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• W2070795929 abstract "A common feature of CAG-expansion neurodegenerative diseases is the presence of intranuclear aggregates in neuronal cells. We have used a synthetic fusion protein containing at the NH2 terminus the influenza hemoagglutinin epitope (HA), a polyglutamine stretch (polyQ) of various size (17, 36, 43 CAG) and a COOH tail encoding the green fluorescent protein (GFP). The fusion proteins were expressed in COS-7 and neuroblastoma SK-N-BE cells. We found that the formation of aggregates largely depends on the length of polyglutamine tracts and on the levels of expression of the fusion protein. Moreover, transglutaminase overexpression caused an increase of insoluble aggregates only in cells expressing the mutant expanded protein. Conversely, treatment of cells with cystamine, a transglutaminase inhibitor, reduced the percentage of aggregates. We found also that the inhibition of the proteasome ubiquitin-dependent degradation increased the formation of intranuclear aggregates. These data suggest that length of polyglutamine tract, its expression, unbalance between cellular transglutaminase activity, and the ubiquitin-degradation pathway are key factors in the formation of intranuclear aggregates." @default.
• W2070795929 created "2016-06-24" @default.
• W2070795929 creator A5004489427 @default.
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• W2070795929 date "1999-06-01" @default.
• W2070795929 modified "2023-10-13" @default.
• W2070795929 title "The Length of Polyglutamine Tract, Its Level of Expression, the Rate of Degradation, and the Transglutaminase Activity Influence the Formation of Intracellular Aggregates" @default.
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• W2070795929 doi "https://doi.org/10.1006/bbrc.1999.0851" @default.
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