期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 404, 期 2, 页码 638-645出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2010.12.030
关键词
Prion protein; Drosophila; Polyglutamine; Oxidative stress; ER stress; Autophagy
资金
- Korean Government [20080401-034016, (MOEHRD) (KRF-2006-521-E00103)]
To investigate the in vivo functions of normal prion protein (PrP) in Drosophila, we utilized characterized transgenic flies expressing 3F4-tagged mouse PrP (Mo-PrP3F4). The neurotoxicity of pathogenic Machado-Joseph Disease (MJD) glutamine (Q) 78 and 127Q proteins were enhanced by the co-expression of Mo-PrP3F4 in the fly eyes, while the eyes of controls flies and flies expressing Mo-PrP3F4 alone or together with MJD-Q27 or 20Q proteins did not show any defect. Susceptibilities to H2O2, paraquat, and Dithiothreitol (DTT) were altered in Mo-PrP3F4 flies. In addition, Mo-PrP3F4 flies were significantly more susceptible to the perturbation of autophagy signaling by an autophagy inhibitor, 3-methyladenine (3-MA), and inducer, LiCl. Taken together, our data suggest that Mo-PrP3F4 may enhance the neurotoxicity of pathogenic Poly-Q proteins by perturbing oxidative and autophagy signaling. (C) 2010 Elsevier Inc. All rights reserved.
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