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Gene Review

VIPR2  -  vasoactive intestinal peptide receptor 2

Homo sapiens

Synonyms: C16DUPq36.3, DUP7q36.3, Helodermin-preferring VIP receptor, PACAP type III receptor, PACAP-R-3, ...
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Disease relevance of VIPR2

  • To initially test the hypothesis that expression of VIP-1 receptors plays an important role in the pathophysiology of human ductal pancreatic adenocarcinomas, we used reverse transcription-PCR with Southern blot hybridization to confirm expression of VIP-1 and VIP-2 receptor mRNA in the vast majority of 28 human ductal pancreatic adenocarcinomas [1].
  • VIP and pituitary adenylate cyclase activating polypeptide (PACAP) have an antiproliferative effect on the T98G human glioblastoma cell line through interaction with VIP2 receptor [2].

High impact information on VIPR2


Biological context of VIPR2

  • Our results suggest that deletion of the VIPR2 gene is not the sole factor responsible for the HPE3 phenotype [7].
  • The VIPR2 gene maps to the human chromosomal region 7q36.3 and to the F2 region of mouse chromosome 12 [7].
  • VIPR2 was expressed in 75.8% of cPNET, in 28.6% of ESFT and in all 10 cell lines. cPNET demonstrated high-affinity binding of 125I-VIP on quantitative autoradiography and in competitive binding assays [8].
  • Here, we describe the characterisation of the VIPR2 gene structure and promoter region [6].
  • The VIPR2 gene is encoded by 13 exons, the initiator codon of the 438 amino acid open reading frame is located in exon 1 and the termination signal and a poly-adenylation signal sequence are located in exon 13 [6].

Anatomical context of VIPR2

  • VIPR2 transduces human T-cell chemotaxis, expression of matrix metalloproteinases (MMPs) 2 and 9 and consequently basement membrane and connective tissue transmigration, while signaling suppression of proliferation and cytokine production [9].
  • Transcripts of the common PACAP/VIP R-2 are also found in human brain and a number of peripheral tissues, such as pancreas, muscle, heart, lund, kidney, stomach and low levels in the liver [10].
  • VIP and PACAP-38 were equipotent in stimulating accumulation of cAMP in COS-7 cells transfected with the human VIP-2 receptor [11].
  • VIP1 and VIP2 receptor immunoreactivity was seen on keratinocytes in the basal layer of the epidermis, with no difference between involved and uninvolved skin [12].

Associations of VIPR2 with chemical compounds

  • Ro 25-1392 evoked concurrent and concentration-dependent increases in intracellular levels of calcium and cyclic AMP (EC50 = 3.0 +/- 0.4 nM, mean +/- S.E.M., n = 4) in VIPR2 transfectants, but not in VIPR1 transfectants [13].

Physical interactions of VIPR2

  • Nonradioactive Ro 25-1392 was as potent a competitive inhibitor as VIP for the binding of 125I-VIP to VIPR2 transfectants (Ki = 9.6 +/- 1.0 and 16 +/- 1.7 nM, respectively; mean +/- S.E.M., n = 4) [13].

Regulatory relationships of VIPR2

  • DU-145/AR cells constitutively expressed both VIP1R and VIP2R mRNA, but the parent DU-145 cells did not [14].

Other interactions of VIPR2


Analytical, diagnostic and therapeutic context of VIPR2


  1. Vasoactive intestinal peptide (VIP) stimulates in vitro growth of VIP-1 receptor-bearing human pancreatic adenocarcinoma-derived cells. Jiang, S., Kopras, E., McMichael, M., Bell, R.H., Ulrich, C.D. Cancer Res. (1997) [Pubmed]
  2. VIP and pituitary adenylate cyclase activating polypeptide (PACAP) have an antiproliferative effect on the T98G human glioblastoma cell line through interaction with VIP2 receptor. Vertongen, P., Camby, I., Darro, F., Kiss, R., Robberecht, P. Neuropeptides (1996) [Pubmed]
  3. Transduction of specific inhibition of HuT 78 human T cell chemotaxis by type I vasoactive intestinal peptide receptors. Xia, M., Gaufo, G.O., Wang, Q., Sreedharan, S.P., Goetzl, E.J. J. Immunol. (1996) [Pubmed]
  4. Localization of the VIP2 receptor protein on GnRH neurons in the female rat. Smith, M.J., Jiennes, L., Wise, P.M. Endocrinology (2000) [Pubmed]
  5. Selective labeling and isolation of functional classes of interstitial cells of Cajal of human and murine small intestine. Chen, H., Redelman, D., Ro, S., Ward, S.M., Ord??g, T., Sanders, K.M. Am. J. Physiol., Cell Physiol. (2007) [Pubmed]
  6. Structure of the human VIPR2 gene for vasoactive intestinal peptide receptor type 2. Lutz, E.M., Shen, S., Mackay, M., West, K., Harmar, A.J. FEBS Lett. (1999) [Pubmed]
  7. Chromosomal localization in mouse and human of the vasoactive intestinal peptide receptor type 2 gene: a possible contributor to the holoprosencephaly 3 phenotype. Mackay, M., Fantes, J., Scherer, S., Boyle, S., West, K., Tsui, L.C., Belloni, E., Lutz, E., Van Heyningen, V., Harmar, A.J. Genomics (1996) [Pubmed]
  8. Vasoactive intestinal peptide (VIP) and VIP receptors: gene expression and growth modulation in medulloblastoma and other central primitive neuroectodermal tumors of childhood. Frühwald, M.C., O'Dorisio, M.S., Fleitz, J., Pietsch, T., Reubi, J.C. Int. J. Cancer (1999) [Pubmed]
  9. Selectivity of effects of vasoactive intestinal peptide on macrophages and lymphocytes in compartmental immune responses. Goetzl, E.J., Pankhaniya, R.R., Gaufo, G.O., Mu, Y., Xia, M., Sreedharan, S.P. Ann. N. Y. Acad. Sci. (1998) [Pubmed]
  10. Tissue specific expression of different human receptor types for pituitary adenylate cyclase activating polypeptide and vasoactive intestinal polypeptide: implications for their role in human physiology. Wei, Y., Mojsov, S. J. Neuroendocrinol. (1996) [Pubmed]
  11. Cloning and functional characterization of the human vasoactive intestinal peptide (VIP)-2 receptor. Adamou, J.E., Aiyar, N., Van Horn, S., Elshourbagy, N.A. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  12. Vasoactive intestinal polypeptide in allergic contact dermatitis: an immunohistochemical and radioimmunoassay study. Lundeberg, L., Nordlind, K. Arch. Dermatol. Res. (1999) [Pubmed]
  13. Novel cyclic peptide agonist of high potency and selectivity for the type II vasoactive intestinal peptide receptor. Xia, M., Sreedharan, S.P., Bolin, D.R., Gaufo, G.O., Goetzl, E.J. J. Pharmacol. Exp. Ther. (1997) [Pubmed]
  14. Vasoactive intestinal peptide (VIP) enhances the cell motility of androgen receptor-transfected DU-145 prostate cancer cells (DU-145/AR). Nagakawa, O., Murata, J., Junicho, A., Matsuda, T., Fujiuchi, Y., Fuse, H., Saiki, I. Cancer Lett. (2002) [Pubmed]
  15. Characterization of the VIP receptor from SUP T1 lymphoblasts. Robberecht, P., Gourlet, P., Vertongen, P., Svoboda, M. Adv. Neuroimmunol. (1996) [Pubmed]
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