scholarly journals Cellular prion protein: A co-receptor mediating neuronal cofilin-actin rod formation induced by β-amyloid and proinflammatory cytokines

Prion ◽  
2014 ◽  
Vol 8 (6) ◽  
pp. 375-380 ◽  
Author(s):  
Keifer P Walsh ◽  
Thomas B Kuhn ◽  
James R Bamburg
Keyword(s):  
Prion Protein ◽  
Proinflammatory Cytokines ◽  
Protein A ◽  
Cellular Prion Protein ◽  
Β Amyloid

scholarly journals The cellular prion protein interacts with and promotes the activity of Na,K-ATPases

PLoS ONE ◽  
2021 ◽  
Vol 16 (11) ◽  
pp. e0258682
Author(s):  
Declan Williams ◽  
Mohadeseh Mehrabian ◽  
Hamza Arshad ◽  
Shehab Eid ◽  
Christopher Sackmann ◽  
...  
Keyword(s):  
Prion Protein ◽  
Prion Diseases ◽  
Protein A ◽  
Neuroblastoma Cells ◽  
Cellular Prion Protein ◽  
Affinity Capture ◽  
Endoproteolytic Cleavage ◽  
Relative Quantitation ◽  
Steady State Levels ◽  
Uptake Activity

The prion protein (PrP) is best known for its ability to cause fatal neurodegenerative diseases in humans and animals. Here, we revisited its molecular environment in the brain using a well-developed affinity-capture mass spectrometry workflow that offers robust relative quantitation. The analysis confirmed many previously reported interactions. It also pointed toward a profound enrichment of Na,K-ATPases (NKAs) in proximity to cellular PrP (PrPC). Follow-on work validated the interaction, demonstrated partial co-localization of the ATP1A1 and PrPC, and revealed that cells exposed to cardiac glycoside (CG) inhibitors of NKAs exhibit correlated changes to the steady-state levels of both proteins. Moreover, the presence of PrPC was observed to promote the ion uptake activity of NKAs in a human co-culture paradigm of differentiated neurons and glia cells, and in mouse neuroblastoma cells. Consistent with this finding, changes in the expression of 5’-nucleotidase that manifest in wild-type cells in response to CG exposure can also be observed in untreated PrPC-deficient cells. Finally, the endoproteolytic cleavage of the glial fibrillary acidic protein, a hallmark of late-stage prion disease, can also be induced by CGs, raising the prospect that a loss of NKA activity may contribute to the pathobiology of prion diseases.

scholarly journals The nucleo-junctional interplay of the cellular prion protein: A new partner in cancer-related signaling pathways?

Prion ◽  
2016 ◽  
Vol 10 (2) ◽  
pp. 143-152 ◽  
Author(s):  
Monique Rousset ◽  
Armelle Leturque ◽  
Sophie Thenet
Keyword(s):  
Signaling Pathways ◽  
Prion Protein ◽  
Protein A ◽  
Cellular Prion Protein

scholarly journals The Cellular Prion Protein: A Player in Immunological Quiescence

2015 ◽  
Vol 6 ◽  
Author(s):  
Maren K. Bakkebø ◽  
Sophie Mouillet-Richard ◽  
Arild Espenes ◽  
Wilfred Goldmann ◽  
Jörg Tatzelt ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein A ◽  
Cellular Prion Protein

The cellular prion protein: A new partner of the lectin CBP70 in the nucleus of NB4 human promyelocytic leukemia cells*

2001 ◽  
Vol 84 (2) ◽  
pp. 408-419 ◽  
Author(s):  
C. Rybner ◽  
S. Finel-Szermanski ◽  
M. Felin ◽  
T. Sahraoui ◽  
C. Rousseau ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein A ◽  
Promyelocytic Leukemia ◽  
Cellular Prion Protein ◽  
Leukemia Cells

Cellular prion protein modulates β-amyloid deposition in aged APP/PS1 transgenic mice

2013 ◽  
Vol 34 (12) ◽  
pp. 2793-2804 ◽  
Author(s):  
Lara Ordóñez-Gutiérrez ◽  
Juan María Torres ◽  
Rosalina Gavín ◽  
Marta Antón ◽  
Ana Isabel Arroba-Espinosa ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Prion Protein ◽  
Amyloid Deposition ◽  
Cellular Prion Protein ◽  
Β Amyloid

scholarly journals Accumulation of cellular prion protein within β‐amyloid oligomer plaques in aged human brains

2021 ◽  
Author(s):  
Reisuke H. Takahashi ◽  
Mayumi Yokotsuka ◽  
Minoru Tobiume ◽  
Yuko Sato ◽  
Hideki Hasegawa ◽  
...  
Keyword(s):  
Prion Protein ◽  
Cellular Prion Protein ◽  
Β Amyloid ◽  
Human Brains ◽  
Amyloid Oligomer

scholarly journals Abnormal prion protein in genetically resistant sheep from a scrapie-infected flock

2004 ◽  
Vol 85 (11) ◽  
pp. 3483-3486 ◽  
Author(s):  
J.-Y. Madec ◽  
S. Simon ◽  
S. Lezmi ◽  
A. Bencsik ◽  
J. Grassi ◽  
...  
Keyword(s):  
Prion Protein ◽  
Sandwich Elisa ◽  
Protein A ◽  
Cellular Prion Protein ◽  
Transmissible Spongiform Encephalopathies ◽  
Motor Nucleus ◽  
Entry Site ◽  
Spongiform Encephalopathies ◽  
Dorsal Motor Nucleus ◽  
The Brain

The central molecular event in transmissible spongiform encephalopathies, such as scrapie in sheep, is the accumulation in tissues of an abnormal isoform of the cellular prion protein. A previous investigation of 26 sheep showed that the accumulation of PrPres in brain correlated more with the prnp genotype than with the severity of the clinical disease. Here, the ability of a sandwich ELISA to detect PrPres distribution in the brain was demonstrated. Immunohistochemistry also strongly supported the hypothesis that the dorsal motor nucleus of the vagus nerve is the possible entry site in the brain for the scrapie agent. Remarkably, three asymptomatic (or possibly asymptomatic for scrapie) sheep carrying an allele known to be associated with clinical scrapie resistance (ARR), which were negative for the detection of PrPres by Western blotting and immunohistochemistry, were positive for the presence of PrPres by ELISA, raising the possibility of carriers resistant to the disease and possibly contributing to the persistence of scrapie in certain flocks.

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