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Peptides

Title:		Pheromonotropic and melanotropic PK/PBAN receptors: differential ligand-receptor interactions
Author(s):		Shalev AH; Altstein M;
Address:		"Department of Entomology, The Volcani Center, Bet Dagan 50250, Israel. Department of Entomology, The Volcani Center, Bet Dagan 50250, Israel. Electronic address: vinnie2@agri.gov.il"
Journal Title:		Peptides
Year:		2015
Volume:		20141105
Issue:
Page Number:		81 - 89
DOI:		10.1016/j.peptides.2014.10.014
ISSN/ISBN:		1873-5169 (Electronic) 0196-9781 (Linking)
Abstract:		"The aim of the present study was to further characterize the PK/PBAN receptors and their interaction with various PK/PBAN peptides in order to get a better understanding of their ubiquitous and multifunctional nature. Two cloned receptors stably expressed in Spodoptera frugiperda (Sf9) cells were used in this study: a Heliothis peltigera pheromone gland receptor (Hep-PK/PBAN-R) (which stimulates sex pheromone biosynthesis) and Spodoptera littoralis larval receptor (Spl-PK/PBAN-R) (which mediates cuticular melanization in moth larvae) and their ability to respond to several native PK/PBAN peptides: beta-subesophageal neuropeptide (beta-SGNP), myotropin (MT) and Leucophaea maderae pyrokinin (LPK), as well as linear and cyclic analogs was tested by monitoring their ability to stimulate Ca(2+) release. The receptors exhibited a differential response to beta-SGNP, which activated the Hep-PK/PBAN-R but not the Spl-PK/PBAN-R - a response opposite to that previously demonstrated with diapause hormone (DH). MT was somewhat more active on Spl-PK/PBAN-R than on Hep-PK/PBAN-R. LPK elicited similar positive responses in both receptors (like that with PBAN). A differential response toward both receptors was also noticed with the PBAN-derived backbone cyclic (BBC) conformationally constrained peptide BBC-5. The peptides BBC-7 and BBC-8 activated both receptors. The results correlate between two PK/PBAN mediated function (cuticular melanization and sex pheromone biosynthesis) and the peptides that activate them and thus advance our understanding of the mode of action of the PK/PBAN family, and might help in exploring novel high-affinity receptor-specific antagonists that could serve as a basis for development of new families of insect-control agents"
Keywords:		"Animals Calcium Signaling Inhibitory Concentration 50 Insect Proteins/*physiology Moths Neuropeptides/pharmacology/*physiology Pheromones/physiology Receptors, Neuropeptide/agonists/*physiology Sf9 Cells Spodoptera Heliothis peltigera Insect neuropeptides;"
Notes:		"MedlineShalev, Aliza Hariton Altstein, Miriam eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. 2014/12/03 Peptides. 2015 Jan; 63:81-9. doi: 10.1016/j.peptides.2014.10.014. Epub 2014 Nov 5"