Cellular prion protein and Alzheimer disease: Link to oligomeric amyloid-β and neuronal cell death

Wataru Kudo; Robert B. Petersen; Hyoung Gon Lee

doi:10.4161/pri.22848

Cellular prion protein and Alzheimer disease: Link to oligomeric amyloid-β and neuronal cell death

Wataru Kudo, Robert B. Petersen, Hyoung Gon Lee

Research output: Contribution to journal › Review article › peer-review

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Abstract

Soluble oligomeric amyloid-ß (Aß) has been suggested to impair synaptic and neuronal function, leading to neurodegeneration that is clinically observed as the memory and cognitive dysfunction characteristic of Alzheimer disease, while the precise mechanism(s) whereby oligomeric Aß causes neurotoxicity remains unknown. Recently, the cellular prion protein (PrP ^C) was reported to be an essential co-factor in mediating the neurotoxic effect of oligomeric Aß. Our recent study showed that Prnp ^-/- mice are resistant to the neurotoxic effect of oligomeric Aß in vivo and in vitro. Furthermore, application of an anti-PrP ^C antibody or PrP^C peptide was able to block oligomeric Aß-induced neurotoxicity. These findings demonstrate that PrP^C may be involved in neuropathologic conditions other than conventional prion diseases, i.e., Creutzfeldt-Jakob disease.

Original language	English
Pages (from-to)	114-116
Number of pages	3
Journal	Prion
Volume	7
Issue number	2
DOIs	https://doi.org/10.4161/pri.22848
State	Published - Mar 2013

Keywords

Amyloid-ß
NMDA receptor
Neurotoxicity
Oligomer
PrPC

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@article{b3404502f1c2402fb78e3445f3804512,

title = "Cellular prion protein and Alzheimer disease: Link to oligomeric amyloid-β and neuronal cell death",

abstract = "Soluble oligomeric amyloid-{\ss} (A{\ss}) has been suggested to impair synaptic and neuronal function, leading to neurodegeneration that is clinically observed as the memory and cognitive dysfunction characteristic of Alzheimer disease, while the precise mechanism(s) whereby oligomeric A{\ss} causes neurotoxicity remains unknown. Recently, the cellular prion protein (PrP C) was reported to be an essential co-factor in mediating the neurotoxic effect of oligomeric A{\ss}. Our recent study showed that Prnp -/- mice are resistant to the neurotoxic effect of oligomeric A{\ss} in vivo and in vitro. Furthermore, application of an anti-PrP C antibody or PrPC peptide was able to block oligomeric A{\ss}-induced neurotoxicity. These findings demonstrate that PrPC may be involved in neuropathologic conditions other than conventional prion diseases, i.e., Creutzfeldt-Jakob disease.",

keywords = "Amyloid-{\ss}, NMDA receptor, Neurotoxicity, Oligomer, PrPC",

author = "Wataru Kudo and Petersen, {Robert B.} and Lee, {Hyoung Gon}",

note = "Funding Information: Work in the authors{\textquoteright} laboratories is supported by the National Institutes of Health (AG028679 to H.-g.L.) and the Alzheimer{\textquoteright}s Association (IIRG-11-173471 to H.-g.L.).",

year = "2013",

month = mar,

doi = "10.4161/pri.22848",

language = "English",

volume = "7",

pages = "114--116",

journal = "Prion",

issn = "1933-6896",

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TY - JOUR

T1 - Cellular prion protein and Alzheimer disease

T2 - Link to oligomeric amyloid-β and neuronal cell death

AU - Kudo, Wataru

AU - Petersen, Robert B.

AU - Lee, Hyoung Gon

N1 - Funding Information: Work in the authors’ laboratories is supported by the National Institutes of Health (AG028679 to H.-g.L.) and the Alzheimer’s Association (IIRG-11-173471 to H.-g.L.).

PY - 2013/3

Y1 - 2013/3

N2 - Soluble oligomeric amyloid-ß (Aß) has been suggested to impair synaptic and neuronal function, leading to neurodegeneration that is clinically observed as the memory and cognitive dysfunction characteristic of Alzheimer disease, while the precise mechanism(s) whereby oligomeric Aß causes neurotoxicity remains unknown. Recently, the cellular prion protein (PrP C) was reported to be an essential co-factor in mediating the neurotoxic effect of oligomeric Aß. Our recent study showed that Prnp -/- mice are resistant to the neurotoxic effect of oligomeric Aß in vivo and in vitro. Furthermore, application of an anti-PrP C antibody or PrPC peptide was able to block oligomeric Aß-induced neurotoxicity. These findings demonstrate that PrPC may be involved in neuropathologic conditions other than conventional prion diseases, i.e., Creutzfeldt-Jakob disease.

AB - Soluble oligomeric amyloid-ß (Aß) has been suggested to impair synaptic and neuronal function, leading to neurodegeneration that is clinically observed as the memory and cognitive dysfunction characteristic of Alzheimer disease, while the precise mechanism(s) whereby oligomeric Aß causes neurotoxicity remains unknown. Recently, the cellular prion protein (PrP C) was reported to be an essential co-factor in mediating the neurotoxic effect of oligomeric Aß. Our recent study showed that Prnp -/- mice are resistant to the neurotoxic effect of oligomeric Aß in vivo and in vitro. Furthermore, application of an anti-PrP C antibody or PrPC peptide was able to block oligomeric Aß-induced neurotoxicity. These findings demonstrate that PrPC may be involved in neuropathologic conditions other than conventional prion diseases, i.e., Creutzfeldt-Jakob disease.

KW - Amyloid-ß

KW - NMDA receptor

KW - Neurotoxicity

KW - Oligomer

KW - PrPC

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DO - 10.4161/pri.22848

M3 - Review article

C2 - 23154635

AN - SCOPUS:84875503806

VL - 7

SP - 114

EP - 116

JO - Prion

JF - Prion

SN - 1933-6896

IS - 2

ER -

Cellular prion protein and Alzheimer disease: Link to oligomeric amyloid-β and neuronal cell death

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Keywords

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