Identification of a steroidogenic neurohormone in female mosquitoes

In the female mosquito, Aedes aegypti , neurohormones are released from the brain in response to a blood meal and stimulate the ovaries to secrete ecdysteroid hormones, which modulate yolk protein synthesis in the fat body. Neuropeptides with this bioactivity were isolated from head extracts, and pa...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1998-02, Vol.273 (7), p.3967-3971
Main Authors: Brown, M.R, Graf, R, Swiderek, K.M, Fendley, D, Stracker, T.H, Champagne, D.E, Lea, A.O
Format: Article
Language:English
Subjects:
ADN
Aedes - chemistry
AEDES AEGYPTI
Amino Acid Sequence
AMINO ACID SEQUENCES
Animals
Base Sequence
BRAIN
Brain - cytology
Brain - physiology
CEREBRO
CHEMICAL COMPOSITION
CHEMISTRY
CHIMIE
Cloning, Molecular
COMPLEMENTARY DNA
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
CONTROL HORMONAL
CONTROLE HORMONAL
DNA
ENCEPHALE
Female
FEMALES
FEMELLE
GENBANK/U69542
GONADOTROPHINE
GONADOTROPINAS
GONADOTROPINS
HEMBRA
HORMONAL CONTROL
HORMONAS
HORMONAS DE INVERTEBRADOS
HORMONAS DE LA MUDA
HORMONE
HORMONE D'INVERTEBRE
HORMONE DE MUE
HORMONES
IMMUNOHISTOCHEMISTRY
IMMUNOLOGIE
IMMUNOLOGY
INMUNOLOGIA
Insect Hormones - chemistry
Insect Proteins - chemistry
INVERTEBRATE HORMONES
MOLECULAR SEQUENCE DATA
MOULTING HORMONES
NEUROPEPTIDES
Neuropeptides - chemistry
NUCLEOTIDE SEQUENCE
OVARY ECDYSTEROIDOGENIC HORMONE
PEPTIDE
Peptide Fragments - analysis
PEPTIDES
PEPTIDOS
QUIMICA
Recombinant Proteins - genetics
SECRECION
SECRETION
SECUENCIA NUCLEOTIDICA
Sequence Analysis
Sequence Analysis, DNA
Sequence Homology, Amino Acid
SEQUENCE NUCLEOTIDIQUE
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:In the female mosquito, Aedes aegypti , neurohormones are released from the brain in response to a blood meal and stimulate the ovaries to secrete ecdysteroid hormones, which modulate yolk protein synthesis in the fat body. Neuropeptides with this bioactivity were isolated from head extracts, and partial sequences from these peptides when aligned gave a 31-residue sequence at the amino terminus. Oligonucleotide primers for this sequence were used to amplify with the polymerase chain reaction a genomic DNA product that hybridized to a clone from a head cDNA library. The cDNA encodes a 149-residue preprohormone that is processed into an 86-residue peptide, as indicated by the mass value obtained from the native peptide, with the expected amino-terminal sequence. After modification, the cDNA for the putative neurohormone was expressed in a bacterial system, and the purified peptide had high specific activity in bioassays, thus confirming that it is a steroidogenic gonadotropin, the first to be identified for invertebrates.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.273.7.3967