Abstract
Prion diseases or transmissible spongiform encephalopathies are fatal neurodegenerative diseases characterized by the aggregation and deposition of the misfolded prion protein in the brain. α-synuclein (α-syn)-Associated multiple system atrophy has been recently shown to be caused by a bona fide α-syn prion strain. Several other misfolded native proteins such as β-Amyloid, tau and TDP-43 share some aspects of prions although none of them is shown to be transmissible in nature or in experimental animals. However, these prion-like 'prionoids' are causal to a variety of neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis. The remarkable recent discovery of at least two new α-syn prion strains and their transmissibility in transgenic mice and in vitro cell models raises a distinct question as to whether some specific strain of other prionoids could have the capability of disease transmission in a manner similar to prions. In this overview, we briefly describe human and other mammalian prion diseases and comment on certain similarities between prion and prionoid and the possibility of prion-like transmissibility of some prionoid strains.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 169-174 |
| Number of pages | 6 |
| Journal | Annals of Indian Academy of Neurology |
| Volume | 19 |
| Issue number | 2 |
| DOIs | |
| State | Published - Apr 1 2016 |
Fingerprint
Keywords
- Neurodegeneration
- prion
- prionoid
- protein aggregate
ASJC Scopus subject areas
- Clinical Neurology
Cite this
Prions, prion-like prionoids, and neurodegenerative disordersVacancy. / Verma, Ashok.
In: Annals of Indian Academy of Neurology, Vol. 19, No. 2, 01.04.2016, p. 169-174.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Prions, prion-like prionoids, and neurodegenerative disordersVacancy
AU - Verma, Ashok
PY - 2016/4/1
Y1 - 2016/4/1
N2 - Prion diseases or transmissible spongiform encephalopathies are fatal neurodegenerative diseases characterized by the aggregation and deposition of the misfolded prion protein in the brain. α-synuclein (α-syn)-Associated multiple system atrophy has been recently shown to be caused by a bona fide α-syn prion strain. Several other misfolded native proteins such as β-Amyloid, tau and TDP-43 share some aspects of prions although none of them is shown to be transmissible in nature or in experimental animals. However, these prion-like 'prionoids' are causal to a variety of neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis. The remarkable recent discovery of at least two new α-syn prion strains and their transmissibility in transgenic mice and in vitro cell models raises a distinct question as to whether some specific strain of other prionoids could have the capability of disease transmission in a manner similar to prions. In this overview, we briefly describe human and other mammalian prion diseases and comment on certain similarities between prion and prionoid and the possibility of prion-like transmissibility of some prionoid strains.
AB - Prion diseases or transmissible spongiform encephalopathies are fatal neurodegenerative diseases characterized by the aggregation and deposition of the misfolded prion protein in the brain. α-synuclein (α-syn)-Associated multiple system atrophy has been recently shown to be caused by a bona fide α-syn prion strain. Several other misfolded native proteins such as β-Amyloid, tau and TDP-43 share some aspects of prions although none of them is shown to be transmissible in nature or in experimental animals. However, these prion-like 'prionoids' are causal to a variety of neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis. The remarkable recent discovery of at least two new α-syn prion strains and their transmissibility in transgenic mice and in vitro cell models raises a distinct question as to whether some specific strain of other prionoids could have the capability of disease transmission in a manner similar to prions. In this overview, we briefly describe human and other mammalian prion diseases and comment on certain similarities between prion and prionoid and the possibility of prion-like transmissibility of some prionoid strains.
KW - Neurodegeneration
KW - prion
KW - prionoid
KW - protein aggregate
UR - http://www.scopus.com/inward/record.url?scp=84969750087&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84969750087&partnerID=8YFLogxK
U2 - 10.4103/0972-2327.179979
DO - 10.4103/0972-2327.179979
M3 - Review article
AN - SCOPUS:84969750087
VL - 19
SP - 169
EP - 174
JO - Annals of Indian Academy of Neurology
JF - Annals of Indian Academy of Neurology
SN - 0972-2327
IS - 2
ER -