Linked Life Data

17590269

Source:http://linkedlifedata.com/resource/pubmed/id/17590269

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2007-7-9
pubmed:abstractText
The FXPRL-amide peptide family (pyrokinin/PBAN family) consists of insect peptides that function broadly in insect life processes and are characterized by a conserved C-terminal motif. In the silkworm, Bombyx mori, sex pheromone biosynthesis and induction of embryonic diapause are regulated by peptides from this family. To elucidate other functions of Bombyx FXPRL-amide peptides, we analyzed the tissue expression patterns of two known Bombyx G-protein coupled receptors for these peptides. We found that the Bombyx diapause hormone receptor (BmDHR), is expressed in the prothoracic gland (PG), the organ which synthesizes and releases the insect molting hormones, ecdysteroids. Furthermore, diapause hormone (DH), a member of the Bombyx FXPRL-amide peptides, increases both intracellular Ca(2+) and cAMP concentrations and induces ecdysteroidogenesis in late fifth instar PGs coincident with BmDHR expression in the PGs. DH also has the highest prothoracicotropic activity among the FXPRL-amide peptides, which corresponds well to the ligand specificity of heterologously expressed BmDHR. These results demonstrate that FXPRL-amide peptides can function as prothoracicotropic factors through the activation of BmDHR and may play an important role in controlling molting and metamorphosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
51-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
FXPRL-amide peptides induce ecdysteroidogenesis through a G-protein coupled receptor expressed in the prothoracic gland of Bombyx mori.
pubmed:affiliation
Department of Integrated Biosciences, Room 201, Graduate School of Frontier Sciences, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8562, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't