scholarly journals Is indeed the prion protein a Harlequin servant of "many" masters?

Prion ◽  
2009 ◽  
Vol 3 (4) ◽  
pp. 202-205 ◽  
Author(s):  
M. Catia Sorgato ◽  
Caterina Peggion ◽  
Alessandro Bertoli
Keyword(s):  
Prion Protein ◽  
Protein A

The complex-formation behaviour of His residues in the fifth Cu2+ binding site of human prion protein: a close look

2009 ◽  
Vol 33 (11) ◽  
pp. 2300 ◽  
Author(s):  
Maurizio Remelli ◽  
Daniela Valensin ◽  
Dimitri Bacco ◽  
Ewa Gralka ◽  
Remo Guerrini ◽  
...  
Keyword(s):  
Complex Formation ◽  
Binding Site ◽  
Prion Protein ◽  
Protein A ◽  
Human Prion Protein

Prion protein: a different concept of replication

1993 ◽  
Vol 16 (11) ◽  
pp. 425-426 ◽  
Author(s):  
Rosalind M. Ridley ◽  
Harry F. Baker
Keyword(s):  
Prion Protein ◽  
Protein A

3PT172 Dynamics of normal prion protein, a raft-associated GPI-anchored molecule, in the live neuronal plasma membrane(The 50th Annual Meeting of the Biophysical Society of Japan)

2012 ◽  
Vol 52 (supplement) ◽  
pp. S170-S171
Author(s):  
Yuri L. Nemoto ◽  
Chieko Nakada ◽  
Hiroko Hijikata ◽  
Takahiro K. Fujiwara ◽  
Rinshi S. Kasai ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Annual Meeting ◽  
Prion Protein ◽  
Protein A ◽  
Biophysical Society ◽  
Neuronal Plasma Membrane

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 Loss of functional prion protein: a role in prion disorders?

1996 ◽  
Vol 3 (8) ◽  
pp. 619-621 ◽  
Author(s):  
David R. Borchelt ◽  
Sangram S. Sisodia
Keyword(s):  
Prion Protein ◽  
Protein A
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