Knockdown of specific cuticular proteins analogous to peritrophin 3 genes disrupt larval and ovarian development in Bactrocera dorsalis (Diptera: Tephritidae)

Cuticular proteins (CPs) are critical components of the insect cuticle and play important roles in maintaining normal insect development and defense against various environmental stresses. The oriental fruit fly (Bactrocera dorsalis) is one of the most destructive pests worldwide, and its eight CPs analogous to peritrophin 3 (BdCPAP3) family genes have been identified in our previous study. In the present study, we further explored the possible roles of CPAP3 genes in B. dorsalis development. Each sequence of BdCPAP3 genes contained three conserved ChtBD2 (chitin-binding) domains. Spatial and temporal expression patterns revealed that the four BdCPAP3 genes (BdCPAP3-A1, B, E, and E2) might play important roles in larval pupariation of B. dorsalis. Moreover, treatment with a juvenile hormone analog (methoprene) significantly restricted expression of these four CPAP3 genes, whereas treatment with 20-hydroxy-ecdysone induced expression. The RNA interference (RNAi) results revealed that down-regulated CPAP3 genes led to significant delay of pupariation, and injection of dsBdCPAP3-E into 5-d-old B. dorsalis larvae caused approximately 40% mortality. Interestingly, we also confirmed that BdCPAP3-D2 was involved in B. dorsalis ovarian development. This study showed that some specific CPAP3 genes had crucial roles in B. dorsalis development, and these CP genes could be used as potential targets to control this pest via RNAi.     

Neprilysin gene expression requires binding of the amyloid precursor protein intracellular domain to its promoter: implications for Alzheimer disease

Amyloid β‐peptide (Aβ) accumulation leads to neurodegeneration and Alzheimer disease; however, amyloid metabolism is a dynamic process and enzymic mechanisms exist for Aβ removal. Considerable controversy surrounds whether the intracellular domain of the amyloid precursor protein (AICD) regulates expression of the Aβ‐degrading metalloprotease, neprilysin (NEP). By comparing two neuroblastoma cell lines differing substantially in NEP expression, we show by chromatin immunoprecipitation (ChIP) that AICD is bound directly to the NEP promoter in high NEP‐expresser (NB7) cells but not in low‐expresser (SH‐SY5Y) cells. The methylation status of the NEP promoter does not regulate expression in these cells, whereas the histone deacetylase inhibitors trichostatin A and valproate partly restore NEP expression and activity in SH‐SY5Y cells. ChIP analysis also reveals AICD binding to the NEP promoter in rat primary neurons but not in HUVEC cells. Chromatin remodelling of crucial Alzheimer disease‐related genes by valproate could provide a new therapeutic strategy.