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Cell Journal، جلد ۱۳، شماره Supplement، صفحات ۰-۰
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عنوان انگلیسی P-54: Study of dNTPs Effects on Alpha-SynuClein Fibril Formation (Amyloidosis
چکیده انگلیسی مقاله Objecive: Several diseases which associated with accumulation of protein aggregation named fibrillar amyloid. Alpha synuclein protein (ASN) is present in brain and consists of protein plaques as a main part in lewy body diseases (including Parkinson's, Lewy body variant of Alzheimer's (LBV), and others). Wild type and mutated ASN can fibrillate in physiological condition. Materials and Method: Here we investigated the effect of dNTPs as natural small aromatic molecules on ASN fibrillation. Recombinant ASN protein was produced and fibrillate by agitation with fixed speed at 37°C. The fibrils were examined by ThT fluorescence, Congo red, CD, TEM and fluorescence image. Fibrils were cytotoxic for SK-N-MC cell. We explored their cytotoxicity by MTT, LDH, and Annexin assay. Results: Presence of fibrils and prefibrils in cell culture, enhanced cell death dramatically. The study showed that dNTPs have different effects on fibril formation. Adding dCTP and dTTP could inhibit fibrillation whereas dATP and dGTP had opposite effect. It seems that pyrimidines derivatives can interrupt fibril formation, but purine ones could not.Results were incredible by adding fibrils in present of dNTP to cell culture. Although adding dCTP and dTTP inhibit formation of mature fibril but, incubation with these dNTPs caused cell cytotoxicity even more than ASN fibril. While the aggregation types of ASN after adding dATP and dGTP had less dangerous effect on cell. Conclusion: It seems that addition of pyrimidines can produce more perilous type of prefibrils like oligomers. Purines not only induce mature fibrils but also make amorphous forms which have less serious effect on cell viability.
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نشانی اینترنتی http://celljournal.org/journal/article/abstract/1586
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