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棉铃虫滞育蛹头部蛋白质组分析及其变化

Analysis of pupal head proteome and its alteration in diapausing pupae of Helicoverpa armigera.

机构信息

Hubei Insect Resources Utilization and Sustainable Pest Management Key Laboratory, College of Plant Science & Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, China.

出版信息

J Insect Physiol. 2010 Mar;56(3):247-52. doi: 10.1016/j.jinsphys.2009.10.008. Epub 2009 Oct 30.

DOI:10.1016/j.jinsphys.2009.10.008
PMID:19852966
Abstract

The proteomic approach has proven to be an useful tool for understanding insect diapause processes. Using 2D gel electrophoresis and matrix assisted laser/desorption ionization (MALDI) time of flight (TOF), we identified 24 proteins in the head of Helicoverpa armigera pupae with diverse functional characteristics, including cytoskeleton proteins, heat-shock proteins, insect development regulation factors, ATPases, proteins regulating signal pathway and enzymes involved in metabolism, etc. A proteomic comparison between nondiapausing and diapausing pupae revealed three proteins that were present only in nondiapausing pupae, and six proteins represented >or=2.0-fold or <or=0.5-fold changes. The differentially expressed proteins, including heat-shock protein 90, chitin deacetylase, alpha-tubulin and transitional endoplasmic reticulum ATPase, etc. were reported for the first time in H. armigera. Identification of these proteins will enable us to further characterize the regulated functions of diapause in this important species.

摘要

蛋白质组学方法已被证明是理解昆虫滞育过程的有用工具。通过使用二维凝胶电泳和基质辅助激光解吸/电离(MALDI)飞行时间(TOF),我们鉴定了 24 种具有不同功能特性的蛋白质,包括细胞骨架蛋白、热休克蛋白、昆虫发育调节因子、ATP 酶、参与代谢的信号通路调节蛋白和酶等。非滞育和滞育蛹之间的蛋白质组比较显示,有三种蛋白质仅存在于非滞育蛹中,有六种蛋白质的表达水平变化大于或等于 2.0 倍或小于或等于 0.5 倍。差异表达的蛋白质,包括热休克蛋白 90、几丁质脱乙酰酶、α-微管蛋白和过渡型内质网 ATP 酶等,在 H. armigera 中是首次报道。这些蛋白质的鉴定将使我们能够进一步描述这个重要物种中滞育的调节功能。

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