Transthyretin gene in Alzheimer's disease patients.
Amyloid beta (Abeta) is known to be the main component of Alzheimer's disease (AD) senile plaques. A homologous peptide is a normal component of biological fluids and is called soluble Abeta (sAbeta). Synthetic peptides homologous to Abeta form amyloid-like fibrils in vitro. This fibril formation can be inhibited by normal human cerebrospinal fluid (CSF) [Wisniewski et al., Ann. Neurol. 34 (1993)]. Furthermore, it has been proposed that normal transthyretin (TTR), which is a component of CSF, can itself bind sAbeta, preventing amyloid fibril formation, and that variants of TTR could be associated with AD [Schwarzman et al., Proc. Natl. Acad. Sci. USA, 91 (1994)]. Because of this possible association, we screened for TTR mutations from 47 sporadic and 19 early-onset familial AD patients using single strand conformation polymorphism analysis. Our results show no correlation between TTR variants and Alzheimer's disease in this group of patients.
Palha
J A
JA
Department of Pathology, New York University Medical Center, 10016, ASA.
Moreira
P
P
Wisniewski
T
T
Frangione
B
B
Saraiva
M J
MJ
D017668:Age of Onset; D000544:Alzheimer Disease / Q000453:epidemiology / Q000235:genetics*; D016229:Amyloid beta-Peptides / Q000096:biosynthesis / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000235:genetics; D005820:Genetic Testing; D006801:Humans; D009154:Mutation / Q000235:genetics; D011110:Polymorphism, Genetic; D011228:Prealbumin / Q000235:genetics*
D016229:Amyloid beta-Peptides; D004277:DNA, Single-Stranded; D011228:Prealbumin