coupled receptor , receptor , biology , transmembrane protein , microbiology and biotechnology , signal transduction , biochemistry , neuropeptide , gene
Vasoactive intestinal peptide (VIP) is a pleiotropic secretagogue involved in crucial biological processes necessary for life. Its biological effects are mediated by two structurally similar integral membrane receptors called vasoactive intestinal peptide receptor‐1 and 2 (VPACR‐1/2). VPACR‐1 is a member of the group IIA G protein coupled receptors (GPCR) which are characterized by 7 transmembrane domains (7TM). VIP binding to VPACR‐1 elicits adenylate cyclase/cAMP/PKA and phospholipase C/D signaling cascades. VPACR‐1 has a wide expression profile in the mouse, including the nervous and immune systems. Recently, a novel VPACR‐1 isoform was identified that lacks exons 10 and 11 to form a 5 transmembrane receptor (5TM), and in contrast, elicits significant tyrosine phosphorylation through a G protein independent mechanism. The biological effects mediated by this recently discovered non‐GPCR linked isoform, 5TM, are not known. To determine the expression profile of this isoform, mRNA will be collected from various mouse tissues, cDNA generated with anchored primers and the expression profile of the 7TM and 5TM quantitated using qPCR. Identifying which mouse tissues express the 5 TM VPACR‐1 isoform is a major first step in understanding its contribution to cellular function and physiology. Supported by NIH‐KO1 1K01DK064828 and COBRE 2P20RR05566.