TY - JOUR
T1 - Intracerebral distribution of the abnormal isoform of the prion protein in sporadic Creutzfeldt-Jakob disease and fatal insomnia
AU - Parchi, Piero
AU - Capellari, Sabina
AU - Gambetti, Pierluigi
PY - 2000/7/1
Y1 - 2000/7/1
N2 - Molecular genetics and protein chemistry have led to major advances in our understanding of the molecular basis of phenotypic variability of prion diseases. A large body of evidence indicates that a common methionine/valine polymorphism at codon 129 in the prion protein gene (PRNP), alone or in conjunction with PRNP mutations, modulates both disease susceptibility and phenotypic expression of human prion diseases. In addition, there are physico-chemical properties of the abnormal isoform of the prion protein (PrP(SC)), such as relative molecular mass and glycosylation, that correlate with distinct phenotypes even in subjects carrying the same PRNP genotype. Different PrP(SC) 'type'-PRNP genotype combinations are found associated with pathological phenotypes that differ in the relative severity of lesions among distinct brain regions, the presence and morphology of certain lesions such as amyloid plaques, and the pattern of intracerebral and tissue deposition of PrP(SC). This review summarizes the currently available data on the molecular pathology of sporadic Creutzfeldt-Jakob disease, the most common human prion disease, and fatal insomnia, a more recently defined entity that has rapidly become one of the best characterized of the human prion diseases. (C) 2000 Wiley-Liss, Inc.
AB - Molecular genetics and protein chemistry have led to major advances in our understanding of the molecular basis of phenotypic variability of prion diseases. A large body of evidence indicates that a common methionine/valine polymorphism at codon 129 in the prion protein gene (PRNP), alone or in conjunction with PRNP mutations, modulates both disease susceptibility and phenotypic expression of human prion diseases. In addition, there are physico-chemical properties of the abnormal isoform of the prion protein (PrP(SC)), such as relative molecular mass and glycosylation, that correlate with distinct phenotypes even in subjects carrying the same PRNP genotype. Different PrP(SC) 'type'-PRNP genotype combinations are found associated with pathological phenotypes that differ in the relative severity of lesions among distinct brain regions, the presence and morphology of certain lesions such as amyloid plaques, and the pattern of intracerebral and tissue deposition of PrP(SC). This review summarizes the currently available data on the molecular pathology of sporadic Creutzfeldt-Jakob disease, the most common human prion disease, and fatal insomnia, a more recently defined entity that has rapidly become one of the best characterized of the human prion diseases. (C) 2000 Wiley-Liss, Inc.
KW - Brain mapping
KW - Dementia
KW - Neurodegeneration
KW - Prion protein gene
KW - Prion strains
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U2 - 10.1002/1097-0029(20000701)50:1<16::AID-JEMT4>3.0.CO;2-Y
DO - 10.1002/1097-0029(20000701)50:1<16::AID-JEMT4>3.0.CO;2-Y
M3 - Article
C2 - 10871544
AN - SCOPUS:0034234437
VL - 50
SP - 16
EP - 25
JO - Microscopy Research and Technique
JF - Microscopy Research and Technique
SN - 1059-910X
IS - 1
ER -