Journal
NEUROSCIENCE LETTERS
Volume 449, Issue 2, Pages 87-92Publisher
ELSEVIER IRELAND LTD
DOI: 10.1016/j.neulet.2008.06.015
Keywords
Protein transduction domain; Antennapedia; TAT; Aggregate inhibition; Neurodegeneration; Polyglutamine; Huntington disease
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Funding
- Ministry of Health, Labor, and Welfare, japan
- Ichiro Kanehara Foundation, Japan
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The polyglutamine (polyQ) diseases are neurodegenerative diseases caused by proteins with an abnormally expanded polyQ stretch, which triggers abnormal aggregation of these proteins in the brain. We previously showed that the polyQ-binding peptide QBP1 inhibits polyQ aggregation, and further that administration of QBP1 fused with a protein transduction domain (PTD) suppresses polyQ-induced neurodegeneration in Drosophila. As the next step towards developing a therapy using QBP1, we investigated the delivery of PTD-QBP1 to the mouse brain upon its administration. Here we successfully detected delivery of PTD QBP1 into mouse brain cells upon its single intracerebroventricular injection. In addition, long-term administration of PTD-QBP1 to polyQ disease mice in proved their weight loss phenotype, suggesting a possible therapeutic effect. Our study indicates the potential of PTD-mediated delivery of QBP1 as a therapeutic strategy for the Currently untreatable polyQ diseases. (C) 2008 Elsevier Ireland Ltd. All rights reserved.
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