<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>44(2)</volume><submitter>Hu X</submitter><pubmed_abstract>Eicosanoids are crucial downstream signals in the insect immune responses. Phospholipase A2 (PLA2) catalyzes phospholipids, the initial step in eicosanoid biosynthesis. In mammals, the biological roles of &lt;i>Ca&lt;sup>2+&lt;/sup>-independent Phospholipase A2 (iPLA2)&lt;/i> have been extensively studied; however, only a few studies have attempted to explore &lt;i>iPLA2&lt;/i> functions in insects. In this study, we identified two &lt;i>iPLA2&lt;/i> genes (designated as &lt;i>BmiPLA2A&lt;/i> and &lt;i>BmiPLA2B&lt;/i>) in the silkworm, &lt;i>Bombyx mori&lt;/i>. &lt;i>BmiPLA2A&lt;/i> had a 2427 base pair (bp) open reading frame (ORF) that coded for a protein with 808 amino acids. In contrast, &lt;i>BmiPLA2B&lt;/i> had a 1731 bp ORF that coded for a protein with 576 amino acids. Domain analysis revealed that BmiPLA2A had six ankyrin repeat domains, but BmiPLA2B lacks these domains. &lt;i>BmiPLA2A&lt;/i> and &lt;i>BmiPLA2B&lt;/i> were transcribed widely in various tissues and developmental stages with different expression patterns. The administration of 20-hydroxyecdysone increased their expression levels in the epidermis and hemocytes. Furthermore, challenged with virus, fungus, Gram-negative bacteria, and Gram-positive bacteria induced the expression of &lt;i>BmiPLA2A&lt;/i> and &lt;i>BmiPLA2B&lt;/i> with variable degrees along with different time points. Our findings imply that &lt;i>BmiPLA2A&lt;/i> and &lt;i>BmiPLA2B&lt;/i> may have important biological roles in the development and innate immunity of &lt;i>B. mori&lt;/i>.</pubmed_abstract><journal>Current issues in molecular biology</journal><pagination>777-790</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8929031</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Molecular Characterization of Two Genes Encoding Novel Ca&lt;sup>2+&lt;/sup>-Independent Phospholipase A2s from the Silkworm, &lt;i>Bombyx mori&lt;/i>.</pubmed_title><pmcid>PMC8929031</pmcid><pubmed_authors>Zheng X</pubmed_authors><pubmed_authors>Ji H</pubmed_authors><pubmed_authors>Feng K</pubmed_authors><pubmed_authors>Zhu Y</pubmed_authors><pubmed_authors>Hu X</pubmed_authors><pubmed_authors>Gul I</pubmed_authors><pubmed_authors>Cui H</pubmed_authors><pubmed_authors>Abbas MN</pubmed_authors><pubmed_authors>Zhang B</pubmed_authors></additional><is_claimable>false</is_claimable><name>Molecular Characterization of Two Genes Encoding Novel Ca&lt;sup>2+&lt;/sup>-Independent Phospholipase A2s from the Silkworm, &lt;i>Bombyx mori&lt;/i>.</name><description>Eicosanoids are crucial downstream signals in the insect immune responses. Phospholipase A2 (PLA2) catalyzes phospholipids, the initial step in eicosanoid biosynthesis. In mammals, the biological roles of &lt;i>Ca&lt;sup>2+&lt;/sup>-independent Phospholipase A2 (iPLA2)&lt;/i> have been extensively studied; however, only a few studies have attempted to explore &lt;i>iPLA2&lt;/i> functions in insects. In this study, we identified two &lt;i>iPLA2&lt;/i> genes (designated as &lt;i>BmiPLA2A&lt;/i> and &lt;i>BmiPLA2B&lt;/i>) in the silkworm, &lt;i>Bombyx mori&lt;/i>. &lt;i>BmiPLA2A&lt;/i> had a 2427 base pair (bp) open reading frame (ORF) that coded for a protein with 808 amino acids. In contrast, &lt;i>BmiPLA2B&lt;/i> had a 1731 bp ORF that coded for a protein with 576 amino acids. Domain analysis revealed that BmiPLA2A had six ankyrin repeat domains, but BmiPLA2B lacks these domains. &lt;i>BmiPLA2A&lt;/i> and &lt;i>BmiPLA2B&lt;/i> were transcribed widely in various tissues and developmental stages with different expression patterns. The administration of 20-hydroxyecdysone increased their expression levels in the epidermis and hemocytes. Furthermore, challenged with virus, fungus, Gram-negative bacteria, and Gram-positive bacteria induced the expression of &lt;i>BmiPLA2A&lt;/i> and &lt;i>BmiPLA2B&lt;/i> with variable degrees along with different time points. Our findings imply that &lt;i>BmiPLA2A&lt;/i> and &lt;i>BmiPLA2B&lt;/i> may have important biological roles in the development and innate immunity of &lt;i>B. mori&lt;/i>.</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Feb</publication><modification>2024-11-20T17:20:55.099Z</modification><creation>2024-11-20T17:20:55.099Z</creation></dates><accession>S-EPMC8929031</accession><cross_references><pubmed>35723339</pubmed><doi>10.3390/cimb44020054</doi></cross_references></HashMap>