Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractSimilarities and differences of the volatile profiles of six spices explored by Proton Transfer Reaction Mass Spectrometry    Next AbstractA recent class of chemosensory neurons developed in mouse and rat »

Chem Senses


Title:The vomeronasal receptor V2R2 does not require escort molecules for expression in heterologous systems
Author(s):Silvotti L; Giannini G; Tirindelli R;
Address:"Dipartimento di Neuroscienze, Universita di Parma, Via Volturno 39, 43100 Parma, Italy"
Journal Title:Chem Senses
Year:2005
Volume:30
Issue:1
Page Number:1 - 8
DOI: 10.1093/chemse/bjh250
ISSN/ISBN:0379-864X (Print) 0379-864X (Linking)
Abstract:"In rodents, many behavioural responses are triggered by pheromones. These molecules are believed to bind and activate two families of G-protein coupled receptors, namely V1Rs and V2Rs, which are specifically expressed in the chemosensory neurons of the vomeronasal organ. V2Rs are homologous with Group 3 of G-protein-coupled receptors, which includes metabotropic glutamate receptors, calcium-sensing receptors, fish olfactory receptors, and taste receptors for sweet molecules and amino acids. The large extracellular region of these receptors is folded as a dimer and, in this form, binds agonists that in many cases are amino acids. It has recently been reported that V2Rs must be physically associated with specific major histocompatibility complex class Ib molecules (MHC) for their expression in both mouse vomeronasal neurons and heterologous cell lines. Here, we show that in contrast to the other V2Rs, V2R2, an atypical member of this receptor family, can be successfully and abundantly expressed by insect cells without the requirement of escort molecules like MHC. Moreover, the extracellular binding domain of V2R2, secreted as a soluble product, forms dimers via cysteine-mediated sulphur bridges. Overall, the data presented in this paper confirm that V2R2 diverges from the other members of the V2R family and suggest a different role for this receptor in pheromonal communication"
Keywords:"Animals Baculoviridae/genetics Base Sequence Humans Major Histocompatibility Complex/physiology Mice Molecular Sequence Data Receptors, Pheromone/*genetics/isolation & purification/*metabolism Recombinant Proteins/genetics/metabolism Spodoptera/cytology V;"
Notes:"MedlineSilvotti, Lucia Giannini, Giuseppina Tirindelli, Roberto eng Research Support, Non-U.S. Gov't England 2005/01/14 Chem Senses. 2005 Jan; 30(1):1-8. doi: 10.1093/chemse/bjh250"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 01-07-2024