Research Papers: Gerotarget (Focus on Aging):
Human prion protein-induced autophagy flux governs neuron cell damage in primary neuron cells
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Ji-Hong Moon1, Ju-Hee Lee1, Uddin MD. Nazim1, You-Jin Lee1, Jae-Won Seol1, Seong-Kug Eo1, John-hwa Lee1 and Sang-Youel Park1
1 Biosafety Research Institute, College of Veterinary Medicine, Chonbuk National University, Iksan, Jeonbuk, South Korea
Sang-Youel Park, email:
Keywords: prion protein; autophagy flux; neurodegeneration; PrPc; ATG5; Gerotarget
Received: January 01, 2016 Accepted: April 13, 2016 Published: April 19, 2016
An unusual molecular structure of the prion protein, PrPsc is found only in mammals with transmissible prion diseases. Prion protein stands for either the infectious pathogen itself or a main component of it. Recent studies suggest that autophagy is one of the major functions that keep cells alive and has a protective effect against the neurodegeneration. In this study, we investigated that the effect of human prion protein on autophagy-lysosomal system of primary neuronal cells. The treatment of human prion protein induced primary neuron cell death and decreased both LC3-II and p62 protein amount indicating autophagy flux activation. Electron microscope pictures confirmed the autophagic flux activation in neuron cells treated with prion protein. Inhibition of autophagy flux using pharmacological and genetic tools prevented neuron cell death induced by human prion protein. Autophagy flux induced by prion protein is more activated in prpc expressing cells than in prpc silencing cells. These data demonstrated that prion protein-induced autophagy flux is involved in neuron cell death in prion disease and suggest that autophagy flux might play a critical role in neurodegenerative diseases including prion disease.
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