Proteomic analysis of spinal cord of presymptomatic amyotrophic lateral sclerosis G93A SOD1 mouse

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• 作者：Tania Massignan ; Filippo Casoni ; Manuela Basso ; Paola Stefanazzi ; Emiliano Biasini ; Massimo Tortarolo ; Mario Salmona ; Elisabetta Gianazza ; Caterina Bendotti ; Valentina Bonetto
• 关键词：Amyotrophic lateral sclerosis ; Transgenic mice ; Superoxide dismutase 1 ; Proteomics ; Two-dimensional gel electrophoresis ; Cyclophilin A ; Acetylation ; Phosphorylation
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2007
• 出版时间：16 February 2007
• 年：2007
• 卷：353
• 期：3
• 页码：719-725
• 全文大小：414 K

文摘

Amyotrophic lateral sclerosis (ALS) is a fatal motor neuron disease, whose primary mechanisms or causes are still not defined and for which no effective treatment is available. We have recently reported that before disease onset the level of tyrosine nitrated proteins is increased in the G93A SOD1 transgenic mouse model of ALS. In the present investigation, we carried out a proteomic analysis of spinal cord extracts from G93A SOD1 mice at the presymptomatic stage of the disease to further unravel primary events in the pathogenesis and tentatively screen for potential pharmacological targets. Using a robust two-dimensional gel electrophoresis-based proteomic approach, we detected a number of proteins differentially represented in presymptomatic mice in comparison with controls. Alterations of these proteins correlate with mitochondrial dysfunction, aggregation, and stress response. Moreover, we found a variation in the isoform pattern of cyclophilin A, a molecular chaperone that protects cells from the oxidative stress.