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Confocal Microscopy Evidence of Prion Protein Fragment hPrP[173-195] Internalization in Rat B104 Neuroblastoma Cell Line

[ Vol. 16 , Issue. 11 ]


Emanuela Urso, Raffaele Acierno, Maria Giulia Lionetto, Antonia Rizzello, Andrea Papa, Trifone Schettino and Michele Maffia   Pages 1281 - 1290 ( 10 )


The cytotoxicity of hPrP[173-195] prion peptide against a neuroblastoma cell model was found independent of its tendency to aggregate over time. Cytosolic and nuclear inclusions of peptide were highlighted by confocal microscopy, suggesting a role as a transcription factor in activating signal transduction pathways involved in cell toxicity.


Prion disease, cellular prion protein (PrPC), helix-2, structural ambivalence, synthetic prion peptides, confocal microscopy


Department of Biological and Environmental Science and Technology, University of Salento, Lecce, Italy.

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