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- W2008810519 abstract "Motor and cognitive deficits in Huntington's disease (HD) are likely caused by progressive neuronal dysfunction preceding neuronal cell death. Synapsin I is one of the major phosphoproteins regulating neurotransmitter release. We report here an abnormal phosphorylation state of synapsin I in the striatum and the cerebral cortex of R6/2 transgenic mice expressing the HD mutation. These changes are mostly characterized by an early overphosphorylation at sites 3-5, whereas phosphorylation at site 1 remains unchanged and at site 6 becomes reduced only close to the end stage of the disease. Such changes do not result from modification in protein expression levels. However, we show a decreased expression of the calcineurin regulatory subunit-B, which may contribute to an imbalance between kinase and phosphatase activities. Together the results suggest that an early impairment in synapsin phosphorylation-dephosphorylation may alter synaptic vesicle trafficking and lead to defective neurotransmission in HD." @default.
- W2008810519 created "2016-06-24" @default.
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- W2008810519 date "2002-08-01" @default.
- W2008810519 modified "2023-10-13" @default.
- W2008810519 title "Abnormal Phosphorylation of Synapsin I Predicts a Neuronal Transmission Impairment in the R6/2 Huntington's Disease Transgenic Mice" @default.
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- W2008810519 doi "https://doi.org/10.1006/mcne.2002.1152" @default.
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