α-synuclein

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O-GlcNAcylation Regulates Dopamine Neuron Function, Survival and Degeneration in Parkinson Disease

The dopamine system in the midbrain is essential for volitional movement, action selection, and reward-related learning. Despite its versatile roles, it contains only a small set of neurons in the brainstem. These dopamine neurons are especially susceptible to Parkinson's disease and prematurely degenerate in the course of disease progression, while the discovery of new therapeutic [...]

December 1st, 2020|Tags: , , |

O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson’s disease

Several aggregation-prone proteins associated with neurodegenerative diseases can be modified by O-linked N-acetyl-glucosamine (O-GlcNAc) in vivo. One of these proteins, α-synuclein, is a toxic aggregating protein associated with synucleinopathies, including Parkinson's disease. However, the effect of O-GlcNAcylation on α-synuclein is not clear. Here, we use synthetic protein chemistry to generate both unmodified α-synuclein and α-synuclein [...]

October 12th, 2015|Tags: , , |

O-GlcNAc modification prevents peptide-dependent acceleration of α-synuclein aggregation

Sweet relief: the Parkinson's disease-associated protein α-synuclein is post-translationally modified by N-acetylglucosamine (O-GlcNAc), but the biochemical consequences are unknown. Here we show that an O-GlcNAc-modified peptide does not participate in α-synuclein aggregation, thus suggesting that O-GlcNAc might directly inhibit aggregation in cells. Source: Marotta, N.P. et al. Chembiochem 13(18), 2665-2670 (2012).

November 9th, 2012|Tags: , , |