Transferrin neutralization of amyloid β 25-35 cytotoxicity

Sergio Giunta, Roberta Galeazzi, M. Beatrice Valli, Elizabeth H. Corder, Luciano Galeazzi

Research output: Contribution to journalArticle

Abstract

Fibrillar aggregates of amyloid β 25-35 (Aβ 25-35) form rapidly in vitro able to lyse human red blood cells (RBCs). Human sera, albumin, and apolipoprotein E (ApoE) each limit fibrillation and cytotoxicity. Potentially, these substances protect neurons from Aβ 1-40/42 aggregates. Transferrin (TF) is investigated in this study. The Mattson red blood cells model was employed to determine whether co-incubation of transferrin and Aβ 25-35 prevented lysis. The formation of fibrillar Aβ 25-35 in the presence of transferrin was investigated using Congo red staining and spectrophotometric studies. We found that incubation of 20 μM Aβ 25-35 with physiologic levels of transferrin prevented red blood cells lysis and the formation of macro-aggregates. These in vitro results suggest that transferrin may limit fibrillar β amyloid formation in vivo and cytotoxicity.

Original languageEnglish
Pages (from-to)129-136
Number of pages8
JournalClinica Chimica Acta
Volume350
Issue number1-2
DOIs
Publication statusPublished - Dec 2004

Fingerprint

Cytotoxicity
Transferrin
Amyloid
Blood
Erythrocytes
Cells
Congo Red
Apolipoproteins E
Serum Albumin
Neurons
Macros
Staining and Labeling
In Vitro Techniques

Keywords

  • Alzheimer pathogenesis
  • Amyloid β
  • Red blood cells
  • Transferrin

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry

Cite this

Transferrin neutralization of amyloid β 25-35 cytotoxicity. / Giunta, Sergio; Galeazzi, Roberta; Valli, M. Beatrice; Corder, Elizabeth H.; Galeazzi, Luciano.

In: Clinica Chimica Acta, Vol. 350, No. 1-2, 12.2004, p. 129-136.

Research output: Contribution to journalArticle

Giunta, Sergio ; Galeazzi, Roberta ; Valli, M. Beatrice ; Corder, Elizabeth H. ; Galeazzi, Luciano. / Transferrin neutralization of amyloid β 25-35 cytotoxicity. In: Clinica Chimica Acta. 2004 ; Vol. 350, No. 1-2. pp. 129-136.
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