Transthyretin gene in Alzheimer's disease patients

Neurosci Lett. 1996 Feb 9;204(3):212-4. doi: 10.1016/0304-3940(96)12334-x.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Age of Onset
  • Alzheimer Disease / epidemiology
  • Alzheimer Disease / genetics*
  • Amyloid beta-Peptides / biosynthesis
  • Amyloid beta-Peptides / metabolism
  • DNA, Single-Stranded / genetics
  • Genetic Testing
  • Humans
  • Mutation / genetics
  • Polymorphism, Genetic
  • Prealbumin / genetics*


  • Amyloid beta-Peptides
  • DNA, Single-Stranded
  • Prealbumin