Protein aggregation containing beta-amyloid, alpha-synuclein and hyperphosphorylated tau in cultured cells of hippocampus, substantia nigra and locus coeruleus after rotenone exposure

• Main Authors: Martins Stephanie A, Melo Thaiany Q, Chaves Rodrigo S, Ferrari Merari FR
• Format: Article
• Language: English
• Published: BMC 2010-11-01
• Series: BMC Neuroscience
• Online Access: http://www.biomedcentral.com/1471-2202/11/144

<p>Abstract</p> <p>Background</p> <p>Protein aggregates containing alpha-synuclein, beta-amyloid and hyperphosphorylated tau are commonly found during neurodegenerative processes which is often accompanied by the impairment of mitochondrial complex I respiratory chain and dysfunction of cellular systems of protein degradation. In view of this, we aimed to develop an <it>in vitro </it>model to study protein aggregation associated to neurodegenerative diseases using cultured cells from hippocampus, locus coeruleus and substantia nigra of newborn Lewis rats exposed to 0.5, 1, 10 and 25 nM of rotenone, which is an agricultural pesticide, for 48 hours.</p> <p>Results</p> <p>We demonstrated that the proportion of cells in culture is approximately the same as found in the brain nuclei they were extracted from. Rotenone at 0.5 nM was able to induce alpha-synuclein and beta amyloid aggregation, as well as increased hyperphosphorylation of tau, although high concentrations of this pesticide (over 1 nM) lead cells to death before protein aggregation. We also demonstrated that the 14kDa isoform of alpha-synuclein is not present in newborn Lewis rats.</p> <p>Conclusion</p> <p>Rotenone exposure may lead to constitutive protein aggregation <it>in vitro</it>, which may be of relevance to study the mechanisms involved in idiopathic neurodegeneration.</p>