Storage proteins (SPs) are hexameric macromolecular protein, an important component of insect serum protein, which plays a variety of roles in insect metamorphosis and development. However, their regulatory mechanisms remain unclear. Our previous studies revealed that the expression of SPs is regulated by nutritional signals and identified FoxO as a negative regulator of SPs in the silkworm Bombyx mori (B. mori). In this study, amino acids upregulated BmSP expression, whereas Rapamycin downregulated it in fat body cultured in vitro. Rapamycin also reduced BmSP expression in B. mori larvae. Overexpression of the nutrient transcription factor GATA family in BmE cells revealed that only BmGATAβ4 significantly upregulated BmSP expression. Furthermore, the amino acid-mTOR signaling pathway modulated BmGATAβ4 expression. Overexpression of BmGATAβ4 resulted in increased BmSP expression in B. mori larvae. Luciferase reporter assays, electrophoretic mobility shift assays, and chromatin immunoprecipitation identified GATA-like CRE 1-1 and GATA-like CRE 2-2 of the BmSP1 promoter as binding sites for BmGATAβ4. These findings provide new insights into the regulation of nutrient protein expression in insects.
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http://dx.doi.org/10.1016/j.ijbiomac.2025.139943 | DOI Listing |
Int J Biol Macromol
January 2025
Integrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, Biological Science Research Center, Southwest University, Chongqing 400715, China. Electronic address:
Storage proteins (SPs) are hexameric macromolecular protein, an important component of insect serum protein, which plays a variety of roles in insect metamorphosis and development. However, their regulatory mechanisms remain unclear. Our previous studies revealed that the expression of SPs is regulated by nutritional signals and identified FoxO as a negative regulator of SPs in the silkworm Bombyx mori (B.
View Article and Find Full Text PDFJ Mol Evol
August 2024
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo, Tokyo, 113-8657, Japan.
Pif is a shell matrix protein (SMP) identified in the nacreous layer of Pinctada fucata (Pfu) comprised two proteins, Pif97 and Pif 80. Pif97 contains a von Willebrand factor A (VWA) and chitin-binding domains, whereas Pif80 can bind calcium carbonate crystals. The VWA domain is conserved in the SMPs of various mollusk species; however, their phylogenetic relationship remains obscure.
View Article and Find Full Text PDFInsect Biochem Mol Biol
October 2022
State Key Laboratory of Silkworm Genome Biology, Southwest University, Beibei, Chongqing, 400715, China; Biological Science Research Center, Southwest University, Beibei, Chongqing, 400715, China; Chongqing Key Laboratory of Sericulture, Southwest University, Chongqing, 400716, China. Electronic address:
Insect serum proteins, also termed storage proteins (SPs), are hexamer proteins that form amino acid reservoirs important for the development of pupae and embryos in most insects. In this study, we investigated the SP genes expression and regulation pathways in silkworms (Bombyx mori). We observed that B.
View Article and Find Full Text PDFInsect Mol Biol
February 2021
Institute of Environment and Plant Protection, Chinese Academy of Tropical Agricultural Sciences, Haikou, China.
Antifungal innate immunity is an important defence used by insects against entomogenous fungi. However, the downstream target antifungal peptides of different immune signalling pathways are unknown. We found that the Toll, Janus kinase/signal transducer and activator of transcription (Jak/STAT) and Immunodeficiency (IMD) signalling pathways in the silkworm, Bombyx mori, can be activated by Beauveria bassiana.
View Article and Find Full Text PDFMol Ther Nucleic Acids
December 2019
School of Medical Laboratory and Department of Cell Biology, Tianjin Medical University, Tianjin 300070, China. Electronic address:
Insufficient delivery of oligonucleotides to muscle and heart remains a barrier for clinical implementation of antisense oligonucleotide (AO)-mediated exon-skipping therapeutics in Duchenne muscular dystrophy (DMD), a lethal monogenic disorder caused by frame-disrupting mutations in the DMD gene. We previously demonstrated that hexose, particularly an equal mix of glucose:fructose (GF), significantly enhanced oligonucleotide delivery and exon-skipping activity in peripheral muscles of mdx mice; however, its efficacy in the heart remains limited. Here we show that co-administration of GF with peptide-conjugated phosphorodiamidate morpholino oligomer (PPMO, namely, BMSP-PMO) induced an approximately 2-fold higher level of dystrophin expression in cardiac muscles of adult mdx mice compared to BMSP-PMO in saline at a single injection of 20 mg/kg, resulting in evident phenotypic improvement in dystrophic mdx hearts without any detectable toxicity.
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