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.
Keywords: Prion disease, cellular prion protein (PrPC), helix-2, structural ambivalence, synthetic prion peptides, confocal microscopy
Protein & Peptide Letters
Title: Confocal Microscopy Evidence of Prion Protein Fragment hPrP[173-195] Internalization in Rat B104 Neuroblastoma Cell Line
Volume: 16 Issue: 11
Author(s): Emanuela Urso, Raffaele Acierno, Maria Giulia Lionetto, Antonia Rizzello, Andrea Papa, Trifone Schettino and Michele Maffia
Affiliation:
Keywords: Prion disease, cellular prion protein (PrPC), helix-2, structural ambivalence, synthetic prion peptides, confocal microscopy
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.
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Cite this article as:
Urso Emanuela, Acierno Raffaele, Lionetto Giulia Maria, Rizzello Antonia, Papa Andrea, Schettino Trifone and Maffia Michele, Confocal Microscopy Evidence of Prion Protein Fragment hPrP[173-195] Internalization in Rat B104 Neuroblastoma Cell Line, Protein & Peptide Letters 2009; 16 (11) . https://dx.doi.org/10.2174/092986609789353655
DOI https://dx.doi.org/10.2174/092986609789353655 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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