Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 37, Issue 5, Pages 643-653Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.freeradbiomed.2004.05.019
Keywords
Cu/Zn superoxide dismutase 1; transgenic mice; hippocampus; two-dimensional gel electrophoresis; neuronal proteins; mitochondrial protein; free radicals
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Mutations of Cu/Zn superoxide dismutase I (SOD1), a metalloenzyme catalyzing the conversion of superoxide anion to hydrogen peroxide (H2O2), are linked to motor neuron degeneration. Transgenic mouse strains overexpressing wild-type human SOD1 (Tg-SOD1) were shown to have mitochondrial swelling, vacuolization, or learning and memory deficits and are widely used for biochemical, genetic, and cognitive studies; this, along with the advent of advanced proteomic methods, made us investigate protein expression in hippocampus. Hippocampal tissues of wild-type, hemizygous, and homozygous Tg-SOD1 mice were isolated and used for two-dimensional gel electrophoresis with subsequent matrix-assisted laser desorption/ionization-time of flight identification. We identified several synaptosomal, neuronal, antioxidant, and mitochondrial proteins in hippocampus, and expression levels of syntaxin-binding protein 1, N-ethylmaleimide-sensitive factor, synaptosomal-associated protein 25, dynamin-1, neurofilament triplet L protein, neurofilament triplet M protein, neuronal tropomodulin, and neuronal protein 25 were significantly decreased in Tg-SOD1. None of the antioxidant proteins were altered except mouse SOD1. Mitochondrial ATP synthase alpha/beta chain and elongation factor Tu were aberrant in Tg-SOD1 We conclude that derangement of neuronal and mitochondrial proteins may indicate synaptosomal and neuronal loss in Tg-SOD1 hippocampus, already reported in morphological terms. This observation is of relevance to understanding brain deficits in Down syndrome, as SOD1 is encoded on chromosome 21. (C) 2004 Elsevier Inc. All rights reserved.
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