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 Abstract[Allelopathy of Phragmites australis on Spartina alterniflora under different salinity]    Next AbstractDataset on collecting volatile compounds produced by three bacteria and testing their efficacy against the pathogen Peronophythora litchii »

Gene


Title:Cloning and characterization of the pheromone biosynthesis activating neuropeptide receptor gene in Spodoptera littoralis larvae
Author(s):Zheng L; Lytle C; Njauw CN; Altstein M; Martins-Green M;
Address:"Department of Cell Biology and Neurosciences, University of California, Riverside, CA 92521, United States"
Journal Title:Gene
Year:2007
Volume:20070117
Issue:1-Feb
Page Number:20 - 30
DOI: 10.1016/j.gene.2006.12.025
ISSN/ISBN:0378-1119 (Print) 0378-1119 (Linking)
Abstract:"In noctuid moths cuticular pigmentation is regulated by the pyrokinin/pheromone biosynthesis activating neuropeptide (PK/PBAN) family, which also mediates a variety of other functions in moths and other insects. Numerous studies have shown that these neuropeptides exert their functions through activation of the PBAN receptor (PBAN-R), with subsequent Ca(2+) influx, followed by either activation of cAMP or direct activation of downstream kinases. Recently, several PBAN-Rs have been identified, all of which are from the pheromone gland of adult female moths, but evidence shows that functional PK/PBAN-Rs can also be expressed in insect larvae, where they mediate melanization and possibly other functions (e.g., diapause). Here, we identified a gene encoding a G-protein-coupled receptor from the 5th instar larval tissue of the moth Spodoptera littoralis. The cDNA of this gene contains an open reading frame with a length of 1050 nucleotides, which translates to a 350-amino acid, 42-kDa protein that shares 92% amino acid identity with Helicoverpa zea and Helicoverpa armigera PBAN-R, 81% with Bombyx mori PBAN-R and 72% with Plutella xylostella PBAN-R. The S. littoralis PBAN-R gene was stably expressed in NIH3T3 cells and transiently in HEK293 cells. We show that it mediates the dose-dependent PBAN-induced intracellular Ca(2+) response and activation of the MAP kinase via a PKC-dependent but Galphai-independent signaling mechanism. Other PK/PBAN family peptides (pheromonotropin and a C-terminally PBAN-derived peptide PBAN(28-33)NH(2)) also triggered MAP kinase activation. This receptor, together with the previously cloned PBAN-R, may facilitate our understanding of the cell-specific responses and functional diversities of this diverse neuropeptide family"
Keywords:"Amino Acid Sequence Animals Base Sequence Calcium Signaling/drug effects Cloning, Molecular DNA, Complementary/genetics Humans Larva/drug effects MAP Kinase Signaling System Mice Molecular Sequence Data NIH 3T3 Cells Neuropeptides/agonists/*metabolism Pep;"
Notes:"MedlineZheng, Lei Lytle, Christian Njauw, Ching-Ni Altstein, Miriam Martins-Green, Manuela eng Research Support, Non-U.S. Gov't Netherlands 2007/03/24 Gene. 2007 May 15; 393(1-2):20-30. doi: 10.1016/j.gene.2006.12.025. Epub 2007 Jan 17"

 
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 05-11-2024