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Long non-coding RNAs (lncRNAs) are of particular interest because of their contributions to many biological processes. Here, we present the genome-wide identification and characterization of putative lncRNAs in a global insect pest, Plutella xylostella . A total of 8096 lncRNAs were identified and classified into three groups. The average length of exons in lncRNAs was longer than that in coding genes and the GC content was lower than that in mRNAs. Most lncRNAs were flanked by canonical splice sites, similar to mRNAs. Expression profiling identified 114 differentially expressed lncRNAs during the DBM development and found that majority were temporally specific. While the biological functions of lncRNAs remain uncharacterized, many are microRNA precursors or competing endogenous RNAs involved in micro-RNA regulatory pathways. This work provides a valuable resource for further studies on molecular bases for development of DBM and lay the foundation for discovery of lncRNA functions in P. xylostella . [ABSTRACT FROM AUTHOR]

Abstract: Secreted phospholipase A2s form a large family of proteins involved in diverse biological and pathophysiological processes. Group IIE secreted phospholipase A2 (sPLA2-IIE) is one of the latest discovered members of this family. Previous studies revealed that the expression profile of sPLA2-IIE was restricted to a few tissue types including brain, heart, lung and placenta compared to the broad expression profile of other isoforms. Accumulating evidence suggests that sPLA2-IIE might play a pivotal role in the progression of inflammatory processes. However, functional study of sPLA2-IIE was hindered by the low yield of soluble expressed protein. In this study, we have expressed human and mouse sPLA2-IIE in Escherichia coli in the form of inclusion bodies. The inclusion bodies were dissolved, purified and refolded in a step-wise dialysis approach and further purified. We obtained soluble and active proteins for human and mouse sPLA2-IIE with a final yield of 1.1 and 1.2mg/500mL bacterial culture, respectively. The refolded sPLA2-IIEs exhibited similar calcium and pH dependence of their enzymatic activity with those expressed in COS cells. This protein expression and purification protocol will facilitate the further structural and functional studies of human and mouse sPLA2-IIEs. [Copyright &y& Elsevier]