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.
Confocal microscopy evidence of prion protein fragment hPrP[173-195] internalization in rat B104 neuroblastoma cell line
URSO, EMANUELA;ACIERNO, Raffaele;LIONETTO, Maria Giulia;RIZZELLO, Antonia;SCHETTINO, Trifone;MAFFIA, Michele
2009-01-01
Abstract
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.File in questo prodotto:
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