<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7(3)</volume><submitter>An S</submitter><pubmed_abstract>&lt;h4>Background&lt;/h4>Bursicon is a heterodimer neuropeptide composed of two cystine knot proteins, bursicon α (burs α) and bursicon β (burs β), that elicits cuticle tanning (melanization and sclerotization) through the Drosophila leucine-rich repeats-containing G protein-coupled receptor 2 (DLGR2). Recent studies show that both bursicon subunits also form homodimers. However, biological functions of the homodimers have remained unknown until now.&lt;h4>Methodology/principal findings&lt;/h4>In this report, we show in Drosophila melanogaster that both bursicon homodimers induced expression of genes encoding antimicrobial peptides (AMPs) in neck-ligated adults following recombinant homodimer injection and in larvae fat body after incubation with recombinant homodimers. These AMP genes were also up-re</pubmed_abstract><journal>PloS one</journal><pagination>e34510</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3314635</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Insect neuropeptide bursicon homodimers induce innate immune and stress genes during molting by activating the NF-κB transcription factor Relish.</pubmed_title><pmcid>PMC3314635</pmcid><pubmed_authors>Wang Q</pubmed_authors><pubmed_authors>Li S</pubmed_authors><pubmed_authors>Song Q</pubmed_authors><pubmed_authors>Gilbert LI</pubmed_authors><pubmed_authors>Stanley D</pubmed_authors><pubmed_authors>Dong S</pubmed_authors><pubmed_authors>An S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Insect neuropeptide bursicon homodimers induce innate immune and stress genes during molting by activating the NF-κB transcription factor Relish.</name><description>&lt;h4>Background&lt;/h4>Bursicon is a heterodimer neuropeptide composed of two cystine knot proteins, bursicon α (burs α) and bursicon β (burs β), that elicits cuticle tanning (melanization and sclerotization) through the Drosophila leucine-rich repeats-containing G protein-coupled receptor 2 (DLGR2). Recent studies show that both bursicon subunits also form homodimers. However, biological functions of the homodimers have remained unknown until now.&lt;h4>Methodology/principal findings&lt;/h4>In this report, we show in Drosophila melanogaster that both bursicon homodimers induced expression of genes encoding antimicrobial peptides (AMPs) in neck-ligated adults following recombinant homodimer injection and in larvae fat body after incubation with recombinant homodimers. These AMP genes were also up-re</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012</publication><modification>2025-04-21T22:48:23.024Z</modification><creation>2019-03-26T23:12:54Z</creation></dates><accession>S-EPMC3314635</accession><cross_references><pubmed>22470576</pubmed><doi>10.1371/journal.pone.0034510</doi></cross_references></HashMap>