Abstract:
:A characteristic feature of Creutzfeldt-Jakob disease (CJD) is the accumulation in the brain of the amyloid protease-resistant protein PrPres. PrPres derives from a host-encoded, protease-sensitive isoform, PrPsen. Mutations of this protein are linked to familial variants of the disease, and the presence of a methionine or valine residue at the polymorphic position 129 may be critical in sporadic CJD cases. We found that in the brain of patients heterozygous for the mutation in which isoleucine is substituted for valine at codon 210 (Val21Olle), the PrPres is formed by both the wild-type and mutant PrPsen. We also found that in a sporadic CJD patient, who was heterozygous (Met/Val) at position 129, PrPres is also formed by both allotypes. These data associate transmissible spongiform encephalopathies with other amyloidosis, although the nature of the transmissible agent remains unsettled.
journal_name
Nat Medjournal_title
Nature medicineauthors
Silvestrini MC,Cardone F,Maras B,Pucci P,Barra D,Brunori M,Pocchiari Mdoi
10.1038/nm0597-521subject
Has Abstractpub_date
1997-05-01 00:00:00pages
521-5issue
5eissn
1078-8956issn
1546-170Xjournal_volume
3pub_type
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