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Cytosolic PrP induces apoptosis of cell by disrupting microtubule assembly.
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- Author(s): Li XL;Li XL; Wang GR; Jing YY; Pan MM; Dong CF; Zhou RM; Wang ZY; Shi Q; Gao C; Dong XP
- Source:
Journal of molecular neuroscience : MN [J Mol Neurosci] 2011 Mar; Vol. 43 (3), pp. 316-25. Date of Electronic Publication: 2010 Sep 14.- Publication Type:
Journal Article; Research Support, Non-U.S. Gov't- Language:
English - Source:
- Additional Information
- Source: Publisher: Humana Press Country of Publication: United States NLM ID: 9002991 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1559-1166 (Electronic) Linking ISSN: 08958696 NLM ISO Abbreviation: J Mol Neurosci Subsets: MEDLINE
- Publication Information: Publication: Totowa, NJ : Humana Press
Original Publication: Boston : Birkhäuser [i.e. Cambridge, MA : Birkhäuser Boston, c1989- - Subject Terms:
- Abstract: Prion protein (PrP) is able to bind with tubulin and to interfere with the formation of microtubule. To investigate the influence of accumulation of cytosolic PrP in cytoplasm on microtubule, plasmid pcDNA3.1-PrP23-230 expressing human PrP23-230 was introduced into HeLa cells. Immunoprecipitation assays identified the molecular interaction between cytosolic PrP and cellular tubulin. Confocal microscopy showed the co-localization of the expressed cytosolic PrP with tubulin in cytoplasm. Immunofluorescent assays of tubulin illustrated remarkable disruption of microtubular structures in the cells accumulated with cytosolic PrP. Meanwhile, the expressed cytosolic PrP significantly reduced cell viability and induced cell apoptosis. The amounts of microtubule protein in the cells expressing cytosolic PrP were decreased. Moreover, the levels of endogenous tubulin in the brain tissues of scrapie-infected hamsters were significantly lower than that of normal one. It highlights a close linkage between disruption of microtubule framework and cell death caused by abnormal presence of cellular PrP in cytoplasm. The association of apoptosis with microtubule-disrupting activity caused by cytosolic PrP may further provide insight into the unresolved biological function of PrP in the neurons.
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- Publication Date: Date Created: 20100915 Date Completed: 20110721 Latest Revision: 20211020
- Publication Date: 20231215
- Accession Number: 10.1007/s12031-010-9443-9
- Accession Number: 20838930
- Source:
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