Transthyretin inhibition of amyloid beta aggregation and toxicity

S. Giunta, M. B. Valli, R. Galeazzi, P. Fattoretti, E. H. Corder, L. Galeazzi

Research output: Contribution to journalArticle

Abstract

Objectives: The aim of this study was to investigate transthyretin (prealbumin) effects on Aβ25-35-induced cytotoxicity. Design and methods: In view of the well-recognized literature data demonstrating that Aβ25-35 fibrillar aggregates cause in vitro cytotoxicity to human red blood cells and apoptotic changes to SK-N-BE neuroblastoma cells in cultures (ultrastructural evidence), we tested transthyretin effects on these two experimental models. Results: Incubation of Aβ25-35 with transthyretin (at transthyretin concentrations equal to CSF physiological levels) demonstrated both inhibition of red blood cells lysis and neutralization of SK-N-BE neuroblastoma cells ultrastructural apoptotic changes. Moreover, transthyretin was shown to be able to inhibit the formation of fibrillar macroaggregates of Aβ25-35. Conclusions: The findings imply that experimental systems investigating Aβ-induced cytotoxicity consider the protective interaction of transthyretin with Aβ; an interaction to be considered also in vivo in view of the fact that transthyretin immunoreactivity has been previously demonstrated in amyloid plaques of brains from Alzheimer's disease patients.

Original languageEnglish
Pages (from-to)1112-1119
Number of pages8
JournalClinical Biochemistry
Volume38
Issue number12
DOIs
Publication statusPublished - Dec 2005

Keywords

  • Alzheimer pathogenesis
  • Amyloid-β
  • Cytotoxicity
  • Erythrocytes
  • Neuroblastoma cell cultures
  • Transthyretin

ASJC Scopus subject areas

  • Clinical Biochemistry

Fingerprint Dive into the research topics of 'Transthyretin inhibition of amyloid beta aggregation and toxicity'. Together they form a unique fingerprint.

  • Cite this