חיפוש מתקדם
Choi, M.-Y., Department of Entomology, Iowa State University, 407 Science II, Ames, IA 50011-3222, United States
Fuerst, E.-J., Department of Entomology, Iowa State University, 407 Science II, Ames, IA 50011-3222, United States
Rafaeli, A., Inst. Technol./Storage Agric. Prod., Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Jurenka, R., Department of Entomology, Iowa State University, 407 Science II, Ames, IA 50011-3222, United States
Pheromone biosynthesis-activating neuropeptide (PBAN), a peptide produced by the subesophageal ganglion, is used by a variety of moths to regulate pheromone production. PBAN acts directly on pheromone gland cells by using calcium and CAMP as second messengers. We have identified a gene encoding a G protein-coupled receptor (GPCR) from pheromone glands of the female moth Helicoverpa zea. The gene was identified based on sequence identity to a group of GPCRs from Drosophila that are homologous to neuromedin U receptors in vertebrates. The full-length PBAN receptor was subsequently cloned, expressed in Sf9 insect cells, and shown to mobilize calcium in response to PBAN. This response was dose-dependent (EC50 = 25 nM) with a maximum response at 300 nM and a minimal observable response at 10 nM. Four additional peptides produced by the PBAN-encoding gene were also tested for activity, and it was determined that three had similar activity to PBAN and the other was slightly less active. Peptides belonging to the same family as PBAN, namely pyrokinins, as well as the vertebrate neuromedin U peptide also induced a calcium response. We have identified a GPCR for the PBAN/pyrokinin family of peptides with a known function of stimulating pheromone biosynthesis in female moths. It is related to several receptors from insects (Drosophila and Anopheles) and to neuromedin U and ghrelin receptors from vertebrates.
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הספר "אוצר וולקני"
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תנאי שימוש
Identification of a G protein-coupled receptor for pheromone biosynthesis activating neuropeptide from pheromone glands of the moth Helicoverpa zea
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Choi, M.-Y., Department of Entomology, Iowa State University, 407 Science II, Ames, IA 50011-3222, United States
Fuerst, E.-J., Department of Entomology, Iowa State University, 407 Science II, Ames, IA 50011-3222, United States
Rafaeli, A., Inst. Technol./Storage Agric. Prod., Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Jurenka, R., Department of Entomology, Iowa State University, 407 Science II, Ames, IA 50011-3222, United States
Identification of a G protein-coupled receptor for pheromone biosynthesis activating neuropeptide from pheromone glands of the moth Helicoverpa zea
Pheromone biosynthesis-activating neuropeptide (PBAN), a peptide produced by the subesophageal ganglion, is used by a variety of moths to regulate pheromone production. PBAN acts directly on pheromone gland cells by using calcium and CAMP as second messengers. We have identified a gene encoding a G protein-coupled receptor (GPCR) from pheromone glands of the female moth Helicoverpa zea. The gene was identified based on sequence identity to a group of GPCRs from Drosophila that are homologous to neuromedin U receptors in vertebrates. The full-length PBAN receptor was subsequently cloned, expressed in Sf9 insect cells, and shown to mobilize calcium in response to PBAN. This response was dose-dependent (EC50 = 25 nM) with a maximum response at 300 nM and a minimal observable response at 10 nM. Four additional peptides produced by the PBAN-encoding gene were also tested for activity, and it was determined that three had similar activity to PBAN and the other was slightly less active. Peptides belonging to the same family as PBAN, namely pyrokinins, as well as the vertebrate neuromedin U peptide also induced a calcium response. We have identified a GPCR for the PBAN/pyrokinin family of peptides with a known function of stimulating pheromone biosynthesis in female moths. It is related to several receptors from insects (Drosophila and Anopheles) and to neuromedin U and ghrelin receptors from vertebrates.
Scientific Publication
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