Confocal microscopy evidence of prion protein fragment hPrP[173-195] internalization in rat B104 neuroblastoma cell line.
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.
Urso
Emanuela
E
Lab. of Adaptive Physiology, Department of Biological and Environmental Science and Technology, University of Lecce, prov.le Lecce-Monteroni, Lecce, Italy.
Acierno
Raffaele
R
Lionetto
Maria Giulia
MG
Rizzello
Antonia
A
Papa
Andrea
A
Schettino
Trifone
T
Maffia
Michele
M
D000818:Animals; D045744:Cell Line, Tumor; D002470:Cell Survival / Q000187:drug effects; D019793:Fluorescein; D018613:Microscopy, Confocal / Q000379:methods*; D009447:Neuroblastoma / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D018621:PrPC Proteins / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D017096:Prion Diseases; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D051381:Rats; D012235:Rhodamines; D015398:Signal Transduction; D013752:Tetracycline / Q000494:pharmacology
D010446:Peptide Fragments; D018621:PrPC Proteins; D012235:Rhodamines; C005358:tetramethylrhodamine; D013752:Tetracycline; D019793:Fluorescein