Isolation of human neuronal cells resistant to toxicity by the prion protein peptide 106-126

2001 ◽  
Vol 3 (2) ◽  
pp. 169-180 ◽  
Author(s):  
Yaping Gu ◽  
Yi Jing ◽  
Anil Kumar ◽  
Yogesh Sharma ◽  
Hisashi Fujioka ◽  
...  
Keyword(s):  
Prion Protein ◽  
Neuronal Cells ◽  
Human Neuronal Cells ◽  
Prion Protein Peptide

scholarly journals Study on the toxic mechanism of prion protein peptide 106–126 in neuronal and non neuronal cells

2006 ◽  
Vol 84 (3) ◽  
pp. 637-646 ◽  
Author(s):  
Ingrid Dupiereux ◽  
Willy Zorzi ◽  
Walid Rachidi ◽  
Danièle Zorzi ◽  
Olivier Pierard ◽  
...  
Keyword(s):  
Prion Protein ◽  
Neuronal Cells ◽  
Toxic Mechanism ◽  
Prion Protein Peptide

scholarly journals Altered toxicity of the prion protein peptide PrP106–126 carrying the Ala117→Val mutation

2000 ◽  
Vol 346 (3) ◽  
pp. 785-791 ◽  
Author(s):  
David R. BROWN
Keyword(s):  
Point Mutation ◽  
Prion Protein ◽  
Prion Diseases ◽  
Point Mutations ◽  
Human Sequence ◽  
Gene Coding ◽  
Normal Human ◽  
Microtubule Formation ◽  
Β Sheet ◽  
Prion Protein Peptide

The inherited prion diseases such as Gerstmann-Sträussler-Scheinker syndrome (GSS) are linked to point mutations in the gene coding for the cellular isoform of the prion protein (PrPC). One particular point mutation A117V (Ala117 → Val) is linked to a variable pathology that usually includes deposition of neurofibrillary tangles. A prion protein peptide carrying this point mutation [PrP106-126(117V)] was generated and compared with a peptide based on the normal human sequence [PrP106-126(117A)]. The inclusion of this point mutation increased the toxicity of PrP106-126 which could be linked to an increased β-sheet content. An assay of microtubule formation in the presence of tau indicated that PrP106-126 decreased the rate of microtubule formation that could be related to the displacement of tau. PrP106-126 carrying the 117 mutation was more efficient at inhibiting microtubule formation. These results suggest a possible mechanism of toxicity for protein carrying this mutation via destabilization of the cytoskeleton and deposition of tau in filaments, as observed in GSS.

scholarly journals Effects of Zinc and DHA on the Epigenetic Regulation of Human Neuronal Cells

2012 ◽  
Vol 29 (1-2) ◽  
pp. 87-98 ◽  
Author(s):  
Nadia Sadli ◽  
M. Leigh Ackland ◽  
Damitha De Mel ◽  
Andrew J. Sinclair ◽  
Cenk Suphioglu
Keyword(s):  
Epigenetic Regulation ◽  
Neuronal Cells ◽  
Human Neuronal Cells

scholarly journals The cytoplasmic tail of the rabies virus G protein is an essential domain controlling death/survival in human neuronal cells

2008 ◽  
Vol 2 (S1) ◽  
Author(s):  
Christophe Prehaud ◽  
Mireille Lafage ◽  
Gene S Tan ◽  
Françoise Mégret ◽  
Pauline Ménager ◽  
...  
Keyword(s):  
G Protein ◽  
Rabies Virus ◽  
Neuronal Cells ◽  
Cytoplasmic Tail ◽  
Essential Domain ◽  
Human Neuronal Cells

The application of magnets directs the orientation of neurite outgrowth in cultured human neuronal cells

2008 ◽  
Vol 174 (1) ◽  
pp. 91-96 ◽  
Author(s):  
Seungchan Kim ◽  
Woo-Seok Im ◽  
Lami Kang ◽  
Soon-Tae Lee ◽  
Kon Chu ◽  
...  
Keyword(s):  
Neurite Outgrowth ◽  
Neuronal Cells ◽  
Human Neuronal Cells

scholarly journals Paired Helical Filament-Forming Region of Tau (297–391) Influences Endogenous Tau Protein and Accumulates in Acidic Compartments in Human Neuronal Cells

2020 ◽  
Vol 432 (17) ◽  
pp. 4891-4907 ◽  
Author(s):  
Saskia J. Pollack ◽  
Jasmine Trigg ◽  
Tahmida Khanom ◽  
Luca Biasetti ◽  
Karen E. Marshall ◽  
...  
Keyword(s):  
Tau Protein ◽  
Neuronal Cells ◽  
Paired Helical Filament ◽  
Human Neuronal Cells ◽  
Acidic Compartments
Sign in / Sign up

Export Citation Format

Share Document