Analysis of the Prion Protein Gene in Thalamic Dementia
R.B. Petersen, M. Tabaton, L. Berg, B. Schrank, R.M. Torack,
S. Leal, J. Julien, C. Vital, B. Deleplanque, W.W.
Pendlebury, D. Drachman, T.W. Smith, J.J. Martin, M. Oda,
P. Montagna, J. Ott, L. Autilio-Gambetti, E. Lugaresi, P. Gambetti
Neurology , 42(10),1859--1063 (1992 Oct)
Abstract
Thalamic degenerations or dementias are poorly understood
conditions. The familial forms are (1) selective thalamic
degenerations and (2) thalamic degenerations associated with
multiple system atrophy. Selective thalamic degenerations share
clinical and pathologic features with fatal familial insomnia, an
autosomal dominant disease linked to a mutation at codon 178 of the
prion protein (PrP) gene that causes the substitution of asparagine
for aspartic acid (178Asn mutation). We amplified the carboxyl
terminal coding region of the PrP gene from subjects with selective
thalamic dementia or thalamic dementia associated with multiple
system atrophy. Three of the four kindreds with selective thalamic
dementia and none of the three kindreds with thalamic dementia
associated with multiple system atrophy had the PrP 178Asn mutation.
Thus, analysis of the PrP gene may be useful in diagnosing the
subtypes of thalamic dementia. Moreover, since selective thalamic
dementia with the PrP 178Asn mutation and fatal familial insomnia
share clinical and histopathologic features, we propose that they
are the same disease.
