Transmissible familial Creutzfeldt-Jakob disease associated with five, seven, and eight extra octapeptide coding repeats in the PRNP gene.
- 1 December 1991
- journal article
- case report
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 88 (23) , 10926-10930
- https://doi.org/10.1073/pnas.88.23.10926
Abstract
The PRNP gene, encoding the amyloid precursor protein that is centrally involved in Creutzfeldt-Jakob disease (CJD), has an unstable region of five variant tandem octapeptide coding repeats between codons 51 and 91. We screened a total of 535 individuals for the presence of extra repeats in this region, including patients with sporadic and familial forms of spongiform encephalopathy, members of their families, other neurological and non-neurological patients, and normal controls. We identified three CJD families (in each of which the proband's disease was neuropathologically confirmed and experimentally transmitted to primates) that were heterozygous for alleles with 10, 12, or 13 repeats, some of which had "wobble" nucleotide substitutions. We also found one individual with 9 repeats and no nucleotide substitutions who had no evidence of neurological disease. These observations, together with data on published British patients with 11 and 14 repeats, strongly suggest that the occurrence of 10 or more octapeptide repeats in the encoded amyloid precursor protein predisposes to CJD.Keywords
This publication has 34 references indexed in Scilit:
- Insertions in the prion protein gene in atypical dementiasExperimental Neurology, 1991
- The new biology of spongiform encephalopathy: infectious amyloidoses with a genetic twistThe Lancet, 1991
- A heptapeptide repeat contributes to the unusual length of chloroplast ribosomal protein S18 Nucleotide sequence and map position of therpl33-rps18 gene cluster in maizeFEBS Letters, 1991
- Prion dementia without characteristic pathologyThe Lancet, 1990
- Creutzfeldt-Jakob disease and kuru patients lack a mutation consistently found in the Gerstmann-Sträussler-Scheinker syndromeExperimental Neurology, 1990
- Mutations in familial Creutzfeldt-Jakob disease and Gerstmann-Sträussler-Scheinker's syndromeExperimental Neurology, 1989
- Pro→Leu change at position 102 of prinon protein is the most common but not the sole mutation related to Gerstmann-Sträussler syndromeBiochemical and Biophysical Research Communications, 1989
- Linkage of a prion protein missense variant to Gerstmann–Sträussler syndromeNature, 1989
- Enzymatic Amplification of β-Globin Genomic Sequences and Restriction Site Analysis for Diagnosis of Sickle Cell AnemiaScience, 1985
- Remarkable conservation of structure among intermediate filament genesCell, 1984