The octarepeat region of hamster PrP (PrP51-91) enhances the formation of microtubule and antagonize Cu(2+)-induced microtubule-disrupting activity

Prion protein (PrP) is considered to associate with microtubule and its major component, tubulin. In the present study, octarepeat region of PrP (PrP51-91) was expressed in prokaryotic-expressing system. Using GST pull-down assay and co-immunoprecipitation, the molecular interaction between PrP51-91...

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Bibliographic Details
Published in:Acta biochimica et biophysica Sinica 2009-11, Vol.41 (11), p.929-937
Main Authors: Li, Xiaoli, Dong, Chenfang, Shi, Song, Wang, Guirong, Li, Yuan, Wang, Xin, Shi, Qi, Tian, Chan, Zhou, Ruimin, Gao, Chen, Dong, Xiaoping
Format: Article
Language:English
Subjects:
Animals
Cells, Cultured
Copper - pharmacology
Cricetinae
Microtubules - drug effects
Peptide Fragments - physiology
Prions - physiology
Repetitive Sequences, Nucleic Acid
Tubulin - metabolism
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Summary:Prion protein (PrP) is considered to associate with microtubule and its major component, tubulin. In the present study, octarepeat region of PrP (PrP51-91) was expressed in prokaryotic-expressing system. Using GST pull-down assay and co-immunoprecipitation, the molecular interaction between PrP51-91 and tubulin was observed. Our data also demonstrated that PrP51-91 could efficiently stimulate microtubule assembly in vitro, indicating a potential effect of PrP on microtubule dynamics. Moreover, PrP51-91 was confirmed to be able to antagonize Cu(2+)-induced microtubule-disrupting activity in vivo, partially protecting against Cu(2+) intoxication to culture cells and stabilize cellular microtubule structure. The association of the octarepeat region of PrP with tubulin may further provide insight into the biological function of PrP in the neurons.
ISSN:1745-7270