Journal Article (Review Article)

DZNE-2020-03201

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Prion disease: a tale of folds and strains.

Kretzschmar, H. (First author)DZNE* ; Tatzelt, J. (Last author)DZNE*

2013
Wiley-Blackwell Oxford

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Please use a persistent id in citations: doi:10.1111/bpa.12045

Abstract: Research on prions, the infectious agents of devastating neurological diseases in humans and animals, has been in the forefront of developing the concept of protein aggregation diseases. Prion diseases are distinguished from other neurodegenerative diseases by three peculiarities. First, prion diseases, in addition to being sporadic or genetic like all other neurodegenerative diseases, are infectious diseases. Animal models were developed early on (a long time before the advent of transgenic technology), and this has made possible the discovery of the prion protein as the infectious agent. Second, human prion diseases have true equivalents in animals, such as scrapie, which has been the subject of experimental research for many years. Variant Creutzfeldt-Jakob disease (vCJD) is a zoonosis caused by bovine spongiform encephalopathy (BSE) prions. Third, they show a wide variety of phenotypes in humans and animals, much wider than the variants of any other sporadic or genetic neurodegenerative disease. It has now become firmly established that particular PrP(Sc) isoforms are closely related to specific human prion strains. The variety of human prion diseases, still an enigma in its own right, is a focus of this article. Recently, a series of experiments has shown that the concept of aberrant protein folding and templating, first developed for prions, may apply to a variety of neurodegenerative diseases. In the wake of these discoveries, the term prion has come to be used for Aβ, α-synuclein, tau and possibly others. The self-propagation of alternative conformations seems to be the common denominator of these 'prions,' which in future, in order to avoid confusion, may have to be specified either as 'neurodegenerative prions' or 'infectious prions.'

Keyword(s): Animals (MeSH) ; Blood-Brain Barrier (MeSH) ; Creutzfeldt-Jakob Syndrome: genetics (MeSH) ; Creutzfeldt-Jakob Syndrome: pathology (MeSH) ; Genome-Wide Association Study (MeSH) ; Humans (MeSH) ; Kuru: genetics (MeSH) ; Kuru: pathology (MeSH) ; PrPC Proteins: chemistry (MeSH) ; PrPC Proteins: genetics (MeSH) ; PrPC Proteins: toxicity (MeSH) ; Prion Diseases: genetics (MeSH) ; Prion Diseases: pathology (MeSH) ; Prion Diseases: transmission (MeSH) ; Protein Folding (MeSH) ; Proteostasis Deficiencies: genetics (MeSH) ; Proteostasis Deficiencies: pathology (MeSH) ; PrPC Proteins

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Contributing Institute(s):

1. Ext Zentrum für Neuropathologie und Proinenforschung (Ext LMU ZNP)
2. Ext Neurobiochemistry, LMU (Ext AG Tatzelt)

Research Program(s):

1. 342 - Disease Mechanisms and Model Systems (POF3-342) (POF3-342)

Appears in the scientific report 2013

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Database coverage:
; BIOSIS Previews ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; IF >= 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection

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