- Peptide (C)EEAQLENETIG(S)SK, corresponding to amino acid residues 52-65 of human VPAC1 (Accession P32241). Extracellular, N-terminus.
- THP-1 monocytic leukemia cells and mouse J774 macrophage cells (2.5-5 µg).
- Cell surface detection of VPAC1 in live intact human THP-1 monocytic leukemia cells:___ Cells.
___ Cells + rabbit IgG isotype control-FITC.
___ Cells + Anti-VPAC1 (VIPR1) (extracellular)-FITC Antibody (#AVR-001-F), (2.5 µg).
Vasointestinal peptide (VIP) and pituitary adenylate cyclase–activating peptide (PACAP) belong to the glucagon hormone superfamily, which includes secretin, growth hormone–releasing hormone (GHRH), glucagon, glucagon-like peptides 1 and 2 (GLP-1 and GLP-2), peptide histidine methionine (PHM), and glucose-dependent insulinotropic polypeptide (GIP)1. PACAP and VIP effects have been described in the digestive tract, cardiovascular system, airways, reproductive system, immune system, endocrine glands, and brain2. VIP and PACAP share a common G-protein coupled receptor, VPAC13.
VPAC1 is a membrane-associated protein and shares significant homology with members of the G-protein coupled class B receptor family, the most important of which is the presence of large N-terminal extracellular domains which contain 10 highly conserved amino acids including six cysteines, putative N-terminal leader sequences and several potential N-glycosylation sites4. In the CNS, VPAC1 receptors are abundantly localized in piriform cortex, cerebral cortex, suprachiasmatic nucleus, hippocampus, and pineal gland5. In peripheral tissues, VPAC1 receptors have been found in breast, kidney, liver, lung, prostate, spleen, and mucosa of the gastrointestinal tract6. VPAC1 mediates a large array of VIP and PACAP actions on exocrine secretion, hormones release, muscle relaxation, metabolism, fetus growth, tumor cells and embryonic brain development7.