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- Bing Gong, Zixuan Cao, Ping Zheng, Ottavio V Vitolo, Shumin Liu, Agnieszka Staniszewski, Donna Moolman, Hong Zhang, Michael Shelanski, and Ottavio Arancio.
- Department of Pathology and Taub Institute, Columbia University, New York, NY 10032, USA.
- Cell. 2006 Aug 25; 126 (4): 775-88.
AbstractThe neuronal ubiquitin/proteasomal pathway has been implicated in the pathogenesis of Alzheimer's disease (AD). We now show that a component of the pathway, ubiquitin C-terminal hydrolase L1 (Uch-L1), is required for normal synaptic and cognitive function. Transduction of Uch-L1 protein fused to the transduction domain of HIV-transactivator protein (TAT) restores normal enzymatic activity and synaptic function both in hippocampal slices treated with oligomeric Abeta and in the APP/PS1 mouse model of AD. Moreover, intraperitoneal injections with the fusion protein improve the retention of contextual learning in APP/PS1 mice over time. The beneficial effect of the Uch-L1 fusion protein is associated with restoration of normal levels of the PKA-regulatory subunit IIalpha, PKA activity, and CREB phosphorylation.
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