RRC ID 553
Author Yamanaka N, Hua YJ, Mizoguchi A, Watanabe K, Niwa R, Tanaka Y, Kataoka H.
Title Identification of a novel prothoracicostatic hormone and its receptor in the silkworm Bombyx mori.
Journal J Biol Chem
Abstract The insect brain regulates the activity of the prothoracic glands to secrete ecdysteroids, which affect growth, molting, and metamorphosis. Here we report the identification of a novel prothoracicostatic factor and its receptor in the silkworm Bombyx mori. The prothoracicostatic factor purified from pupal brains of B. mori is a decapeptide with the conserved structure of an insect myosuppressin and thus named Bommo-myosuppressin. Bommo-myosuppressin dose dependently suppressed the cAMP level and inhibited ecdysteroidogenesis in the larval prothoracic glands at much lower concentrations than the prothoracicostatic peptide, the other prothoracicostatic factor reported previously. In vitro analyses using a prothoracic gland incubation method revealed that Bommo-myosuppressin and prothoracicostatic peptide regulate the prothoracic gland activity via different receptors. In situ hybridization and immunohistochemistry revealed the existence of Bommo-myosuppressin in the brain neurosecretory cells projecting to neurohemal organs in which it is stored. We also identified and functionally characterized a specific receptor for Bommo-myosuppressin and showed its high expression in the prothoracic glands. All these results suggest that Bommo-myosuppressin functions as a prothoracicostatic hormone and plays an important role in controlling insect development.
Volume 280(15)
Pages 14684-90
Published 2005-4-15
DOI 10.1074/jbc.M500308200
PII S0021-9258(20)65988-9
PMID 15701625
MeSH Amino Acid Sequence Animals Blotting, Northern Bombyx Brain / metabolism Calcium / metabolism Cell Line Chromatography, High Pressure Liquid Cyclic AMP / metabolism DNA, Complementary / metabolism Databases as Topic Ecdysone / chemistry Expressed Sequence Tags Gene Library Humans Image Processing, Computer-Assisted Immunohistochemistry In Situ Hybridization Insect Hormones / biosynthesis* Insect Hormones / chemistry* Ligands Mass Spectrometry Metamorphosis, Biological Molecular Sequence Data Neuropeptides / chemistry* Neuropeptides / physiology* Peptides / chemistry Phylogeny Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Spectrophotometry Ultraviolet Rays
IF 4.238
Times Cited 63
Silkworms EST database